目录号 | 产品详情 | 靶点 | |
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T8527 | Others | ||
CPYPP 是DOCK2-Rac1相互作用的抑制剂。它能够结合DOCK2DHR-2结构域,并以剂量依赖性方式抑制 DOCK2DHR-2 (IC50:22.8 µM) 对 Rac1 的鸟嘌呤核苷酸交换因子活性。它还抑制DOCK180和DOCK5,对 DOCK9 的抑制作用较小。 | |||
T3481 | Topoisomerase | ||
Bimolane 是一种拓扑异构酶 II 抑制剂。 | |||
T23256 | PDE | ||
RS 25344 hydrochloride 是 cAMP-磷酸二酯酶 4 的选择性抑制剂,在人淋巴细胞中的 IC50为 0.28 nM,对 PDE I、II、III 仅具有微弱的抑制作用,IC50分别为 >100 μM、160 μM、330 μM。它具有抗炎、增强记忆力和认知能力以及抗肿瘤活性。 | |||
T6403 | S1P Receptor LPL Receptor | ||
Siponimod (BAF-312) 是有效,选择性的鞘氨醇-1-磷酸 (S1P)受体调节剂,对 S1P1 和 S1P5 受体具有特异性,EC50 分别为 0.39 nM 和 0.98 nM。 BAF312 对 S1P1 和 S1P5 受体的特异性比 S1P2、S1P3 和 S1P4 受体高 1000 倍以上。 | |||
T6588 | Topoisomerase PKC | ||
Mitoxantrone (mitozantrone) 是一种拓扑异构酶 II 的抑制剂,也可抑制蛋白激酶C (PKC),IC50值为8.5 μM。 | |||
T10765 | Apoptosis Ligand for E3 Ligase Molecular Glues | ||
Eragidomide (CC-90009; Cereblon modulator 1) 是一种 GSPT1 选择性 cereblon (CRBN)E3 连接酶调节剂,以分子胶的方式作用。Eragidomide 通过 CRL4CRBN 选择性靶向 GSPT1 进行泛素化和蛋白酶体降解。 | |||
T7739 | Others Endogenous Metabolite | ||
L-Leucyl-L-Leucine methyl ester hydrochloride (Leu-Leu-ome hydrochloride) 是一种人单核细胞或多形核白细胞产生的 L-亮氨酸甲酯的二肽缩合产物,能够选择性消除具有细胞毒性潜能的淋巴细胞,也能够诱导溶酶体途径应激。 | |||
T0158 | Topoisomerase PKC | ||
Mitoxantrone dihydrochloride (NSC-301739) 是一种拓扑异构酶 II 的抑制剂;也可抑制蛋白激酶C (PKC),IC50值为8.5 μM。 | |||
T6933 | Tyrosine Kinases JAK | ||
Peficitinib (ASP015K) 是一种可口服的 JAK 抑制剂,对 JAK1、JAK2、JAK3 和 Tyk2 的IC50值分别为 3.9、5.0、0.7 和 4.8 nM。 | |||
T25705 | Others | ||
Imupedone (LF 1695) 是一种合成免疫调节剂,可调节 T 淋巴细胞和巨噬细胞,诱导骨髓前体细胞的 T 细胞分化,增加淋巴细胞对有丝分裂原、抗原和同种异体细胞的增殖反应。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04578 | Interferon alpha 1/IFNA1 Protein, Human, Recombinant (His) | Human | Yeast | ||
IFNA1, also known as IFN-alpha and IFNA, belongs to the alpha/beta interferon family. Interferons(IFNs) are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. They belong to the large class of glycoproteins known as cytokines. IFNs stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs can activate immune cells, such as natural killer cells and macrophages; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes, and they also increase the ability of uninfected host cells to resist new infection by the virus. Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon is produced by mitogen- or antigen-stimulated T lymphocytes. IFNA1 is produced by macrophages and has antiviral activities.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01255 | CD2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
T-cell surface antigen CD2, also known as T-cell surface antigen T11/Leu-5, and SRBC, is a single-pass type I membrane protein. It contains one Ig-like C2-type domain and one Ig-like V-type domain. CD2 is a cell adhesion molecule expressed on T cells and is recognized as a target for CD48 (rats) and CD58 (humans). CD2 has been shown to set quantitative thresholds in T cell activation both in vivo and in vitro. Further, intracellular CD2 signaling pathways and networks are being discovered by the identification of several cytosolic tail binding proteins. CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain of CD2 is implicated in the signaling function. The complex of CD2 and CD58 also plays an important role in enhancing the adhesion of T lymphocytes to target cells, and promoting hyperplasia and activation of T lymphocytes. As a cell surface glycoprotein, CD2 expressed on most human T cells and natural killer (NK) cells and plays an important role in mediating cell adhesion in both T-lymphocytes and in signal transduction.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04717 | CD122/IL2RB Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-01068 | CD70 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CD70, a member of the tumor necrosis factor superfamily, is restricted to activated T-and B-lymphocytes and mature dendritic cells. Binding of CD70 to its receptor, CD27, is important in priming, effector functions, differentiation and memory formation of T-cells as well as plasma and memory B-cell generation. Tight control of CD70 expression is required to prevent lethal immunodeficiency. By selective transcription, CD70 is largely confined to activated lymphocytes and dendritic cells (DC). As a type II transmembrane receptor, CD70 is normally expressed on a subset of B, T and NK cells, where it plays a costimulatory role in immune cell activation. Immunohistochemical analysis of CD70 expression in multiple carcinoma types. The restricted expression pattern of CD70 in normal tissues and its widespread expression in various malignancies makes it an attractive target for antibody-based therapeutics. Investigations to exploit CD70 as a cancer target have lead to the identification of potential antibody-based clinical candidates.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05102 | CD122/IL2RB Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-05047 | CD44 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CD44 is a type I transmembrane protein and a member of the cartilage link protein family. It is involved in cell-cell and cell-matrix interactions and signal transduction. Several CD44 ligands have been identified. The most extensively characterized ligand for CD44 is hyaluronan, a component of the extracellular matrix. CD44 protein is expressed on the majority of immune cells. The binding of CD44 to hyaluronan is induced on T lymphocytes after activation by antigen and on monocytes after stimulation by inflammatory agents. Under inflammatory conditions, CD44 on endothelial cells presents hyaluronan to CD44 on activated T lymphocytes and mediates a rolling interaction under flow conditions. Perturbations of the hyaluronan-CD44 interaction at the plasma membrane by various antagonists result in attenuation of receptor tyrosine kinase and transporter activities and inhibition of tumor progression in vivo. CD44 is known to interact with the ezrin family (ERM family) members and form a complex that plays diverse roles within both normal and abnormal cells, particularly cancer cells. CD44 and ezrin and their respective complex have properties suggesting that they may be important in the process of tumour-endothelium interactions, cell migrations, cell adhesion, tumour progression and metastasis.
