目录号 | 产品详情 | 靶点 | |
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TN2054 | Calcium Channel | ||
Periplocymarin 是一种强心苷,从 Periploca sepium 和 Periploca graeca 中分离得到,具有抗癌潜力。 | |||
T11285 | Others | ||
FIDAS-5 是甲硫氨酸腺苷转移酶 2A 抑制剂(IC50:2.1 μM),具有口服活性。它能够与 S-腺苷甲硫氨酸有效竞争 MAT2A 结合,并具有抗癌作用。 | |||
T6400 | Androgen Receptor | ||
AZD3514 是一种口服雄激素受体下调剂(Ki :2.2 μM),能够减少 AR 蛋白表达。 | |||
T11284 | Others Wnt/beta-catenin Methionine Adenosyltransferase (MAT) | ||
FIDAS-3 是一种强效Wnt 抑制剂,也是一种二苯乙烯衍生物,对甲硫氨酸腺苷转移酶 2A (MAT2A) 的IC50为 4.9 μM。它能够与 S-腺苷甲硫氨酸有效竞争MAT2A 结合,并具有抗癌作用。 | |||
T8839 | Apoptosis Others | ||
ICCB280 是一种 C/EBPα诱导剂,通过激活 C/EBPα 并影响其下游靶点,具有终末分化、增殖停滞和凋亡的抗白血病特性。 | |||
T7138 | Apoptosis Others | ||
FB23-2 是一种 mRNA N6- 甲基腺嘌呤脱甲基酶 FTO 选择性抑制剂,IC50值为 2.6 μM。它具有抗增殖作用,可研究急性髓系白血病。 | |||
T13996 | HDAC | ||
1-Naphthohydroxamic acid 是一种选择性 HDAC8抑制剂,IC50为 14 μM。它对 HDAC8的选择性高于 I 类 HDAC1 和 II 类 HDAC6,IC50大于100 μM,可诱导微管蛋白乙酰化。 | |||
T8872 | EGFR | ||
(Rac)-JBJ-04-125-02 (JBJ-04-125-02) 是 JBJ-04-125-02 的消旋体,是选择性突变,可口服的 EGFR 变构抑制剂,对EGFRL858R/T790M 的IC50为 0.26 nM。 | |||
T1923 | Histone Methyltransferase | ||
BRD4770 是组蛋白甲基转移酶G9a 抑制剂,可激活共济失调毛细血管扩张突变途径并诱导细胞衰老。它可抑制H3K9的二甲基和三甲基化,EC50为 5 µM。 | |||
T9195 | Apoptosis JAK | ||
SHR0302 (ARQ252) 是一种具有口服活性的 JAK 抑制剂。它对 JAK1的结合力是 JAK2的 10 倍以上,是 JAK3的 77 倍,是 Tyk2的 420 倍。它抑制JAK1-STAT3磷酸化并诱导肝星状细胞凋亡,具有抗增殖和抗炎作用。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-01738 | IL-1 alpha/IL-1A Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00854 | IL-1 alpha/IL-1A Protein, Human, Recombinant | Human | HEK293 | ||
IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-06981 | IL-1 alpha/IL-1A Protein, Human, Recombinant (E. coli) | Human | E. coli | ||
IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.
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TMPJ-00038 | IL-7 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Mouse interleukin-7(IL-7) is the member of hemopoietin family which is important to the differentiation, proliferation, and survival of lymphocyte. Mouse IL-7 shares approximately 88% aa sequence identity with rat IL-7 and 58-60% with human, equine, bovine, ovine, porcine, feline and canine IL-7. It is widely expressed in primary and secondary lymphoid tissues cell and stromal epithelial cells of the thymus, bone marrow, and intestines. IL-7 activation of IL-7 R alpha is critical for both T cell and B cell lineage development. It is important for proliferation during certain stages of B-cell maturation. IL-7 contributes to the maintenance of all naïve and memory T cells, mainly by promoting expression of the anti-apoptotic protein Bcl-2. It is required for optimal T cell-dendritic cell interaction.
