目录号 | 产品详情 | 靶点 | |
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T16699 | Others E1/E2/E3 Enzyme | ||
PYZD-4409 是一种特异性 UBA1 抑制剂,IC50 为 20 μM。 PYZD-4409 在恶性细胞中诱导细胞死亡,并且对恶性细胞的细胞毒性优于对正常造血细胞的细胞毒性。 | |||
T20797 | Sigma receptor | ||
NE-100 hydrochloride (NE-100 HCl) 是选择性sigma-1 受体拮抗剂,IC50为 4.16 nM。它在体内具有抗精神病活性。它也能抑制内质网应激诱导的海马细胞死亡。 | |||
T8808L | Apoptosis Autophagy | ||
LYN-1604 2HCl 是一种有效的 UNC-51 样激酶 1 激活剂,EC50值为 18.94 nM。LYN-1604 可研究三阴性乳腺癌。 | |||
T9024 | Others PARP | ||
OUL35 (NSC-39047) 是一种选择性 PARP-10 抑制剂和小分子 ARTD10 抑制剂,其 IC50值为 329 nM。 | |||
T10268 | Others | ||
AGX51 是 DNA 结合蛋白抑制剂 (ID) 的拮抗剂。 AGX51 治疗导致泛 Id 降解、细胞周期停滞和细胞死亡。 | |||
T65013 | Others | ||
Cuprizone 是一种铜螯合剂。Cuprizone 可用于诱导小鼠精神分裂症。Cuprizone 可诱导少突胶质细胞死亡,诱导脱髓鞘反应。 | |||
T14007 | PAFR | ||
PAF-AN-1是一种新型有效的血小板激活因子受体 (PAF) 拮抗剂,参与研究过敏性死亡。 | |||
T14912 | Retinoid Receptor | ||
CD3254 是一种具有选择性和强效性的类视黄醇 X 受体 (RXR) 激动剂,可抑制伴有OGD/再氧合的神经元细胞死亡。 | |||
T16817 | Lipoxygenase COX | ||
S-2474 是 COX-2 和 5-脂氧合酶的抑制剂 ,具有抗炎活性和神经保护活性,可抑制 Abeta(25 - 35) 和 Abeta(1 - 40) 诱导的细胞死亡。 | |||
TQ0318L | KSP | ||
ARRY 520 hydrochloride 是一种驱动蛋白纺锤体蛋白 (KSP) 抑制剂。它通过凋亡诱导细胞死亡,并具有有效的抗增殖活性。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-05815 | PD-1 Protein, Canine, Recombinant (His & Avi), Biotinylated | Canine | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05260 | PD-1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-04342 | PD-1 Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05395 | PD-1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00996 | PD-1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-04898 | PD-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05079 | PD-1 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00897 | PD-1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05827 | PD-L2 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04957 | PD-L2 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04346 | PD-L2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-00253 | PD-1 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00633 | PD-1 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00250 | PD-1 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-03717 | PD-1 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPJ-01059 | CRADD Protein, Human, Recombinant | Human | E. coli | ||
Death Domain-Containing Protein CRADD (CRADD) is widely expressed in most tissues, with particularly high expression in the adult heart, testis, liver, skeletal muscle, fetal liver, and kidney. CRADD contains one CARD domain that mediates the interaction with caspase-2, and one death domain involved in the binding of RIP protein. CRADD functions as an apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. CRADD induces cell apoptosis/cell death in numerous tissues. Defects in CRADD will result in mental retardation.