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TMPY-05680 | CD122/IL2RB Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-02033 | CD44 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD44 is a type I transmembrane protein and a member of the cartilage link protein family. It is involved in cell-cell and cell-matrix interactions and signal transduction. Several CD44 ligands have been identified. The most extensively characterized ligand for CD44 is hyaluronan, a component of the extracellular matrix. CD44 protein is expressed on the majority of immune cells. The binding of CD44 to hyaluronan is induced on T lymphocytes after activation by antigen and on monocytes after stimulation by inflammatory agents. Under inflammatory conditions, CD44 on endothelial cells presents hyaluronan to CD44 on activated T lymphocytes and mediates a rolling interaction under flow conditions. Perturbations of the hyaluronan-CD44 interaction at the plasma membrane by various antagonists result in attenuation of receptor tyrosine kinase and transporter activities and inhibition of tumor progression in vivo. CD44 is known to interact with the ezrin family (ERM family) members and form a complex that plays diverse roles within both normal and abnormal cells, particularly cancer cells. CD44 and ezrin and their respective complex have properties suggesting that they may be important in the process of tumour-endothelium interactions, cell migrations, cell adhesion, tumour progression and metastasis.
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TMPY-00860 | CD122/IL2RB Protein, Human, Recombinant | Human | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-05784 | CD122/IL2RB Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-05216 | CD122/IL2RB Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-04031 | CD122/IL2RB Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Interleukin-2 receptor (IL-2R) also known as High-affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms concerning the ability to bind interleukin 2. The low-affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high-affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high-affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.
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TMPY-03956 | Fas Ligand Protein, Human, Recombinant (His) | Human | Yeast | ||
Fas Ligand, also known as FASLG and CD95L, is the ligand for FAS. It is a transmembrane protein which binds to TNFRSF6/FAS. Interaction of FAS with fas Ligand is critical in triggering apoptosis of some types of cells such as lymphocytes. Fas Ligand may be involved in cytotoxic T-cell mediated apoptosis and in T-cell development. TNFRSF6/FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both.
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TMPY-03967 | BTN3A3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The three butyrophilin BTN3A molecules, BTN3A1, BTN3A2, and BTN3A3, are members of the B7/butyrophilin-like group of Ig superfamily receptors, which modulate the function of T cells. The butyrophilin 3 (BTN3) receptors are implicated in the T lymphocytes regulation and present a wide plasticity in mammals. A thorough phylogenetic analysis reveals a concerted evolution of BTN3 characterized by a strong and recurrent homogenization of the region encoding the signal peptide and the immunoglobulin variable (IgV) domain in Hominoids, where the sequences of BTN3A1 or BTN3A3 are replaced by BTN3A2 sequence.
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TMPY-00072 | GITR/TNFRSF18 Protein, Human, Recombinant (His) | Human | HEK293 | ||
GITR, also known as TNFRSF18(CD357), belongs to the tumor necrosis factor receptor (TNF-R) superfamily. It is the receptor for TNFSF18. GITR plays a key role in dominant immunological self-tolerance maintained by CD25(+)CD4(+) regulatory T cells. GITR may be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. GITR and its ligand are important costimulatory molecules in the pathogenesis of autoimmune diseases. It also mediates NF-kappa-B activation via the TRAF2/NIK pathway.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPJ-00139 | 4-1BB Ligand/TNFSF9 Protein, Human, Recombinant (His) | Human | E. coli | ||
Tumor necrosis factor ligand superfamily member 9(4-1BBL) is single-pass type II membrane protein which is a member of the the tumor necrosis factor family. 4-1BBL is a 254 amino acids cytokine that is expressed in brain, placenta, lung, skeletal muscle and kidney. TNFSF9 has been shown to reactivate anergic T lymphocytes in addition to promoting T lymphocyte proliferation. This cytokine may have a role in activation-induced cell death (AICD) and cognate interactions between T-cells and B-cells/macrophages. It has also been shown to be required for the optimal CD8 responses in CD8 T cells, and is thought to be involved in T cell-tumor cell interaction.