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TMPJ-01467 | Oncostatin M/OSM Protein, Human, Recombinant (E. coli, His) | Human | E.coli | ||
Oncostatin M (OSM) is a glycoprotein belonging to the interleukin-6 family of cytokines that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. OSM encodes a growth regulator, which Inhibits the proliferation of a number of tumor cell lines. It stimulates proliferation of AIDS-KS cells. OSM regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. OSM is considered as a pleiotropic cytokine that initiates its biological activities through specific cell surface receptors. The low affinity LIF receptor that shares the similarity of containing protein gp130 has now been identified to be a component of a high- affinity OSM receptor that will transduce OSM signals. OSM has also been shown to play a role in both pro and anti-inflammatory actions. OSM may also be involved in many biometabolism processes including liver development, haematopoeisis, inflammation, bone formation and destruction and possibly CNS development.
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TMPJ-01464 | IL-2 Superkine Protein, Human, Recombinant (L100F, R101D, L105V, I106V, I112F) | Human | Human Cells | ||
Interleukin-2(IL-2) is an interleukin, a type of cytokine signaling molecule in the immune system,belongs to the IL-2 family. It is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. New research has shown that IL-2 mutant reduced toxicity while being more potent at stimulating anti-tumor effector immune cells.
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TMPY-05176 | AMH Protein, Human, Recombinant (His) | Human | HEK293 | ||
Anti-Mullerian hormone (AMH), a member of the TGF-beta superfamily, is produced by granulosa cells (GCs) of preantral and small antral follicles and plays a role in regulating the recruitment of primordial follicles and the FSH-dependent development of follicles. BMP15 up-regulates the transcription of AMH and that the inhibition of p38 MAPK decreases the BMP15-induced expression of AMH and SOX9, suggesting that BMP15 up-regulates the expression of AMH via the p38 MAPK signaling pathway, and this process involves the SOX9 transcription factor. AMH is widely used for assessing ovarian reserve, and it is particularly convenient, because it is thought to have minimal variability throughout the menstrual cycle. Fetal anti-Mullerian hormone (AMH) is responsible for normal male sexual differentiation, and circulating AMH is used as a marker of testicular tissue in newborns with disorders of sex development. Anti-Mullerian hormone (AMH) produced in the developing testis induces the regression of the Mullerian duct, which develops into the oviducts, uterus and upper vagina. As well as other hormone receptors, and a decreased ovarian cortex cell proliferation. These results help understand the inhibitory effects of AMH on follicular development.
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TMPY-01743 | 4-1BB/CD137/TNFRSF9 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05376 | 4-1BB/CD137/TNFRSF9 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05594 | 4-1BB/CD137/TNFRSF9 Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05504 | 4-1BB/CD137/TNFRSF9 Protein, Rhesus, Recombinant (His), Biotinylated | Rhesus | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05767 | 4-1BB/CD137/TNFRSF9 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-03156 | VEGFC Protein, Mouse/Rat, Recombinant (aa 108-223, His) | Mouse,Rat | HEK293 | ||
Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF family. Upon biosynthesis, VEGF-C protein is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGF-C protein is a dimeric glycoprotein, as a ligand for two receptors, VEGFR-3 (Flt4), and VEGFR-2. VEGF-C may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis. VEGF-C protein is over-expressed in various human cancers including breast cancer and prostate cancer. VEGF-C/VEGFR-3 axis, through different signaling pathways, plays a critical role in cancer progression by regulating different cellular functions, such as invasion, proliferation, and resistance to chemotherapy. Thus, targeting the VEGF-C/VEGFR-3 axis may be therapeutically significant for certain types of tumors.
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TMPY-01007 | VEGFC Protein, Human, Recombinant (His) | Human | HEK293 | ||
Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF family. Upon biosynthesis, VEGF-C protein is secreted as a non-covalent momodimer in an anti-parellel fashion. VEGF-C protein is a dimeric glycoprotein, as a ligand for two receptors, VEGFR-3 (Flt4), and VEGFR-2. VEGF-C may function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis. VEGF-C protein is over-expressed in various human cancers including breast cancer and prostate cancer. VEGF-C/VEGFR-3 axis, through different signaling pathways, plays a critical role in cancer progression by regulating different cellular functions, such as invasion, proliferation, and resistance to chemotherapy. Thus, targeting the VEGF-C/VEGFR-3 axis may be therapeutically significant for certain types of tumors.