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TMPY-04341 | PD-1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00233 | PD-1 Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05295 | PD-1 Protein, Cynomolgus, Recombinant (hFc & Avi), Biotinylated | Cynomolgus | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-00047 | Dengue virus DENV-2 (Strain New Guinea C) Capsid protein/DENV-C Protein (His) | DENV | E. coli | ||
Dengue virus DENV-2 (Strain New Guinea C) Capsid protein/DENV-C Protein (His) is expressed in E. coli with His tag. The predicted molecular weight is 14 kDa. Accession number: W0GCK5
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TMPY-03738 | PD-L2 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04223 | PD-L2 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04282 | Fas/CD95 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
CD95 (APO-1/Fas) is an important inducer of the extrinsic apoptosis signaling pathway and therapy induced apoptosis of many tumor cells has been linked to the activity of CD95. is a prototype death receptor characterized by the presence of an 80 amino acid death domain in its cytoplasmic tail. This domain is essential for the recruitment of a number of signaling components upon activation by either agonistic anti-CD95 antibodies or cognate CD95 ligand that initiate apoptosis. The complex of proteins that forms upon triggering of CD95 is called the death-inducting signaling complex (DISC). The DISC consists of an adaptor protein and initiator caspases and is essential for induction of apoptosis. CD95 is also crucial for the negative selection of B cells within the germinal center (GC). Impairment of CD95-mediated apoptosis results in defective affinity maturation and the persistence of autoreactive B-cell clones. Changes in the expression of CD95 and/or its ligand CD95L are frequently found in human cancer. The downregulation or mutation of CD95 has been proposed as a mechanism by which cancer cells avoid destruction by the immune system through reduced apoptosis sensitivity. Thus, CD95 has therefore been viewed as a tumor suppressor. CD95 has been reported to be involved in the activation of NF-kappaB, MAPK3/ERK1, MAPK8/JNK, and the alternate pathways for CTL-mediated cytotoxicity. Accordingly, this protein is implicated in the pathogenesis of various malignancies and diseases of the immune system. The CD95/CD95L system was implicated in the etiology of inflammatory bowel disease (IBD) based, primarily, on the finding that CD95 is highly expressed in the intestinal epithelial cells and that epithelial apoptosis is increased in IBD.
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TMPY-03834 | Fas/CD95 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
CD95 (APO-1/Fas) is an important inducer of the extrinsic apoptosis signaling pathway and therapy induced apoptosis of many tumor cells has been linked to the activity of CD95. is a prototype death receptor characterized by the presence of an 80 amino acid death domain in its cytoplasmic tail. This domain is essential for the recruitment of a number of signaling components upon activation by either agonistic anti-CD95 antibodies or cognate CD95 ligand that initiate apoptosis. The complex of proteins that forms upon triggering of CD95 is called the death-inducting signaling complex (DISC). The DISC consists of an adaptor protein and initiator caspases and is essential for induction of apoptosis. CD95 is also crucial for the negative selection of B cells within the germinal center (GC). Impairment of CD95-mediated apoptosis results in defective affinity maturation and the persistence of autoreactive B-cell clones. Changes in the expression of CD95 and/or its ligand CD95L are frequently found in human cancer. The downregulation or mutation of CD95 has been proposed as a mechanism by which cancer cells avoid destruction by the immune system through reduced apoptosis sensitivity. Thus, CD95 has therefore been viewed as a tumor suppressor. CD95 has been reported to be involved in the activation of NF-kappaB, MAPK3/ERK1, MAPK8/JNK, and the alternate pathways for CTL-mediated cytotoxicity. Accordingly, this protein is implicated in the pathogenesis of various malignancies and diseases of the immune system. The CD95/CD95L system was implicated in the etiology of inflammatory bowel disease (IBD) based, primarily, on the finding that CD95 is highly expressed in the intestinal epithelial cells and that epithelial apoptosis is increased in IBD.
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TMPJ-00137 | APRIL/TNFSF13 Protein, Human, Recombinant (Flag & His) | Human | Human Cells | ||
APRIL (a proliferation-inducing ligand), also known as TNFSF13, TALL2, TRDL1, and CD256, is a member of the TNF ligand superfamily. It is synthesized as a 32 kDa proprotein which is cleaved by furin in the Golgi to release the active 17 kDa soluble molecule. Secreted human APRIL, which consists almost entirely of a single TNF homology domain, shares 85% amino acid sequence identity with mouse and rat APRIL. Both APRIL and its close relative BAFF bind and signal through the TNF superfamily receptors TACI and BCMA, while BAFF additionally functions through BAFF R. APRIL binds to heparan sulfate proteoglycans (HSPGs) independently of its binding to TACI and BCMA. APRIL can form bioactive heterotrimers with BAFF, and these circulate in the serum of patients with rheumatic immune disorders. APRIL enhances the proliferation and survival of plasma cells and also promotes T cell-dependent humoral responses. APRIL levels are elevated in the serum during coronary artery disease, and it is also elevated in many cancers primarily due to expression by tumor-infiltratin neutrophils.
