目录号 | 产品详情 | 靶点 | |
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T10276 | Akt | ||
AKT Kinase Inhibitor 是一种具有抗肿瘤活性的 Akt 抑制剂,以剂量依赖的方式选择性抑制细胞增殖。 | |||
T25017 | Akt | ||
AKT-I-1 是一种特异性和可逆的 Akt1 抑制剂。 | |||
T23695 | Akt | ||
Akt-I-1,2 是 Akt1 和 Akt2 的选择性抑制剂。 | |||
T36310 | Akt | ||
AKT-IN-6 (INCB-047775)对ATK 有抑制作用。Akt 是对生长因子、细胞因子和其他细胞刺激的细胞信号传导的重要组成部分。Akt 的异常激活与2型糖尿病和癌症的发生密切相关。 | |||
T3346 | Apoptosis Akt | ||
AKT inhibitor VIII (AKTi-1/2) 是一种细胞渗透的喹喔啉化合物,可逆的选择性抑制Akt1、Akt2和Akt3的活性,IC50值分别为 58 nM、210 nM 和 2119 nM。 | |||
T10276L | Akt | ||
AKT Kinase Inhibitor HCl 是一种 Akt 抑制剂,具有抗肿瘤活性。 | |||
T9393 | Akt | ||
(E)-Akt inhibitor-IV ((E)-AKTIV) 是PI3K-Akt 抑制剂,表现出明显的细胞毒性。 | |||
T5508 | Akt | ||
PF-AKT400 (AKT protein kinase inhibitor) 是 ATP 竞争性的、选择性的 Akt 抑制剂,对 PKBα(IC50=0.5 nM) 的选择性比 PKA(IC50=450 nM) 高 900 倍。 | |||
T4489 | Akt | ||
AKT-IN-1 (AZD-26) 是一种变构的 AKT 抑制剂,其 IC50=1.042 μM。 | |||
TP2175 | Others | ||
substrate for Akt/PKB |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04552 | AKT1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
v-akt murine thymoma viral oncogene homolog 1 (AKT1), or protein kinase B-alpha (PKB-ALPHA) is a serine-threonine protein kinase, belonging to the Protein Kinase Superfamily. AKT1 is a major mediator of the responses to insulin, insulin-like growth factor 1 (IGF1), and glucose. AKT1 also plays a key role in the regulation of both muscle cell hypertrophy and atrophy. AKT1 activity is required for physiologic cardiac growth in response to IGF1 stimulation or exercise training. In contrast, AKT1 activity was found to antagonize pathologic cardiac growth that occurs in response to endothelin 1 stimulation or pressure overload. AKT1 selectively promotes physiological cardiac growth while AKT2 selectively promotes insulin-stimulated cardiac glucose metabolism. AKT1 deletion prevented tumor initiation as well as tumor progression, coincident with decreased Akt signaling in tumor tissues. AKT1 is the primary Akt isoform activated by mutant K-ras in lung tumors, and that AKT3 may oppose AKT1 in lung tumorigenesis and lung tumor progression. A number of separate studies have implicated AKT1 as an inhibitor of breast epithelial cell motility and invasion. AKT1 may have a dual role in tumorigenesis, acting not only pro-oncogenically by suppressing apoptosis but also anti-oncogenically by suppressing invasion and metastasis.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04574 | AKT3 Protein, Mouse, Recombinant (aa 106-479, His & GST) | Mouse | Baculovirus-Insect Cells | ||
v-akt murine thymoma viral oncogene homolog 3 (AKT3), also known as PKB-GAMMA, with AKT1/PKBalpha, AKT2/PKBbeta, are the memerbers of Akt kinase family, share extensive structural similarity and perform common as well as unique functions within cells. The Akt signaling cascade initiates at the cell surface when growth factors or other extracellular stimuli activate phosphoinositide 3-kinase (PI3K). AKT3 was discovered to be the predominant isoform activated in sporadic melanomas. Levels of activity increased during melanoma progression with metastatic melanomas having the highest activity. Although mechanisms of AKT3 activation remain to be fully characterized, overexpression of AKT3 and decreased PTEN activity play important roles in this process. Targeted reduction of AKT3 activity decreased survival of melanoma tumor cells leading to inhibition of tumor development, which may be therapeutically effective for shrinking tumors in melanoma patients. AKT2 and AKT3 play an important role in the viability of human malignant glioma cells. Targeting AKT2 and AKT3 may hold promise for the treatment of patients with gliomas.