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TMPY-02778 | ENPP2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
ENPP2 (Ectonucleotide pyrophosphatase/phosphodiesterase family member 2), also referred as Autotaxin, is a secreted enzyme encoded by the ENPP2 gene. This gene product stimulates the motility of tumor cells, has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The Autotaxin protein is important for generating the lipid signaling molecule lysophosphatidic acid (LPA), which is a potent mitogen, which facilitates cell proliferation and migration, neurite retraction, platelet aggregation, smooth muscle contraction, actin stress formation and cytokine and chemokine secretion. ATX has been found to catalyze the formation of cyclic phosphatidic acid (cPA), which have antitumor role by antimitogenic regulation of cell cycle, inhibition of cancer invasion and metastasis. LPA receptors and ATX are upregulated in numerous cancer cell types and show expression patterns that correlate with tumor cell invasiveness. Thus, Autotaxin has recently emerged as an attractive target for the development of anti-cancer chemotherapeutics. In addition, Serum ATX activity was found to be enhanced in relation to hepatic fibrosis in chronic liver disease due to hepatitis virus C infection.
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TMPY-00463 | ENPP2 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
ENPP2 (Ectonucleotide pyrophosphatase/phosphodiesterase family member 2), also referred as Autotaxin, is a secreted enzyme encoded by the ENPP2 gene. This gene product stimulates the motility of tumor cells, has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The Autotaxin protein is important for generating the lipid signaling molecule lysophosphatidic acid (LPA), which is a potent mitogen, which facilitates cell proliferation and migration, neurite retraction, platelet aggregation, smooth muscle contraction, actin stress formation and cytokine and chemokine secretion. ATX has been found to catalyze the formation of cyclic phosphatidic acid (cPA), which have antitumor role by antimitogenic regulation of cell cycle, inhibition of cancer invasion and metastasis. LPA receptors and ATX are upregulated in numerous cancer cell types and show expression patterns that correlate with tumor cell invasiveness. Thus, Autotaxin has recently emerged as an attractive target for the development of anti-cancer chemotherapeutics. In addition, Serum ATX activity was found to be enhanced in relation to hepatic fibrosis in chronic liver disease due to hepatitis virus C infection.
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TMPY-03577 | Pleiotrophin/PTN Protein, Mouse, Recombinant | Mouse | Baculovirus-Insect Cells | ||
HB-GAM belongs to the pleiotrophin family. During embryonic and early postnatal development, HB-GAM is expressed in the central and peripheral nervous system and also in several non-neural tissues, notably lung, kidney, gut and bone. While in the adult central nervous system, it is expressed in an activity-dependent manner in the hippocampus where it can suppress long term potentiation induction. HB-GAM has a low expression in other areas of the adult brain, but it can be induced by ischemic insults, or targeted neuronal damage in the entorhinal cortex or in the substantia nigra pars compacta. It is structurally related to midkine and retinoic acid induced heparin-binding protein and has a high affinity for heparin. HB-GAM binds anaplastic lymphoma kinase (ALK) which induces MAPK pathway activation, an important step in the anti-apoptotic signaling of PTN and regulation of cell proliferation. It also functions as a secreted growth factor and induces neurite outgrowth and which is mitogenic for fibroblasts, epithelial, and endothelial cells.