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TMPY-04779 | BTN3A2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The three butyrophilin BTN3A molecules, BTN3A1, BTN3A2, and BTN3A3, are members of the B7/butyrophilin-like group of Ig superfamily receptors, which modulate the function of T cells. BTN3A2 is overexpressed in gastric tumors, and deletion of BTN3A2 inhibited proliferation, migration, and invasion of gastric cancer cells. The butyrophilin 3 (BTN3) receptors are implicated in the T lymphocytes regulation and present a wide plasticity in mammals. A thorough phylogenetic analysis reveals a concerted evolution of BTN3 characterized by a strong and recurrent homogenization of the region encoding the signal peptide and the immunoglobulin variable (IgV) domain in Hominoids, where the sequences of BTN3A1 or BTN3A3 are replaced by BTN3A2 sequence.
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TMPY-06076 | LILRA2/CD85h/ILT1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
LILRA2 (Leukocyte Immunoglobulin Like Receptor A2, also known as LIR7 and ILT1) is a Protein Coding gene. The encoded protein is an activating receptor that inhibits dendritic cell differentiation and antigen presentation and suppresses the innate immune response. It is an activating receptor highly expressed in inflammatory tissues and is involved in granulocyte and macrophage activation. LILRA2 is primarily expressed on the surface of cells of the innate immunity including monocytes, macrophages, neutrophils, basophils, and eosinophils but not on lymphocytes and NK cells. LILRA2 cross-linking on monocytes induces pro-inflammatory cytokines while inhibiting dendritic cell differentiation and antigen presentation. Diseases associated with LILRA2 include Tuberculoid Leprosy and Leprosy 3.
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TMPY-00817 | Granzyme B/GZMB Protein, Human, Recombinant (His) | Human | HEK293 | ||
Granzyme B, also known as GZMB, is the most prominent member of the granzyme family of cell death-inducing serine proteases expressed in the granules of cytotoxic T lymphocytes (CTLs) and NK cells. Granzyme B enters the target cells depending on another membrane-binding granule protein, perforin, results in the activation of effector caspases and mitochondrial depolarization through caspase-dependent and -independent pathways, and consequently induces rapid cell apoptosis. Over 3 substrates of GZMB have been identified including the key substrate caspase-3, ICAD, and Bid. GZMB is suggested to protect the host by lysing cells bearing on their surface 'nonself' antigens such as bacterial and viral infected-cells and tumor cells and accordingly plays an essential role in immunosurveillance.
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TMPY-00369 | LY6D Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
LY6D (Lymphocyte Antigen 6 Family Member D) is a Protein Coding gene. It may act as a specification marker at the earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. The expression of LY6D is induced in MCF10A cells by X-ray irradiation. The induction of LY6D expression is triggered through a pathway regulated by ATM, CHK2, and p53. This method is a new Ab-directed proteomic strategy for the analysis of membrane proteins and applies to various biological phenomena in situations in which both target molecule-expressing cells and nonexpressing cells are available. Diseases associated with LY6D include Alzheimer's Disease 16 and Inferior Myocardial Infarction.
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TMPY-03488 | IL-11 Protein, Human, Recombinant | Human | E. coli | ||
IL11 is a multifunctional cytokine first isolated in 199 from bone marrow-derived stromal cells. It is a key regulator of multiple events in hematopoiesis, most notably the stimulation of megakaryocyte maturation. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin. IL11 can improve platelet recovery after chemotherapy-induced thrombocytopenia, induce acute-phase proteins, modulate antigen-antibody responses, participate in the regulation of bone cell proliferation and differentiation, and could be used as a therapeutic for osteoporosis. IL11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.
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TMPY-04178 | IL-11 Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL11 is a multifunctional cytokine first isolated in 199 from bone marrow-derived stromal cells. It is a key regulator of multiple events in hematopoiesis, most notably the stimulation of megakaryocyte maturation. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin. IL11 can improve platelet recovery after chemotherapy-induced thrombocytopenia, induce acute-phase proteins, modulate antigen-antibody responses, participate in the regulation of bone cell proliferation and differentiation, and could be used as a therapeutic for osteoporosis. IL11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.
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TMPY-04793 | IL-35 Protein, Human, Recombinant (Flag & His) | Human | HEK293 | ||
IL12A is a subunit of a cytokine that acts on T and natural killer cells and has a broad array of biological activities. The cytokine is a disulfide-linked heterodimer composed of the 35-kD subunit encoded by this gene, and a 40-kD subunit that is a member of the cytokine receptor family. IL12A, together with IL27B, form a disulfide-linked heterodimer: IL12A&IL27B. IL12A&IL27B is required for the T-cell-independent induction of IFN-gamma and is important for the differentiation of both Th1 and Th2 cells. The responses of lymphocytes to this cytokine are mediated by the activator of transcription protein STAT4. Nitric oxide synthase 2A (NOS2A/NOS2) is found to be required for the signaling process of IL12A&IL27B in innate immunity.