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TMPY-04387 | AKT2 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
AKT (AK mouse plus Transforming or Thymoma) is a frequent oncogene expressed in most tissues which includes three isoforms AKT1, AKT2, and AKT3. Hyperactivation of AKT signaling is a central key in many human cancer progressions, through modulating angiogenesis, tumor growth, and cell migration, invasion, metastasis, and chemoresistance. Among all three isoforms, AKT2 is most related to cancer cell invasion, metastasis, and survival. Amplification and overexpression of AKT2 have been shown in many cancers. Accumulating evidence shows the potential role of different miRNA involvements in cancer progression by activating or suppressing AKT2 expression. The AKT2/NAB1/SPK1 pathway is a novel regulating factor of macrophage migration and cardiac remodeling after myocardial infarction. The novel mechanism of the AKT2-PKM2-STAT3/NF-kappaB axis in the regulation of ovarian cancer progression, that both AKT2 and PKM2 may be potential targets for the treatment of ovarian cancer. AKT1 and AKT2, the AKT isoforms that are highly expressed in skeletal muscle, have distinct and overlapping functions, with AKT2 more important for insulin-stimulated glucose metabolism. In adipocytes, AKT2 versus AKT1 has greater susceptibility for insulin-mediated redistribution from cytosolic to membrane localization, and insulin also causes subcellular redistribution of AKT Substrate of 160 kDa (AS160), an AKT2 substrate and crucial mediator of insulin-stimulated glucose transport.
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TMPY-04446 | AKT3 Protein, Mouse, Recombinant (aa 106-479) | Mouse | Baculovirus-Insect Cells | ||
v-akt murine thymoma viral oncogene homolog 3 (AKT3), also known as PKB-GAMMA, with AKT1/PKBalpha, AKT2/PKBbeta, are the memerbers of Akt kinase family, share extensive structural similarity and perform common as well as unique functions within cells. The Akt signaling cascade initiates at the cell surface when growth factors or other extracellular stimuli activate phosphoinositide 3-kinase (PI3K). AKT3 was discovered to be the predominant isoform activated in sporadic melanomas. Levels of activity increased during melanoma progression with metastatic melanomas having the highest activity. Although mechanisms of AKT3 activation remain to be fully characterized, overexpression of AKT3 and decreased PTEN activity play important roles in this process. Targeted reduction of AKT3 activity decreased survival of melanoma tumor cells leading to inhibition of tumor development, which may be therapeutically effective for shrinking tumors in melanoma patients. AKT2 and AKT3 play an important role in the viability of human malignant glioma cells. Targeting AKT2 and AKT3 may hold promise for the treatment of patients with gliomas.
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TMPY-04553 | AKT3 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
v-akt murine thymoma viral oncogene homolog 3 (AKT3), also known as PKB-GAMMA, with AKT1/PKBalpha, AKT2/PKBbeta, are the memerbers of Akt kinase family, share extensive structural similarity and perform common as well as unique functions within cells. The Akt signaling cascade initiates at the cell surface when growth factors or other extracellular stimuli activate phosphoinositide 3-kinase (PI3K). AKT3 was discovered to be the predominant isoform activated in sporadic melanomas. Levels of activity increased during melanoma progression with metastatic melanomas having the highest activity. Although mechanisms of AKT3 activation remain to be fully characterized, overexpression of AKT3 and decreased PTEN activity play important roles in this process. Targeted reduction of AKT3 activity decreased survival of melanoma tumor cells leading to inhibition of tumor development, which may be therapeutically effective for shrinking tumors in melanoma patients. AKT2 and AKT3 play an important role in the viability of human malignant glioma cells. Targeting AKT2 and AKT3 may hold promise for the treatment of patients with gliomas.
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TMPY-02333 | ULBP-2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
NKG2D ligand 2, also known as N2DL-2, NKG2DL2, ALCAN-alpha, Retinoic acid early transcript 1H, UL16-binding protein 2, ULBP2 and N2DL2, is cell membrane protein that belongs to the MHC class I family. ULBP2 / N2DL-2 is expressed in various types of cancer cell lines and in the fetus, but not in normal tissues. ULBP2 / N2DL-2 is a ligand for the NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway.