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TMPY-00834 | IGF1R/CD221 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The insulin-like growth factor-1 receptor (IGF1R) is a transmembrane tyrosine kinase involved in several biological processes including cell proliferation, differentiation, DNA repair, and cell survival. This a disulfide-linked heterotetrameric transmembrane protein consisting of two α and two β subunits, and among which, the α subunit is extracellular while the β subunit has an extracellular domain, a transmembrane domain, and a cytoplasmic tyrosine kinase domain. The IGF1R signaling pathway is activated in the mammalian nervous system from the early developmental stages. Its major effect on developing neural cells is to promote their growth and survival. This pathway can integrate its action with signaling pathways of growth and morphogenetic factors that induce cell fate specification and selective expansion of specified neural cell subsets. Modulation of cell migration is another possible role that IGF1R activation may play in neurogenesis. In the mature brain, IGF-I binding sites have been found in different regions of the brain, and multiple reports confirmed a strong neuroprotective action of the IGF-IR against different pro-apoptotic insults. IGF1R is an important signaling molecule in cancer cells and plays an essential role in the establishment and maintenance of the transformed phenotype. Inhibition of IGF1R signaling thus appears to be a promising strategy to interfere with the growth and survival of cancer cells. IGF1R is frequently overexpressed by tumors and mediates proliferation and apoptosis protection. IGF signaling also influences hypoxia signaling, protease secretion, tumor cell motility, and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, IGF1R is now an attractive anti-cancer treatment target.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02219 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Non-structural/NS1 Protein (His) | H1N1 | E. coli | ||
The NS1 Influenza protein is created by the internal protein-encoding, linear negative-sense, single-stranded RNA, NS gene segment and which also codes for the nuclear export protein or NEP, formerly referred to as the NS2 protein, which mediates the export of vRNPs. The non-structural (NS1) protein is found in Influenzavirus A, Influenzavirus B, and Influenzavirus C. The non-structural (NS1) protein of the highly pathogenic avian H5N1 viruses circulating in poultry and waterfowl in Southeast Asia is currently believed to be responsible for the enhanced virulence of the strain. The Non-structural (NS1) protein of influenza A virus is a non-essential virulence factor that has multiple accessory functions during viral infection. The major role ascribed to NS1 has been its inhibition of host immune responses, especially the limitation of both interferon (IFN) production and the antiviral effects of IFN-induced proteins, such as dsRNA-dependent protein kinase R (PKR) and 2'5'-oligoadenylate synthetase (OAS)/RNase L. Non-structural (NS1) protein is a non-structural protein of the influenza A virus, which could only be expressed when cells are infected. The effect of NS1 protein on the host cell is still not clear. Not only could NS1 remarkably affect metabolism, but it could also slow down cell proliferation by blocking the cell cycle. Non-structural (NS1) protein may lead to the development of novel antiviral drugs, and the use of oncolytic influenza A viruses as potential anti-cancer agents.
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TMPY-03547 | IL-10 Protein, Human, Recombinant | Human | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01107 | TIMP-1 Protein, Human, Recombinant | Human | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPY-01845 | IL-10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05064 | IL-10 Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02820 | SDF-1 Protein, Human, Recombinant (isoform a) | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-00740 | SDF-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-02591 | SDF-1 Protein, Human, Recombinant | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPH-02590 | COL4A2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.
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TMPK-00455 | IGF1R/CD221 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
The type 1 IGF receptor (IGF1R) is a transmembrane tyrosine kinase that is frequently overexpressed by tumours, and mediates proliferation and apoptosis protection. IGF signalling also influences hypoxia signalling, protease secretion, tumour cell motility and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, the IGF1R is now an attractive anti-cancer treatment target.
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TMPK-00658 | IGF1R/CD221 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
The type 1 IGF receptor (IGF1R) is a transmembrane tyrosine kinase that is frequently overexpressed by tumours, and mediates proliferation and apoptosis protection. IGF signalling also influences hypoxia signalling, protease secretion, tumour cell motility and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, the IGF1R is now an attractive anti-cancer treatment target.
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TMPK-00314 | B7-H3 (4Ig) /B7-H3b Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
B7-H3, a member of the B7 family of immunomodulatory molecules, is overexpressed in a wide range of solid cancers.B7-H3 binds to activated T cells via an as yet unidentified receptor. In assays using sub-optimal amount so anti-CD3 stimulation, 2Ig‑B7‑H3 enhances T cell proliferation, T cell interferon-gamma (IFN-gamma) production, and cytotoxic T cells induction.
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TMPK-01017 | B7-H3 Protein, Human, Recombinant (aa 29-245, hFc) | Human | HEK293 | ||
B7-H3, a member of the B7 family of immunomodulatory molecules, is overexpressed in a wide range of solid cancers.B7-H3 binds to activated T cells via an as yet unidentified receptor. In assays using sub-optimal amount so anti-CD3 stimulation, 2Ig‑B7‑H3 enhances T cell proliferation, T cell interferon-gamma (IFN-gamma) production, and cytotoxic T cells induction.
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TMPK-00456 | IGF1R/CD221 Protein, Human, Recombinant (aa 31-932, His & Avi), Biotinylated | Human | HEK293 | ||
The type 1 IGF receptor (IGF1R) is a transmembrane tyrosine kinase that is frequently overexpressed by tumours, and mediates proliferation and apoptosis protection. IGF signalling also influences hypoxia signalling, protease secretion, tumour cell motility and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, the IGF1R is now an attractive anti-cancer treatment target.