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TMPY-00632 | Fas/CD95 Protein, Cynomolgus, Recombinant | Cynomolgus | HEK293 | ||
CD95 (APO-1/Fas) is an important inducer of the extrinsic apoptosis signaling pathway and therapy induced apoptosis of many tumor cells has been linked to the activity of CD95. is a prototype death receptor characterized by the presence of an 80 amino acid death domain in its cytoplasmic tail. This domain is essential for the recruitment of a number of signaling components upon activation by either agonistic anti-CD95 antibodies or cognate CD95 ligand that initiate apoptosis. The complex of proteins that forms upon triggering of CD95 is called the death-inducting signaling complex (DISC). The DISC consists of an adaptor protein and initiator caspases and is essential for induction of apoptosis. CD95 is also crucial for the negative selection of B cells within the germinal center (GC). Impairment of CD95-mediated apoptosis results in defective affinity maturation and the persistence of autoreactive B-cell clones. Changes in the expression of CD95 and/or its ligand CD95L are frequently found in human cancer. The downregulation or mutation of CD95 has been proposed as a mechanism by which cancer cells avoid destruction by the immune system through reduced apoptosis sensitivity. Thus, CD95 has therefore been viewed as a tumor suppressor. CD95 has been reported to be involved in the activation of NF-kappaB, MAPK3/ERK1, MAPK8/JNK, and the alternate pathways for CTL-mediated cytotoxicity. Accordingly, this protein is implicated in the pathogenesis of various malignancies and diseases of the immune system. The CD95/CD95L system was implicated in the etiology of inflammatory bowel disease (IBD) based, primarily, on the finding that CD95 is highly expressed in the intestinal epithelial cells and that epithelial apoptosis is increased in IBD.
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TMPY-02057 | Fas/CD95 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
CD95 (APO-1/Fas) is an important inducer of the extrinsic apoptosis signaling pathway and therapy induced apoptosis of many tumor cells has been linked to the activity of CD95. is a prototype death receptor characterized by the presence of an 80 amino acid death domain in its cytoplasmic tail. This domain is essential for the recruitment of a number of signaling components upon activation by either agonistic anti-CD95 antibodies or cognate CD95 ligand that initiate apoptosis. The complex of proteins that forms upon triggering of CD95 is called the death-inducting signaling complex (DISC). The DISC consists of an adaptor protein and initiator caspases and is essential for induction of apoptosis. CD95 is also crucial for the negative selection of B cells within the germinal center (GC). Impairment of CD95-mediated apoptosis results in defective affinity maturation and the persistence of autoreactive B-cell clones. Changes in the expression of CD95 and/or its ligand CD95L are frequently found in human cancer. The downregulation or mutation of CD95 has been proposed as a mechanism by which cancer cells avoid destruction by the immune system through reduced apoptosis sensitivity. Thus, CD95 has therefore been viewed as a tumor suppressor. CD95 has been reported to be involved in the activation of NF-kappaB, MAPK3/ERK1, MAPK8/JNK, and the alternate pathways for CTL-mediated cytotoxicity. Accordingly, this protein is implicated in the pathogenesis of various malignancies and diseases of the immune system. The CD95/CD95L system was implicated in the etiology of inflammatory bowel disease (IBD) based, primarily, on the finding that CD95 is highly expressed in the intestinal epithelial cells and that epithelial apoptosis is increased in IBD.
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TMPY-06819 | PD-L2 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-03404 | PD-L2 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-06838 | PD-L2 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-02027 | BID Protein, Human, Recombinant | Human | E. coli | ||
The BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family, which contains only the BH3 domain, and is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. Recent studies further indicate that Bid may be more than just a killer molecule, it could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint. BID is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. BID is activated by Caspase 8 in response to Fas/TNF-R1 death receptor activation. Activated BID is translocated to mitochondria and induces cytochrome c release, which in turn activates downstream caspases. BID action has been proposed to involve the mitochondrial re-location of its truncated form, tBid, to facilitate the release of apoptogenic proteins like cytochrome c.
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TMPY-04225 | PD-L2 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04385 | ZIP Kinase/DAPK3 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Death-associated protein kinase 3, also known as DAP kinase 3, ZIP-kinase, DAPK3 and ZIPK, is a nucleus and cytoplasm protein which belongs to theprotein kinase superfamily, CAMK Ser/Thr protein kinase family and DAP kinase subfamily. DAPK3 / ZIPK contains oneprotein kinase domain. It is a serine/threonine kinase which acts as a positive regulator of apoptosis. It phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. DAPK3 / ZIPK is a homodimer or forms heterodimers with ATF4. Both interactions require an intact leucine zipper domain and oligomerization is required for full enzymatic activity. It also binds to DAXX and PAWR, possibly in a ternary complex which plays a role in caspase activation. DAPK3 / ZIPK regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. It is involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection.