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TMPY-05592 | ULBP-2 Protein, Human, Recombinant(aa 1-217, His&AVI),Biotinylated | Human | HEK293 | ||
NKG2D ligand 2, also known as N2DL-2, NKG2DL2, ALCAN-alpha, Retinoic acid early transcript 1H, UL16-binding protein 2, ULBP2 and N2DL2, is cell membrane protein that belongs to the MHC class I family. ULBP2 / N2DL-2 is expressed in various types of cancer cell lines and in the fetus, but not in normal tissues. ULBP2 / N2DL-2 is a ligand for the NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway.
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TMPJ-00059 | IL-7 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Human Interleukin 7 (IL-7) is a potent lymphoid cell growth factor stimulating the proliferation of lymphoid progenitors. IL7 can associate with the hepatocyte growth factor (HGF) to form a hybrid cytokine that functions as a pre-pro-B cell growth-stimulating factor. Human IL7 cDNA encodes a 177 amino acid precursor protein containing a 25 amino acid signal peptide and a 152 amino acid mature protein. Human and mouse IL7 share 65% sequence identity in the mature region and both exhibit cross-species activity. IL-7 signals via IL-7 receptor (IL7R) activating multiple pathways including JaK/STAT and PI3K/AKT, which regulate lymphocyte survival, glucose uptake, proliferation, and differentiation. IL-7 is also associated with cytoplasmic IL2-R gamma for signal transduction.
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TMPY-01413 | Cripto Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cripto/TDGF1 is a member of the epidermal growth factor (EGF)- Cripto, Frl-1, and Cryptic (CFC) family. EGF-CFC family member proteins share a variant EGF-like motif, a conserved cysteine-rich domain, and a C-terminal hydrophobic region. Before gastrulation, Cripto is asymmetrically expressed in a proximal–distal gradient in the epiblast, and subsequently is expressed in the primitive streak and newly formed embryonic mesoderm. These proteins play key roles in intercellular signaling pathways during vertebrate embryogenesis. Mutations in Cripto/TDGF1 can cause autosomal visceral heterotaxy. Cripto/TDGF1 is involved in left-right asymmetric morphogenesis during organ development. Cripto signalling is essential for the conversion of a proximal–distal asymmetry into an orthogonal anterior–posterior axis. The mechanism of inhibitory effects of the Cripto includes both cancer cell apoptosis, activation of c-Jun-NH(2)-terminal kinase and p38 kinase signaling pathways and blocking of Akt phosphorylation. Thus, Cripto is a unique target, and Immunohistochemistry to Cripto could be of therapeutic value for human cancers.
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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-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-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-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-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-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-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-05636 | G-CSF Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Granulocyte-colony stimulating factor (G-CSF) is a growth factor and an essential cytokine belonging to the CSF family of hormone-like glycoproteins. It is produced by numerous cell types including immune and endothelial cells. G-CSF binding to its receptor G-CSF-R which belongs to the cytokine receptor type I family depends on the interaction of alpha-helical motifs of the former and two fibronectin type III as well as an immunoglobulin-like domain of the latter. Recent animal studies have also revealed that G-CSF activates multiple signaling pathways, such as Akt and also the Janus family kinase-2 and signal transducer and activation of transcription-3 (Jak2-STAT3) pathway, thereby promoting survival, proliferation, differentiation and mobilisation of haematopoietic stem and progenitor cells. G-CSF is a cytokine that have been demonstrated to improve cardiac function and perfusion in myocardial infarction. And it was initially evaluated as a stem cell mobilizer and erythropoietin as a cytoprotective agent. G-CSF prevents left ventricular remodeling after myocardial infarction by decreasing cardiomyocyte death and by increasing the number of blood vessels, suggesting the importance of direct actions of G-CSF on the myocardium rather than through mobilization and differentiation of stem cells. Accordingly, recombinant human (rh)G-CSF has been extensively used in clinical haematology and oncology to enable bone marrow transplantation or to treat chemotherapy-associated neutropenia. In preclinical study, G-CSF improved cardiac function and perfusion by angiomyogenesis and protection of cardiomyocytes in myocardial infarction.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04829 | G-CSF Protein, Human, Recombinant | Human | HEK293 | ||