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TMPK-01016 | B7-H3 Protein, Human, Recombinant (hFc), FITC-Labeled | Human | HEK293 | ||
B7-H3, a member of the B7 family of immunomodulatory molecules, is overexpressed in a wide range of solid cancers.B7-H3 binds to activated T cells via an as yet unidentified receptor. In assays using sub-optimal amount so anti-CD3 stimulation, 2Ig‑B7‑H3 enhances T cell proliferation, T cell interferon-gamma (IFN-gamma) production, and cytotoxic T cells induction.
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TMPK-01018 | B7-H3 Protein, Human, Recombinant (aa 29-245, His) | Human | HEK293 | ||
B7-H3, a member of the B7 family of immunomodulatory molecules, is overexpressed in a wide range of solid cancers.B7-H3 binds to activated T cells via an as yet unidentified receptor. In assays using sub-optimal amount so anti-CD3 stimulation, 2Ig‑B7‑H3 enhances T cell proliferation, T cell interferon-gamma (IFN-gamma) production, and cytotoxic T cells induction.
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TMPK-00315 | B7-H3 (4Ig) /B7-H3b Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
B7-H3, a member of the B7 family of immunomodulatory molecules, is overexpressed in a wide range of solid cancers.B7-H3 binds to activated T cells via an as yet unidentified receptor. In assays using sub-optimal amount so anti-CD3 stimulation, 2Ig‑B7‑H3 enhances T cell proliferation, T cell interferon-gamma (IFN-gamma) production, and cytotoxic T cells induction.
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TMPY-05836 | IL-1 alpha/IL-1A Protein, Rat, Recombinant | Rat | E. coli | ||
IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPK-01137 | FAM3D Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The physiological homeostasis of gut mucosal barrier is maintained by both genetic and environmental factors and its impairment leads to pathogenesis such as inflammatory bowel disease. A cytokine like molecule, FAM3D (mouse Fam3D), is highly expressed in mouse gastrointestinal tract. Here, we demonstrate that deficiency in Fam3D is associated with impaired integrity of colonic mucosa, increased epithelial hyper-proliferation, reduced anti-microbial peptide production and increased sensitivity to chemically induced colitis associated with high incidence of cancer.
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TMPY-03341 | ASF1B Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
The histone chaperone anti-silencing factor 1a (ASF1a) interacts with MDC1 and is recruited to sites of DSBs to facilitate the interaction of phospho-ATM with MDC1 and phosphorylation of MDC1, which are required for the recruitment of RNF8/RNF168 histone ubiquitin ligases. Thus, ASF1a deficiency reduces histone ubiquitination at DSBs, decreasing the recruitment of 53BP1, and decreases NHEJ, rendering cells more sensitive to DSBs. This role of ASF1a in DSB repair cannot be provided by the closely related ASF1b and does not require its histone chaperone activity. Homozygous deletion of ASF1A is seen in 10%-15% of certain cancers, suggesting that loss of NHEJ may be selected in some malignancies and that the deletion can be used as a molecular biomarker for cancers susceptible to radiotherapy or to DSB-inducing chemotherapy. Anti-silencing function 1 (ASF1) is a histone H3-H4 chaperone involved in DNA replication and repair, and transcriptional regulation. Here, we identify ASF1B, the mammalian paralog to ASF1, as a proliferation-inducing histone chaperone in human β-cells. Overexpression of ASF1B led to distinct transcriptional signatures consistent with increased cellular proliferation and reduced cellular death.
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TMPH-02439 | CD40L Protein, Rhesus macaque, Recombinant (His) | Rhesus | E. coli | ||
Cytokine that acts as a ligand to CD40/TNFRSF5. Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B. Induces the activation of kinases MAPK8 and PAK2 in T-cells. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4. Involved in immunoglobulin class switching.; Acts as a ligand for integrins, specifically ITGA5:ITGB1 and ITGAV:ITGB3; both integrins and the CD40 receptor are required for activation of CD40-CD40LG signaling, which have cell-type dependent effects, such as B-cell activation, NF-kappa-B signaling and anti-apoptotic signaling.