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TMPY-05842 | IL-11 Protein, Cynomolgus, Recombinant | Cynomolgus | E. coli | ||
IL11 is a multifunctional cytokine first isolated in 199 from bone marrow-derived stromal cells. It is a key regulator of multiple events in hematopoiesis, most notably the stimulation of megakaryocyte maturation. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin. IL11 can improve platelet recovery after chemotherapy-induced thrombocytopenia, induce acute-phase proteins, modulate antigen-antibody responses, participate in the regulation of bone cell proliferation and differentiation, and could be used as a therapeutic for osteoporosis. IL11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.
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TMPJ-01469 | NGF Protein, Human, Recombinant (E. colli) | Mouse | E.coli | ||
NGF is the first member discovered in the Neurotrophin family, which includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Mouse beta -NGF is a homodimer of two 120 amino acid polypeptides. It shares approximately 90% homology at the amino acid level with human beta -NGF and 95.8% with rat beta -NGF. NGF signaling has been shown to play an important role in neuroprotection and repair. β-NGF acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. It is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems.
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TMPY-00694 | Carbonic Anhydrase 12 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12, also known as Car12 and carbonic anhydrase XII, is a type I membrane enzyme of an N-terminal extracellular catalytic domain, a membrane-spanning α-helix, and a small intracellular C-terminal domain. It is highly expressed in colon, kidney, prostate, intestine and activated lymphocytes and moderately expressed in pancreas, ovary, and testis. Overexpression of the CA12 is observed in certain human cancers and is used as a tumor marker. rmCA12 corresponds to the extracellular domain and has both carbonic anhydrase activity and esterase activity.
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TMPY-00638 | Interferon alpha B/IFNA8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interferon alpha-B, also known as IFNA8, belongs to the alpha/beta interferon family. Interferons are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They also allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. Interferons also activate immune cells, such as natural killer cells and macrophages. They increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes. They also increase the ability of uninfected host cells to resist new infections by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Produced by macrophages, IFN-alpha has antiviral activities.
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TMPY-01827 | CD30/TNFRSF8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00095 | IL-3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
IL3 (interleukin 3), also known as IL-3, is a potent growth-promoting cytokine that belongs to the IL-3 family. IL3/IL-3 also belongs to the group of interleukins. Interleukins are produced by a wide variety of body cells. The function of the immune system depends in a large part on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency. The majority of interleukins are synthesized by helper CD4+ T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T, B, and hematopoietic cells. IL3/IL-3 is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation, and apoptosis. IL3/IL-3 has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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TMPY-03377 | CD73 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
5'-nucleotidase, also known as NT5E, NTE, and CD73, is a cell membrane protein that belongs to the 5'-nucleotidase family. CD73 is a glycosylphosphatidylinositol (GPI) anchored purine salvage enzyme expressed on the surface of human T and B lymphocytes. CD73 catalyzes the conversion of purine and pyrimidine ribo- and deoxyribonucleoside monophosphates to the corresponding nucleosides. CD73 serves as a costimulatory molecule in activating T cells. CD73 generated adenosine functions in cell signaling in many physiologic systems, including intestinal epithelium, ischemic myocardium, and cholinergic synapses. CD73 might mediate lymphocyte-stromal cell interactions or condition the local microenvironment to facilitate lymphocyte development and/or function. In CD73-depleted cells, surface levels of the leukocyte adhesion molecules ICAM-1, VCAM-1, and E-selectin increase. CD73 produces extracellular adenosine, which then acts on G protein-coupled purinergic receptors to induce cellular responses. CD73 has also been reported to regulate the expression of pro-inflammatory molecules in mouse endothelium.
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TMPY-04845 | IL-3 Protein, Mouse, Recombinant | Mouse | HEK293 | ||
IL3 (interleukin 3), also known as IL-3, is a potent growth-promoting cytokine that belongs to the IL-3 family. IL3/IL-3 also belongs to the group of interleukins. Interleukins are produced by a wide variety of body cells. The function of the immune system depends in a large part on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency. The majority of interleukins are synthesized by helper CD4+ T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T, B, and hematopoietic cells. IL3/IL-3 is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation, and apoptosis. IL3/IL-3 has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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TMPY-01851 | CD73 Protein, Human, Recombinant (His) | Human | HEK293 | ||
5'-nucleotidase, also known as NT5E, NTE, and CD73, is a cell membrane protein that belongs to the 5'-nucleotidase family. CD73 is a glycosylphosphatidylinositol (GPI) anchored purine salvage enzyme expressed on the surface of human T and B lymphocytes. CD73 catalyzes the conversion of purine and pyrimidine ribo- and deoxyribonucleoside monophosphates to the corresponding nucleosides. CD73 serves as a costimulatory molecule in activating T cells. CD73 generated adenosine functions in cell signaling in many physiologic systems, including intestinal epithelium, ischemic myocardium, and cholinergic synapses. CD73 might mediate lymphocyte-stromal cell interactions or condition the local microenvironment to facilitate lymphocyte development and/or function. In CD73-depleted cells, surface levels of the leukocyte adhesion molecules ICAM-1, VCAM-1, and E-selectin increase. CD73 produces extracellular adenosine, which then acts on G protein-coupled purinergic receptors to induce cellular responses. CD73 has also been reported to regulate the expression of pro-inflammatory molecules in mouse endothelium.