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TMPY-04417 | DAPK1 Protein, Human, Recombinant (aa 1-363, His & GST) | Human | Baculovirus-Insect Cells | ||
Death-associated protein kinase 1, also known as DAP kinase 1, DAPK1 and DAPK, is a cytoplasm protein which belongs to theprotein kinase superfamily, CAMK Ser / Thr protein kinase family and DAP kinase subfamily. DAPK1 contains tenANK repeats, onedeath domain and oneprotein kinase domain. DAPK1 is a calcium / calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis. DAPK1 gene is a candidate tumor suppressor (TSG) and the abnormal methylation of DAPK1 gene has been found in many carcinomas. DAPK1 over-expression can induce cell apoptosis and inhibit tumor cell metastasis. DAPK1 gene over-expression could suppress PGCl3 cells malignant phenotype, inhibit PGCl3 cells growth, invasive, migration and adhesion ability, upregulate p53 gene and downregulate bcl-2 gene. Loss of activity of death-associated protein kinase 1 ( DAPK1 ) may be an independent factor affecting survival of non-small cell lung cancer patients. DAPK1 promoter methylation might play a significant role in the progression of chronic myeloid leukemia ( CML ).
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TMPY-04967 | PD-1 Protein, Mouse, Recombinant (His), Biotinylated | Mouse | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-02065 | BID Protein, Mouse, Recombinant (His & GST) | Mouse | E. coli | ||
The BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family, which contains only the BH3 domain, and is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. Recent studies further indicate that Bid may be more than just a killer molecule, it could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint. BID is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. BID is activated by Caspase 8 in response to Fas/TNF-R1 death receptor activation. Activated BID is translocated to mitochondria and induces cytochrome c release, which in turn activates downstream caspases. BID action has been proposed to involve the mitochondrial re-location of its truncated form, tBid, to facilitate the release of apoptogenic proteins like cytochrome c.
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TMPJ-00181 | PD-1 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Human Cells | ||
Programmed cell death protein 1(PDCD1) is a single-pass type I membrane protein and contains 1 Ig-like V-type domain. PD-1 is a member of the extended CD28/CTLA-4 family of T cell regulators. PDCD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PDCD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PDCD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.
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TMPY-03317 | DcR2/TRAIL R4 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Tumor necrosis factor receptor superfamily member 10D (TNFRSF10D), also known as TNF-related apoptosis-inducing ligand receptor 4 (TRAIL R4), CD264, and Decoy receptor 2, is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplamic death domain. This receptor does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis. TRAIL R4/CD264/TNFRSF10D is widely expressed, in particular in fetal kidney, lung and liver, and in adult testis and liver. TRAIL R4/CD264/TNFRSF10D is also expressed in peripheral blood leukocytes, colon and small intestine, ovary, prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart. The signaling capacity of TRAIL R4 is similar to that of TRAIL R1 and TRAIL R2 with respect to NF-κB activation, but differs in its inability to induce apoptosis. TRAIL R4 retains a C-terminal element containing one third of a consensus death domain motif. Transient overexpression of TRAIL R4 in cells normally sensitive to TRAIL-mediated killing confers complete protection, suggesting that one function of TRAIL R4 may be inhibition of TRAIL cytotoxicity.
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TMPJ-00183 | PD-L1 Protein, Human, Recombinant (Flag) | Human | Human Cells | ||
CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.
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TMPJ-00182 | PD-L1 Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | Human Cells | ||
CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.
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TMPY-05282 | PD-L2 Protein, Mouse, Recombinant (His), Biotinylated | Mouse | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-02352 | PD-L2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-02436 | PD-L2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Programmed death ligand 2 (PD-L2), also referred to as B7-DC and CD273, is a member of the B7 family of proteins including B7-1, B7-2, B7-H2, B7-H1 (PD-L1), and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain, a transmembrane region, and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells, placental endothelium and medullary thymic epithelial cells, and can be induced by LPS in B cells, INF-γ in monocytes, or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1, member of the CD28/CTLA4 family expressed on activated lymphoid cells, and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-03318 | DcR2/TRAIL R4 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Tumor necrosis factor receptor superfamily member 10D (TNFRSF10D), also known as TNF-related apoptosis-inducing ligand receptor 4 (TRAIL R4), CD264, and Decoy receptor 2, is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplamic death domain. This receptor does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis. TRAIL R4/CD264/TNFRSF10D is widely expressed, in particular in fetal kidney, lung and liver, and in adult testis and liver. TRAIL R4/CD264/TNFRSF10D is also expressed in peripheral blood leukocytes, colon and small intestine, ovary, prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart. The signaling capacity of TRAIL R4 is similar to that of TRAIL R1 and TRAIL R2 with respect to NF-κB activation, but differs in its inability to induce apoptosis. TRAIL R4 retains a C-terminal element containing one third of a consensus death domain motif. Transient overexpression of TRAIL R4 in cells normally sensitive to TRAIL-mediated killing confers complete protection, suggesting that one function of TRAIL R4 may be inhibition of TRAIL cytotoxicity.