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TMPY-04916 | RGMB Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
RGMB was knocked down in breast cancer cells by way of an anti-RGMB ribozyme transgene. Knockdown of RGMB resulted in enhanced capacities of proliferation, adhesion, and migration in breast cancer cells. Further investigations demonstrated RGMB knockdown resulted in a reduced expression and activity of Caspase-3, accompanied with better survival in RGMB knockdown cells under serum starvation, which might be induced by its repression on MAPK JNK pathway. That RGMB may act as a negative regulator in breast cancer through BMP signaling.
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TMPY-04906 | RGMB Protein, Human, Recombinant (His) | Human | HEK293 | ||
RGMB was knocked down in breast cancer cells by way of an anti-RGMB ribozyme transgene. Knockdown of RGMB resulted in enhanced capacities of proliferation, adhesion, and migration in breast cancer cells. Further investigations demonstrated RGMB knockdown resulted in a reduced expression and activity of Caspase-3, accompanied with better survival in RGMB knockdown cells under serum starvation, which might be induced by its repression on MAPK JNK pathway. That RGMB may act as a negative regulator in breast cancer through BMP signaling.
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TMPJ-00766 | ANXA1 Protein, Human, Recombinant | Human | E. coli | ||
Annexin A1 is the first characterized member of the annexin family of proteins and is able to bind to cellular membranes in a calcium-dependent manner, promoting membrane fusion and endocytosis. Annexin A1 has anti-inflammatory properties and inhibits phospholipase A2 activity. Annexin A1 also has roles in many diverse cellular functions, such as membrane aggregation, inflammation, phagocytosis, proliferation, apoptosis, and tumorigenesis and cancer development. ANXA1 is strongly expressed on the cell membrane and occasionally in the cytoplasm of tumor cells in 97% of samples from patients with hairy cell leukemia.
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TMPY-03416 | TNFAIP8 Protein, Human, Recombinant (His) | Human | E. coli | ||
Tumor necrosis factor (TNF)-alpha-induced protein 8 (TNFAIP8) family is a newly identified protein with vital roles in maintaining immune homeostasis. Tumor necrosis factor-alpha-inducible protein 8 (TNFAIP8) is a TNF-alpha inducible anti-apoptotic protein with multiple roles in tumor growth and survival. by the creation of cellular autophagy events, TNFAIP8 promotes cell survival and drug resistance in prostate cancer cells. TNFAIP8 regulates Hippo pathway through interacting with LATS1 to promote cell proliferation and invasion in lung cancer. TNFAIP8 may serve as a candidate biomarker for poor prognosis and a target for new therapies.
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TMPJ-00439 | BTNL6 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Butyrophilin-like 6 (BTNL6) is a member of the BTN/MOG Ig-superfamily and functions with BTNL1 as a regulator of immune cell proliferation. The Btnl6 gene is found only in mice. BTNL6 expression is coordinated as a heteromeric protein with BTNL1, and the presence of this complex is correlated with expansion of gamma δ T cells, especially those containing V gamma 7Vδ4 TCR. Btnl6 shows striking sequence similarity to Skint1; is also largely restricted to an epithelial tissue (the small intestine) replete with T cells. Our in-house studies showed BTNL6 co-inhibited anti-CD3 induced IL-2 secretion on CD3+ cells.
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TMPH-03081 | ACE2 Protein, Paguma larvata, Recombinant (hFc) | Paguma larvata | HEK293 | ||
Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity.; (Microbial infection) Acts as a receptor for human coronavirus SARS.
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TMPY-06329 | 4-1BB/CD137/TNFRSF9 Protein, Mouse, Recombinant (aa 1-211, His&AVI), Biotinylated | Mouse | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-05105 | 4-1BB/CD137/TNFRSF9 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-04720 | 4-1BB/CD137/TNFRSF9 Protein, Cynomolgus, Rhesus, Recombinant (His) | Cynomolgus,Rhesus | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-06794 | 4-1BB/CD137/TNFRSF9 Protein, Mouse, Recombinant (aa 1-187, His & Avi), Biotinylated | Mouse | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPY-06279 | 4-1BB/CD137/TNFRSF9 Protein, Mouse, Recombinant (His), Biotinylated | Mouse | HEK293 | ||
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+and CD8+T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials. Soluble forms of CD137 (sCD137) are generated by differential splicing. sCD137 can bind to CD137 ligand to antagonize the costimulatory activities of the membrane-bound CD137 and reduce T cell proliferation and IL-2 secretion.Cancer ImmunotherapyCo-stimulatory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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