Granulocyte-colony stimulating factor (G-CSF) is a growth factor and an essential cytokine belonging to the CSF family of hormone-like glycoproteins. It is produced by numerous cell types including immune and endothelial cells. G-CSF binding to its receptor G-CSF-R which belongs to the cytokine receptor type I family depends on the interaction of alpha-helical motifs of the former and two fibronectin type III as well as an immunoglobulin-like domain of the latter. Recent animal studies have also revealed that G-CSF activates multiple signaling pathways, such as Akt and also the Janus family kinase-2 and signal transducer and activation of transcription-3 (Jak2-STAT3) pathway, thereby promoting survival, proliferation, differentiation and mobilisation of haematopoietic stem and progenitor cells. G-CSF is a cytokine that have been demonstrated to improve cardiac function and perfusion in myocardial infarction. And it was initially evaluated as a stem cell mobilizer and erythropoietin as a cytoprotective agent. G-CSF prevents left ventricular remodeling after myocardial infarction by decreasing cardiomyocyte death and by increasing the number of blood vessels, suggesting the importance of direct actions of G-CSF on the myocardium rather than through mobilization and differentiation of stem cells. Accordingly, recombinant human (rh)G-CSF has been extensively used in clinical haematology and oncology to enable bone marrow transplantation or to treat chemotherapy-associated neutropenia. In preclinical study, G-CSF improved cardiac function and perfusion by angiomyogenesis and protection of cardiomyocytes in myocardial infarction.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-01348 | FSHR Protein, Human, Recombinant (His) | Human | HEK293 | ||
G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.
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TMPY-02518 | TCL1A Protein, Human, Recombinant (His) | Human | E. coli | ||
T-cell leukemia/lymphoma protein 1A (abbreviated for TCL1A) is a member of the TCL1 family. TCL1 protooncogene is expressed in CD3-CD4-CD8-precursor T cells and is extinguished at the CD4+CD8+stage of thymocyte development. In B cells, TCL1 is first expressed in pro-B cells and remains high in naive mantle zone B cells of peripheral lymphoid tissues. The TCL1 protooncogene is overexpressed in many mature B cell lymphomas, especially from AIDS patients. It has been demonstrated that TCL1 is a powerful oncogene that, when overexpressed in both B and T cells, predominantly yields mature B cell lymphomas. All TCL1 isoforms bind to the Akt pleckstrin homology domain. Both in vitro and in vivo TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. In vivo, TCL1 stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. It has been shown that TCL1 is a novel Akt kinase coactivator, which promotes Akt-induced cell survival and proliferation.
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TMPH-01347 | FSHR Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.
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TMPH-02496 | Adipolin Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
Insulin-sensitizing adipocyte-secreted protein (adipokine) that regulates glucose metabolism in liver and adipose tissue. Promotes glucose uptake in adipocytes and suppresses de novo glucose production in hepatocytes via the PI3K-Akt signaling pathway. Administration lead to reduction of blood glucose. Able to attenuate inflammation in fat tissue.; Acts by activating the Akt signaling in hepatocytes and adipocytes. Not able to increase insulin-stimulated glucose uptake in adipocytes.; Acts by activating the MAP kinase. Increases insulin-stimulated glucose uptake in adipocytes.
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TMPH-02497 | Adipolin Protein, Mouse, Recombinant (His) | Mouse | Baculovirus | ||
Insulin-sensitizing adipocyte-secreted protein (adipokine) that regulates glucose metabolism in liver and adipose tissue. Promotes glucose uptake in adipocytes and suppresses de novo glucose production in hepatocytes via the PI3K-Akt signaling pathway. Administration lead to reduction of blood glucose. Able to attenuate inflammation in fat tissue.; Acts by activating the Akt signaling in hepatocytes and adipocytes. Not able to increase insulin-stimulated glucose uptake in adipocytes.; Acts by activating the MAP kinase. Increases insulin-stimulated glucose uptake in adipocytes.
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TMPK-00136 | ULBP-2 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway, mediating natural killer cell cytotoxicity.