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TMPY-02213 | RAIDD Protein, Human, Recombinant (His) | Human | E. coli | ||
Death domain-containing protein CRADD, also known as Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CRADD and RAIDD, is a protein which is constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney. CRADD / RAIDD contains oneCARD domain and onedeath domain. CRADD / RAIDD contains a death domain involved in the binding of RIP protein. The CARD domain mediates the interaction with caspase-2. FADD / MORT1 is a death domain (DD)-containing adaptor / signaling molecule that interacts with the intracellular DD of FAS / APO-I ( CD95 ) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 ( Mch5 / MACH / FLICE). CRADD / RAIDD has a dual-domain structure similar to that of FADD. CRADD / RAIDD has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD / RAIDD could play a role in regulating apoptosis in mammalian cells. CRADD / RAIDD is a apoptotic adaptor molecule specific for caspase-2 and FASL / TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD / RAIDD recruits caspase-2 to the TNFR-1 signalling complex.
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TMPY-06682 | PD-1 Protein, Human, Recombinant (Asp26-Pro39 deletion, His) | Human | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPY-05619 | PD-1 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Programmed cell death 1, also known as PDCD1, is a type I transmembrane glycoprotein, and is an immunoreceptor belonging to the CD28/CTLA-4 family negatively regulates antigen receptor signaling by recruiting protein tyrosine phosphatase, SHP-2 upon interacting with either of two ligands, PD-L1 or PD-L2. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. PD1 has been suggested to be involved in lymphocyte clonal selection and peripheral tolerance, and thus contributes to the prevention of autoimmune diseases. Furthermore, PD1 is shown to be a regulator of virus-specific CD8+ T cell survival in HIV infection. As a cell surface molecule, PDCD1 regulates the adaptive immune response. Engagement of PD-1 by its ligands PD-L1 or PD-L2 transduces a signal that inhibits T-cell proliferation, cytokine production, and cytolytic function.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Blockade: Blocking AntibodiImmune Checkpoint Blockade: PD1 / PDCD1 / CD2Immune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyPD1 / PDCD1 / CD279 Immune CheckpointPD1 / PDCD1 / CD279 Immune Checkpoint AntibodPD1 / PDCD1 / CD279 Immune Checkpoint ProteinTargeted Therapy
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TMPJ-00718 | AIF Protein, Human, Recombinant (His) | Human | E. coli | ||
Apoptosis-Inducing Factor 1, Mitochondrial (AIFM1) is a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. During apoptosis, it is translocated from the mitochondria to the nucleus to function as a proapoptotic factor in a caspase-independent pathway, while in normal mitochondria, it functions as an antiapoptotic factor via its oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces parthanatos i.e., caspase-independent fragmentation of chromosomal DNA. AIFM1 interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. It binds to DNA in a sequence-independent manner and plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells.
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TMPJ-00246 | TRAIL R2/DR5/TNFRSF10B Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Mouse tumor necrosis factor receptor superfamily member 10B (TNFRSF10B) is a member of the TNFR family which contains 1 death domain and 3 TNFR-Cys repeats. TNFRSF10B exhibits high structural and functional homology to TRAIL-R1 (DR-4). TNFRSF10B is highly expressed in heart, lung, lymphocytes, spleen and kidney. In addition, it is regulated by the tumor suppressor p53. TNFRSF10B is the receptor for the cytotoxic ligand TNFSF10/TRAIL. It promotes the activation of NF-kappa-B and is essential for ER stress-induced apoptosis. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis.
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TMPJ-00245 | TRAIL R2/DR5/TNFRSF10B Protein, Mouse, Recombinant (Avi & His), Biotinylated | Mouse | Human Cells | ||
Mouse tumor necrosis factor receptor superfamily member 10B (TNFRSF10B) is a member of the TNFR family which contains 1 death domain and 3 TNFR-Cys repeats. TNFRSF10B exhibits high structural and functional homology to TRAIL-R1 (DR-4). TNFRSF10B is highly expressed in heart, lung, lymphocytes, spleen and kidney. In addition, it is regulated by the tumor suppressor p53. TNFRSF10B is the receptor for the cytotoxic ligand TNFSF10/TRAIL. It promotes the activation of NF-kappa-B and is essential for ER stress-induced apoptosis. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis.
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