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TMPY-01342 | CD73 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
5'-nucleotidase, also known as NT5E, NTE, and CD73, is a cell membrane protein that belongs to the 5'-nucleotidase family. CD73 is a glycosylphosphatidylinositol (GPI) anchored purine salvage enzyme expressed on the surface of human T and B lymphocytes. CD73 catalyzes the conversion of purine and pyrimidine ribo- and deoxyribonucleoside monophosphates to the corresponding nucleosides. CD73 serves as a costimulatory molecule in activating T cells. CD73 generated adenosine functions in cell signaling in many physiologic systems, including intestinal epithelium, ischemic myocardium, and cholinergic synapses. CD73 might mediate lymphocyte-stromal cell interactions or condition the local microenvironment to facilitate lymphocyte development and/or function. In CD73-depleted cells, surface levels of the leukocyte adhesion molecules ICAM-1, VCAM-1, and E-selectin increase. CD73 produces extracellular adenosine, which then acts on G protein-coupled purinergic receptors to induce cellular responses. CD73 has also been reported to regulate the expression of pro-inflammatory molecules in mouse endothelium.
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TMPY-03540 | CD73 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
5'-nucleotidase, also known as NT5E, NTE, and CD73, is a cell membrane protein that belongs to the 5'-nucleotidase family. CD73 is a glycosylphosphatidylinositol (GPI) anchored purine salvage enzyme expressed on the surface of human T and B lymphocytes. CD73 catalyzes the conversion of purine and pyrimidine ribo- and deoxyribonucleoside monophosphates to the corresponding nucleosides. CD73 serves as a costimulatory molecule in activating T cells. CD73 generated adenosine functions in cell signaling in many physiologic systems, including intestinal epithelium, ischemic myocardium, and cholinergic synapses. CD73 might mediate lymphocyte-stromal cell interactions or condition the local microenvironment to facilitate lymphocyte development and/or function. In CD73-depleted cells, surface levels of the leukocyte adhesion molecules ICAM-1, VCAM-1, and E-selectin increase. CD73 produces extracellular adenosine, which then acts on G protein-coupled purinergic receptors to induce cellular responses. CD73 has also been reported to regulate the expression of pro-inflammatory molecules in mouse endothelium.
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TMPY-00297 | IL-3 Protein, Human, Recombinant(aa 20-152) | Human | E. coli | ||
IL3 (interleukin 3), also known as IL-3, is a potent growth-promoting cytokine that belongs to the IL-3 family. IL3/IL-3 also belongs to the group of interleukins. Interleukins are produced by a wide variety of body cells. The function of the immune system depends in a large part on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency. The majority of interleukins are synthesized by helper CD4+ T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. They promote the development and differentiation of T, B, and hematopoietic cells. IL3/IL-3 is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation, and apoptosis. IL3/IL-3 has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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TMPY-05016 | HHLA2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
B7H7 gene encodes a protein-ligand found on the surface of monocytes. The encoded protein is thought to regulate cell-mediated immunity by binding to a receptor on T lymphocytes and inhibiting the proliferation of these cells. Alternate splicing results in multiple transcript variants. HERV–H LTR-associating 2 (HHLA2, also called B7H7/B7-H5/B7y)has been recently discovered as the newest member of the B7 family and has 23–33% similarity in amino acid sequence with the other B7 molecules. This ligand is the only B7 family member that is found in humans but not in mice. It is constitutively expressed on the surface of human monocytes and is induced on B cells. HHLA2 binds to its putative receptor(s) on a variety of immune cells including CD4 and CD8 T cells and antigen-presenting cells. Similar to B7-H3, both a T cell coinhibitory role, as well as a costimulatory role, has been reported for this ligand.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04925 | CD8 beta Protein, Human, Recombinant, Biotinylated | Human | HEK293 | ||
CD8B (CD8b molecule), also known as P37 and LEU2, contains 1 Ig-like V-type (immunoglobulin-like) domain. The CD8 antigen is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. The CD8 antigen, acting as a coreceptor, and the T-cell receptor on the T lymphocyte recognize antigens displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional coreceptor is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains. P37 gene encodes the CD8 beta chain isoforms. Multiple alternatively spliced transcript variants encoding distinct membrane associated or secreted isoforms have been described. A pseudogene, also located on chromosome 2, has been identified. CD8 is thought to play a role in the process of T-cell mediated killing.