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TMPK-01263 | B7-H7 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
B7-H7, also known as HHLA2 (HERV-H LTR-associating 2), is a member of the B7 family of immune regulatory proteins.Through interaction with TMIGD2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade.
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TMPK-00723 | RANK/TNFRSF11A Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
TNFRSF11A, also known as receptor activator of NF-κB (RANK), activates several signaling pathways, such as NF-κB, JNK, ERK, p38α, and Akt/PKB. RANK/TNFRSF11A is a novel and frequent target for de novo methylation in gliomas, which affects apoptotic activity and focus formation thereby contributing to the molecular pathogenesis of gliomas.
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TMPK-00351 | RANK/TNFRSF11A Protein, Human, Recombinant (aa 30-212, hFc) | Human | HEK293 | ||
TNFRSF11A, also known as receptor activator of NF-κB (RANK), activates several signaling pathways, such as NF-κB, JNK, ERK, p38α, and Akt/PKB. RANK/TNFRSF11A is a novel and frequent target for de novo methylation in gliomas, which affects apoptotic activity and focus formation thereby contributing to the molecular pathogenesis of gliomas.
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TMPH-01230 | DIP2A Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Catalyzes the de novo synthesis of acetyl-CoA in vitro. Promotes acetylation of CTTN, possibly by providing the acetyl donor, ensuring correct dendritic spine morphology and synaptic transmission. Binds to follistatin-related protein FSTL1 and may act as a cell surface receptor for FSTL1, contributing to AKT activation and subsequent FSTL1-induced survival and function of endothelial cells and cardiac myocytes.
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TMPH-00001 | CD133/PROM1 Protein-VLP, Human, Recombinant (His) | Human | HEK293 | ||
May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner.
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TMPH-01231 | DIP2A Protein, Human, Recombinant (His) | Human | Baculovirus | ||
Catalyzes the de novo synthesis of acetyl-CoA in vitro. Promotes acetylation of CTTN, possibly by providing the acetyl donor, ensuring correct dendritic spine morphology and synaptic transmission. Binds to follistatin-related protein FSTL1 and may act as a cell surface receptor for FSTL1, contributing to AKT activation and subsequent FSTL1-induced survival and function of endothelial cells and cardiac myocytes.
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TMPK-00926 | Noggin/NOG Protein, Mouse, Recombinant (His & Flag) | Mouse | HEK293 | ||
Noggin is an antagonist of bone morphogenetic proteins (BMP), being indispensable for certain developmental events.Noggin expression positively correlated with EGFR expression in both GC cell line models and The Cancer Genome Atlas human GC cohort. Targeting EGFR and its downstream pathways diminished cell proliferation which was promoted by Noggin. Noggin promotes the proliferation of GC cells by upregulating EGFR and enhancing a vicious circle formed by β‑catenin, EGFR, ERK and Akt.
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TMPH-01559 | IL-26 Protein, Human, Recombinant (His) | Human | Yeast | ||
May play a role in local mechanisms of mucosal immunity and seems to have a proinflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin.
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TMPK-00732 | WISP1/CCN4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The interplay between glioma stem cells (GSCs) and the tumor microenvironment plays crucial roles in promoting malignant growth of glioblastoma (GBM), the most lethal brain tumor. WISP1 is preferentially expressed and secreted by GSCs. Silencing WISP1 markedly disrupts GSC maintenance, reduces tumor-supportive TAMs (M2), and potently inhibits GBM growth. WISP1 signals through Integrin α6β1-Akt to maintain GSCs by an autocrine mechanism and M2 TAMs through a paracrine manner.
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TMPH-02842 | CD133/PROM1 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner.
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TMPH-01560 | IL-26 Protein, Human, Recombinant (His & Trx) | Human | E. coli | ||
May play a role in local mechanisms of mucosal immunity and seems to have a proinflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin.
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TMPK-00925 | Noggin/NOG Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Noggin is an antagonist of bone morphogenetic proteins (BMP), being indispensable for certain developmental events.Noggin expression positively correlated with EGFR expression in both GC cell line models and The Cancer Genome Atlas human GC cohort. Targeting EGFR and its downstream pathways diminished cell proliferation which was promoted by Noggin. Noggin promotes the proliferation of GC cells by upregulating EGFR and enhancing a vicious circle formed by β‑catenin, EGFR, ERK and Akt.