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TMPY-01371 | IL-17RA Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-01226 | CD4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
T-cell surface glycoprotein CD4, is a single-pass type I membrane protein. CD4 contains three Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. CD4 is a glycoprotein expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells. The CD4 surface determinant, previously associated as a phenotypic marker for helper/inducer subsets of T lymphocytes, has now been critically identified as the binding/entry protein for human immunodeficiency viruses (HIV). The human CD4 molecule is readily detectable on monocytes, T lymphocytes, and brain tissues. All human tissue sources of CD4 bind radiolabeled gp120 to the same relative degree; however, the murine homologous protein, L3T4, does not bind the HIV envelope protein. CD4 is a co-receptor that assists the T cell receptor (TCR) to activate its T cell following an interaction with an antigen-presenting cell. Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR. CD4 interacts directly with MHC class II molecules on the surface of the antigen-presenting cell via its extracellular domain. The CD4 molecule is currently the object of intense interest and investigation both because of its role in normal T-cell function, and because of its role in HIV infection. CD4 is a primary receptor used by HIV-1 to gain entry into host T cells. HIV infection leads to a progressive reduction of the number of T cells possessing CD4 receptors.Viral protein U (VpU) of HIV-1 plays an important role in downregulation of the main HIV-1 receptor CD4 from the surface of infected cells. Physical binding of VpU to newly synthesized CD4 in the endoplasmic reticulum is an early step in a pathway leading to proteasomal degradation of CD4. Amino acids in both helices found in the cytoplasmic region of VpU in membrane-mimicking detergent micelles experience chemical shift perturbations upon binding to CD4, whereas amino acids between the two helices and at the C-terminus of VpU show no or only small changes, respectively. Paramagnetic spin labels were attached at three sequence positions of a CD4 peptide comprising the transmembrane and cytosolic domains of the receptor. VpU binds to a membrane-proximal region in the cytoplasmic domain of CD4.
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TMPY-01400 | CD4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
T-cell surface glycoprotein CD4, is a single-pass type I membrane protein. CD4 contains three Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. CD4 is a glycoprotein expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells. The CD4 surface determinant, previously associated as a phenotypic marker for helper/inducer subsets of T lymphocytes, has now been critically identified as the binding/entry protein for human immunodeficiency viruses (HIV). The human CD4 molecule is readily detectable on monocytes, T lymphocytes, and brain tissues. All human tissue sources of CD4 bind radiolabeled gp120 to the same relative degree; however, the murine homologous protein, L3T4, does not bind the HIV envelope protein. CD4 is a co-receptor that assists the T cell receptor (TCR) to activate its T cell following an interaction with an antigen-presenting cell. Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR. CD4 interacts directly with MHC class II molecules on the surface of the antigen-presenting cell via its extracellular domain. The CD4 molecule is currently the object of intense interest and investigation both because of its role in normal T-cell function, and because of its role in HIV infection. CD4 is a primary receptor used by HIV-1 to gain entry into host T cells. HIV infection leads to a progressive reduction of the number of T cells possessing CD4 receptors.Viral protein U (VpU) of HIV-1 plays an important role in downregulation of the main HIV-1 receptor CD4 from the surface of infected cells. Physical binding of VpU to newly synthesized CD4 in the endoplasmic reticulum is an early step in a pathway leading to proteasomal degradation of CD4. Amino acids in both helices found in the cytoplasmic region of VpU in membrane-mimicking detergent micelles experience chemical shift perturbations upon binding to CD4, whereas amino acids between the two helices and at the C-terminus of VpU show no or only small changes, respectively. Paramagnetic spin labels were attached at three sequence positions of a CD4 peptide comprising the transmembrane and cytosolic domains of the receptor. VpU binds to a membrane-proximal region in the cytoplasmic domain of CD4.
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TMPY-05384 | CD4 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
T-cell surface glycoprotein CD4, is a single-pass type I membrane protein. CD4 contains three Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. CD4 is a glycoprotein expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells. The CD4 surface determinant, previously associated as a phenotypic marker for helper/inducer subsets of T lymphocytes, has now been critically identified as the binding/entry protein for human immunodeficiency viruses (HIV). The human CD4 molecule is readily detectable on monocytes, T lymphocytes, and brain tissues. All human tissue sources of CD4 bind radiolabeled gp120 to the same relative degree; however, the murine homologous protein, L3T4, does not bind the HIV envelope protein. CD4 is a co-receptor that assists the T cell receptor (TCR) to activate its T cell following an interaction with an antigen-presenting cell. Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR. CD4 interacts directly with MHC class II molecules on the surface of the antigen-presenting cell via its extracellular domain. The CD4 molecule is currently the object of intense interest and investigation both because of its role in normal T-cell function, and because of its role in HIV infection. CD4 is a primary receptor used by HIV-1 to gain entry into host T cells. HIV infection leads to a progressive reduction of the number of T cells possessing CD4 receptors.Viral protein U (VpU) of HIV-1 plays an important role in downregulation of the main HIV-1 receptor CD4 from the surface of infected cells. Physical binding of VpU to newly synthesized CD4 in the endoplasmic reticulum is an early step in a pathway leading to proteasomal degradation of CD4. Amino acids in both helices found in the cytoplasmic region of VpU in membrane-mimicking detergent micelles experience chemical shift perturbations upon binding to CD4, whereas amino acids between the two helices and at the C-terminus of VpU show no or only small changes, respectively. Paramagnetic spin labels were attached at three sequence positions of a CD4 peptide comprising the transmembrane and cytosolic domains of the receptor. VpU binds to a membrane-proximal region in the cytoplasmic domain of CD4.