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TMPK-01034 | SEMA4B Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Semaphorin 4B (SEMA4B) inhibits the invasion of non-small cell lung cancer (NSCLC) through PI3K-dependent suppression of MMP9 activation. SEMA4B may induce FoxO1 nuclear retention through suppressing PI3K/Akt signaling pathway, which subsequently inhibited cell growth through the direct nuclear target of FoxO1, p21. A role of SEMA4B in suppressing NSCLC growth, besides its role in inhibiting cell metastasis, and highlights SEMA4B as a promising therapeutic target for NSCLC.
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TMPK-00538 | Osteopontin Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Ovarian cancer is one of the most lethal malignant tumors in women. Secreted phosphoprotein 1 (SPP1) plays an important role in some cancer types. The expression of SPP1 was higher in epithelial ovarian cancer tissues than in normal ovarian tissues. Silencing SPP1 decreased the cell proliferation, migration, and invasion. Ectopic expression of SPP1 increased the cell proliferation, migration, and invasion. Silencing SPP1 prevented ovarian cancer growth in mice. Silencing SPP1 inhibited Integrin β1/FAK/AKT pathway.
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TMPK-00676 | Osteopontin Protein, Human, Recombinant (aa 17-300, His) | Human | HEK293 | ||
Ovarian cancer is one of the most lethal malignant tumors in women. Secreted phosphoprotein 1 (SPP1) plays an important role in some cancer types. The expression of SPP1 was higher in epithelial ovarian cancer tissues than in normal ovarian tissues. Silencing SPP1 decreased the cell proliferation, migration, and invasion. Ectopic expression of SPP1 increased the cell proliferation, migration, and invasion. Silencing SPP1 prevented ovarian cancer growth in mice. Silencing SPP1 inhibited Integrin β1/FAK/AKT pathway.
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TMPY-02398 | TLE3 Protein, Human, Recombinant (aa 484-772, GST) | Human | E. coli | ||
The association between high TLE3 expression and a favorable response to taxane-containing chemotherapy regimens was validated in patients with non-serous ovarian cancer. That TLE3 expression may serve as a marker of chemosensitivity in taxane-treated patients with non-serous histologies. Transducin-like enhancer of Split3 (TLE3) serves as a transcriptional corepressor during cell differentiation and shows multiple roles in different kinds of cancers. TLE3 repressed CRC proliferation partly through inhibition of MAPK and AKT signaling pathways, suggesting the possibility of TLE3 as a biomarker for CRC prognosis.
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TMPY-04899 | OGN/Osteoglycin Protein, Human, Recombinant (His) | Human | HEK293 | ||
OGN (Osteoglycin) is a Protein Coding gene. This gene encodes a member of the small leucine-rich proteoglycan (SLRP) family of proteins. It belongs to the small leucine-rich proteoglycan (SLRP) family. The encoded protein induces ectopic bone formation in conjunction with transforming growth factor-beta and may regulate osteoblast differentiation. OGN is broadly expressed in the gall bladder, endometrium, and other tissues. OGN reduced Zeb-1 expression via EGFR/Akt leading to inhibition of epithelial-mesenchymal transition. In vitro and in vivo, the OGN expression was demonstrated to reduce cell proliferation, inhibit invasion of colon cancer cells then impede cancer progression. Diseases associated with OGN include Inhibited Male Orgasm and Cornea Plana.
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TMPY-02334 | ULBP-2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
NKG2D ligand 2, also known as N2DL-2, NKG2DL2, ALCAN-alpha, Retinoic acid early transcript 1H, UL16-binding protein 2, ULBP2 and N2DL2, is cell membrane protein that belongs to the MHC class I family. ULBP2 / N2DL-2 is expressed in various types of cancer cell lines and in the fetus, but not in normal tissues. ULBP2 / N2DL-2 is a ligand for the NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway.
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TMPK-00474 | IL-22RA1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
IL-22 receptor, also known as IL-22 R alpha 1 and CRF2-9, is an approximately 65 kDa transmembrane glycoprotein in the type II cytokine receptor family (CRF).Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
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TMPY-06828 | Claudin-18 Protein, Human, Recombinant (CLDN18.1) | Human | HEK293 | ||
Claudins family member Claudin18 (CLDN18) is a four-pass transmembrane protein with two extracellular loops and cytoplasmic N- and C-tails found in tight junctions. CLDN18 modulates paracellular permeability, polarity, and signaling. CLDN18 deficiency has been associated with atrophic gastritis, spasmolytic polypeptide-expressing metaplasia (SPEM), and asthma. Lung-specific CLDN18.1 modulates alveolar epithelial type II (AT2) cell proliferation and organ size. Restoration of CLDN18.1 expression in human lung cancer cells has been shown to suppress proliferation, inhibiting the IGF-1R/AKT axes. Not expressed in other healthy tissues, gastric mucosa-specific isoform CLDN18.2 expression manifests in primary gastric cancers. CLDN18.2 at the surface of epithelial tumor cells is a target in antibody and CAR-therapies currently in development.
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TMPY-04933 | PIK3IP1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
PIK3IP1 contains 1 kringle domain and is a negative regulator of phosphatidylinositol-3-kinase (PI3K), suppresses the development of hepatocellular carcinoma. PI3K is a well-known regulator of cell division, motility, metabolism and survival in most cell types. Proper liver function and development highly depend on intact PI3K signal transduction. Aberrant PI3K pathway signaling in the liver is associated with hepatocellular carcinoma. PI3K signaling is involved in the homeostasis of lipid and glucose metabolism. Activation of the PI3K pathway induces lipogenesis and glycogenesis in the liver, since both Akt overexpressing transgenic mice and PTEN knockout mice develop fatty liver and hypoglycemia. PIK3IP1 overexpression can contribute to glucose homeostasis and fatty deposition.
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TMPY-03111 | PIK3IP1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
PIK3IP1 contains 1 kringle domain and is a negative regulator of phosphatidylinositol-3-kinase (PI3K), suppresses the development of hepatocellular carcinoma. PI3K is a well-known regulator of cell division, motility, metabolism and survival in most cell types. Proper liver function and development highly depend on intact PI3K signal transduction. Aberrant PI3K pathway signaling in the liver is associated with hepatocellular carcinoma. PI3K signaling is involved in the homeostasis of lipid and glucose metabolism. Activation of the PI3K pathway induces lipogenesis and glycogenesis in the liver, since both Akt overexpressing transgenic mice and PTEN knockout mice develop fatty liver and hypoglycemia. PIK3IP1 overexpression can contribute to glucose homeostasis and fatty deposition.
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TMPY-06822 | Claudin-18 Protein, Human, Recombinant (CLDN18.2), Fluorescent | Human | HEK293 | ||
Claudins family member Claudin18 (CLDN18) is a four-pass transmembrane protein with two extracellular loops and cytoplasmic N- and C-tails found in tight junctions. CLDN18 modulates paracellular permeability, polarity, and signaling. CLDN18 deficiency has been associated with atrophic gastritis, spasmolytic polypeptide-expressing metaplasia (SPEM), and asthma. Lung-specific CLDN18.1 modulates alveolar epithelial type II (AT2) cell proliferation and organ size. Restoration of CLDN18.1 expression in human lung cancer cells has been shown to suppress proliferation, inhibiting the IGF-1R/AKT axes. Not expressed in other healthy tissues, gastric mucosa-specific isoform CLDN18.2 expression manifests in primary gastric cancers. CLDN18.2 at the surface of epithelial tumor cells is a target in antibody and CAR-therapies currently in development.
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TMPY-03691 | CD133/PROM1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
CD133, also known as PROM1 and Prominin 1, is a pentaspan transmembrane glycoprotein that belongs to the prominin family. It localizes to membrane protrusions and is often expressed on adult stem cells. CD133 is known to play a role in maintaining stem cell properties by suppressing differentiation. CD133 binds cholesterol in cholesterol-containing plasma membrane microdomains. It is proposed to play a role in apical plasma membrane organization of epithelial cells. CD133 is also involved in regulation of MAPK and Akt signaling pathways. Mutations in PROM1 gene have been shown to result in retinitis pigmentosa and Stargardt disease. PROM1 gene is expressed from at least five alternative promoters that are expressed in a tissue-dependent manner. Expression of this gene is also associated with several types of cancer.
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TMPH-02878 | PTPRS Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans. Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase. Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3. Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta.
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