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TMPY-02515 | Interferon alpha 7/IFNA7 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Interferon alpha-7(IFNA7) is a member of the interferon family. Interferons belong to the group of the regulatory glycoproteins, of low molecular mass. They are the products of infected cell-genome, but not virus, as a consequence of the cause answer by different inductors. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs have other functions: they activate immune cells, such as natural killer cells and macrophages; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes, and they increase the ability of uninfected host cells to resist new infection by the virus. Certain host symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Human IFN is divided on the sequence of amino-acids into three groups: Alpha, Beta, and Gamma interferons.
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TMPY-03686 | NKG2A/CD159a Protein, Cynomolgus/Rhesus, Recombinant (hFc) | Cynomolgus,Rhesus | HEK293 | ||
NKG2, also known as NKG2A(CD159A), is a member of the killer cell lectin-like receptor family. This family is a group of transmembrane proteins preferentially expressed in NK cells. Members of this family are characterized by the type II membrane orientation and the presence of a C-type lectin domain. NKG2 contains 1 C-type lectin domain and forms a complex with another family member, KLRD1/CD94. It is expressed only in NK-cells, but not in T-cells or B-cells. It has been shown that NKG2 represents a family of related cDNA clones, designated NKG2A, NKG2B, NKG2C, and NKG2D, which encode type 2 integral membrane proteins (extracellular C-terminus) containing a C-type lectin domain. Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NKG2 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.
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TMPY-05319 | BCMA/TNFRSF17 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Tumor necrosis factor receptor superfamily, member 17 (TNFRSF17), also known as B cell maturation antigen (BCMA) or CD269 antigen, is a member of the TNF-receptor superfamily. This receptor is preferentially expressed in mature B lymphocytes, and may be important for B cell development and autoimmune response. This receptor has been shown to specifically bind to the tumor necrosis factor (ligand) superfamily, member 13b (TNFSF13BBAFF), and to lead to NF-kappaB and MAPK8/JNK activation. TNFRSF17/BCMA/CD269 also binds to various TRAF family members, and thus may transduce signals for cell survival and proliferation. TNFRSF17/BCMA/CD269 is a receptor for TALL-1 and BCMA activates NF-kappaB through a TRAF5-, TRAF6-, NIK-, and IKK-dependent pathway. The identification of TNFRSF17 as a NF-kappaB-activating receptor for TALL-1 suggests molecular targets for drug development against certain immunodeficient or autoimmune diseases. TNFRSF17/BCMA is a target of donor B-cell immunity in patients with myeloma who respond to DLI. Antibody responses to cell-surface BCMA may contribute directly to tumor rejection in vivo.
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TMPY-05039 | LTBR Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
LTBR (lymphotoxin beta receptor (TNFR superfamily, member 3)) is a member of the tumor necrosis factor (TNF) family of receptors. The tumor necrosis factor receptor is a trimeric cytokine receptor that binds tumor necrosis factors. The receptor cooperates with an adaptor protein (such as TRADD, TRAF, RIP), which is important in determining the outcome of the response. LTBR is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. LTBR specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphotoxin-beta). LTBR and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of this protein can trigger apoptosis. Not only does the LTBR help trigger apoptosis, but it can also lead to the release of the cytokine interleukin 8. Overexpression of LTBR in HEK293 cells increases IL-8 promoter activity and leads to IL-8 release. It is also essential for the development and organization of the secondary lymphoid organs and chemokine release.
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TMPY-02457 | IL-2 Protein, Rat, Recombinant | Rat | E. coli | ||
Interleukin-2, also known as a T-cell growth factor, TCGF, Aldesleukin, and IL2, is a secreted protein that belongs to the IL-2 family. Interleukin-2 / IL-2 was the first interleukin molecule to be discovered. Interleukin-2 / IL-2 molecule was first purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School. Interleukin-2 / IL-2 was also the first cytokine shown to mediate its effects via a specific IL-2 receptor, and it was also the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library. Interleukin-2 / IL-2 was designated number 2 because Smith's data at the time indicated that IL-1, produced by macrophages, facilitates IL-2 production by T lymphocytes (T cells).Interleukin-2 / IL-2 is produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Interleukin-2 / IL-2 is normally produced by the body during an immune response. When environmental substances (molecules or microbes) gain access to the body, these substances (termed antigens) are recognized as foreign by antigen receptors that are expressed on the surface of lymphocytes. Antigen binding to the T cell receptor (TCR) stimulates the secretion of Interleukin-2 / IL-2 and the expression of IL-2 receptors IL-2R. The IL-2 / IL-2R interaction then stimulates the growth, differentiation, and survival of antigen-selected cytotoxic T cells via the activation of the expression of specific genes. Interleukin-2 / IL-2 can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. The World Reference Standard for Interleukin-2 / IL-2 is produced by the National Institute of Biological Standards and Control in the UK. A recombinant form of Interleukin-2 / IL-2 for clinical use is manufactured by Chiron Corporation with the brand name Proleukin. It has been approved by the Food and Drug Administration (FDA) for the treatment of cancers (malignant melanoma, renal cell cancer), and is in clinical trials for the treatment of chronic viral infections, and as a booster (adjuvant) for vaccines. The use of Interleukin-2 / IL-2 in HIV therapy is ineffective.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02788 | IL-2 Protein, Mouse, Recombinant | Mouse | E. coli | ||
Interleukin-2, also known as a T-cell growth factor, TCGF, Aldesleukin, and IL2, is a secreted protein that belongs to the IL-2 family. Interleukin-2 / IL-2 was the first interleukin molecule to be discovered. Interleukin-2 / IL-2 molecule was first purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School. Interleukin-2 / IL-2 was also the first cytokine shown to mediate its effects via a specific IL-2 receptor, and it was also the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library. Interleukin-2 / IL-2 was designated number 2 because Smith's data at the time indicated that IL-1, produced by macrophages, facilitates IL-2 production by T lymphocytes (T cells).Interleukin-2 / IL-2 is produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Interleukin-2 / IL-2 is normally produced by the body during an immune response. When environmental substances (molecules or microbes) gain access to the body, these substances (termed antigens) are recognized as foreign by antigen receptors that are expressed on the surface of lymphocytes. Antigen binding to the T cell receptor (TCR) stimulates the secretion of Interleukin-2 / IL-2 and the expression of IL-2 receptors IL-2R. The IL-2 / IL-2R interaction then stimulates the growth, differentiation, and survival of antigen-selected cytotoxic T cells via the activation of the expression of specific genes. Interleukin-2 / IL-2 can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. The World Reference Standard for Interleukin-2 / IL-2 is produced by the National Institute of Biological Standards and Control in the UK. A recombinant form of Interleukin-2 / IL-2 for clinical use is manufactured by Chiron Corporation with the brand name Proleukin. It has been approved by the Food and Drug Administration (FDA) for the treatment of cancers (malignant melanoma, renal cell cancer), and is in clinical trials for the treatment of chronic viral infections, and as a booster (adjuvant) for vaccines. The use of Interleukin-2 / IL-2 in HIV therapy is ineffective.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04493 | BCMA/TNFRSF17 Protein, Human, Recombinant (rFc) | Human | HEK293 | ||
Tumor necrosis factor receptor superfamily, member 17 (TNFRSF17), also known as B cell maturation antigen (BCMA) or CD269 antigen, is a member of the TNF-receptor superfamily. This receptor is preferentially expressed in mature B lymphocytes, and may be important for B cell development and autoimmune response. This receptor has been shown to specifically bind to the tumor necrosis factor (ligand) superfamily, member 13b (TNFSF13BBAFF), and to lead to NF-kappaB and MAPK8/JNK activation. TNFRSF17/BCMA/CD269 also binds to various TRAF family members, and thus may transduce signals for cell survival and proliferation. TNFRSF17/BCMA/CD269 is a receptor for TALL-1 and BCMA activates NF-kappaB through a TRAF5-, TRAF6-, NIK-, and IKK-dependent pathway. The identification of TNFRSF17 as a NF-kappaB-activating receptor for TALL-1 suggests molecular targets for drug development against certain immunodeficient or autoimmune diseases. TNFRSF17/BCMA is a target of donor B-cell immunity in patients with myeloma who respond to DLI. Antibody responses to cell-surface BCMA may contribute directly to tumor rejection in vivo.
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TMPY-05074 | NKG2A/CD159a Protein, Human, Recombinant (aa 94-233, His) | Human | HEK293 | ||
NKG2, also known as NKG2A(CD159A), is a member of the killer cell lectin-like receptor family. This family is a group of transmembrane proteins preferentially expressed in NK cells. Members of this family are characterized by the type II membrane orientation and the presence of a C-type lectin domain. NKG2 contains 1 C-type lectin domain and forms a complex with another family member, KLRD1/CD94. It is expressed only in NK-cells, but not in T-cells or B-cells. It has been shown that NKG2 represents a family of related cDNA clones, designated NKG2A, NKG2B, NKG2C, and NKG2D, which encode type 2 integral membrane proteins (extracellular C-terminus) containing a C-type lectin domain. Natural killer (NK) cells are lymphocytes that can mediate lysis of certain tumor cells and virus-infected cells without previous activation. They can also regulate specific humoral and cell-mediated immunity. NKG2 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.
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TMPY-03213 | BCMA/TNFRSF17 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Tumor necrosis factor receptor superfamily, member 17 (TNFRSF17), also known as B cell maturation antigen (BCMA) or CD269 antigen, is a member of the TNF-receptor superfamily. This receptor is preferentially expressed in mature B lymphocytes, and may be important for B cell development and autoimmune response. This receptor has been shown to specifically bind to the tumor necrosis factor (ligand) superfamily, member 13b (TNFSF13BBAFF), and to lead to NF-kappaB and MAPK8/JNK activation. TNFRSF17/BCMA/CD269 also binds to various TRAF family members, and thus may transduce signals for cell survival and proliferation. TNFRSF17/BCMA/CD269 is a receptor for TALL-1 and BCMA activates NF-kappaB through a TRAF5-, TRAF6-, NIK-, and IKK-dependent pathway. The identification of TNFRSF17 as a NF-kappaB-activating receptor for TALL-1 suggests molecular targets for drug development against certain immunodeficient or autoimmune diseases. TNFRSF17/BCMA is a target of donor B-cell immunity in patients with myeloma who respond to DLI. Antibody responses to cell-surface BCMA may contribute directly to tumor rejection in vivo.
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