目录号 | 产品详情 | 靶点 | |
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T3593 | Src | ||
Src Inhibitor 1 (Src Kinase Inhibitor 1) 是一种选择性的、高效的、ATP-竞争性的双位点 Src 酪氨酸激酶抑制剂,能够抑制 Src (IC50:44 nM) 和 Lck (IC50:88 nM)。 | |||
T13000 | Others Src | ||
Src Inhibitor 3 是一种有效的 c-terminal Src 激酶抑制剂(CSK HTRF 中 IC50 <3 nM,Caliper 中 IC50 <4 nM)。 Src Inhibitor 3 增加由 T 细胞受体信号传导诱导的 T 细胞增殖。 | |||
TP2289L | Others | ||
RR-src acetate 是一种合成肽,来源于 pp60src 中磷酸化位点周围的氨基酸序列。 | |||
TP2137L | Others | ||
pp60 c-src (521-533) (phosphorylated) acetate 是粘着斑形成和细胞扩散的调节剂。它还调节细胞运动,是由促运动透明质酸受体 RHAMM 触发的信号通路中的关键成分。 | |||
T11745 | Src | ||
KB SRC 4 是一种具有选择性和高效性的 c-Src 抑制剂,具有抗肿瘤活性,可抑制癌细胞生长。 | |||
T39149 | |||
Src Optimal Peptide Substrate, a highly specific substrate of Src, serves as a reliable indicator of Src activity. It enables accurate assessment of Src kinase function. | |||
TP2289 | Others | ||
Tyrosine kinase substrate peptide | |||
T39185 | |||
pp60 (v-SRC) Autophosphorylation Site, Phosphorylated is a phosphorylated peptide derived from an EGFR substrate. It serves as a valuable tool for quantifying phosphorylated substrates in screening EGFR Kinase inhibitors. | |||
T1811 | Src | ||
WH-4-023 (Dual LCK/SRC inhibitor) 是选择性Lck 和Src 抑制剂,它们的 IC50 分别为 2 nM、6 nM,对p38α 和 KDR 作用效果稍弱。 | |||
T13061 | Others | ||
T338C Src-IN-1 is a potent mutant-Src T338C inhibitor(T338C,IC50=111 nM relative to WT c-Src (10-fold increase)). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04384 | Src Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Proto-oncogene tyrosine-protein kinase SRC is a hydrophobic protein belonging to the SRC family kinase including nine members that is a family of non-receptor tyrosine kinases. SRC protein may exist in different forms: C-SRC and V-SRC. C-SRC is only activated under certain circumstances where it is required such as growth factor signaling, while V-SRC is constitutively active as opposed to normal SRC (C-SRC). Thus, V-SRC is an instructive example of an oncogene protein kinase whereas C-SRC is a proto-oncogene protein kinase. Inhibition of SRC with NR2A tyrosine phosphorylation mediated by PSD-95 may contribute to the lithium-induced downregulation of NMDA receptor function and provide neuroprotection against excitotoxicity.
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TMPY-04434 | Src Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
Proto-oncogene tyrosine-protein kinase SRC is a hydrophobic protein belonging to the SRC family kinase including nine members that is a family of non-receptor tyrosine kinases. SRC protein may exist in different forms: C-SRC and V-SRC. C-SRC is only activated under certain circumstances where it is required such as growth factor signaling, while V-SRC is constitutively active as opposed to normal SRC (C-SRC). Thus, V-SRC is an instructive example of an oncogene protein kinase whereas C-SRC is a proto-oncogene protein kinase. Inhibition of SRC with NR2A tyrosine phosphorylation mediated by PSD-95 may contribute to the lithium-induced downregulation of NMDA receptor function and provide neuroprotection against excitotoxicity.
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TMPY-04383 | CSK Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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TMPH-01977 | Src Protein, Human, Recombinant (His) | Human | E. coli | ||
Src Protein, Human, Recombinant (His) is expressed in E. coli.
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TMPY-04760 | CSK Protein, Mouse, Recombinant | Mouse | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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TMPY-04444 | CSK Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.References
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TMPY-04388 | BLK Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Tyrosine-protein kinase Blk, also known as B lymphocyte kinase, p55-Blk and BLK, is a member of theprotein kinase superfamily, Tyr protein kinase family and SRC subfamily. BLK / p55-Blk is expressed in lymphatic organs, pancreatic islets, Leydig cells, striate ducts of salivary glands and hair follicles. BLK / p55-Blk is a src-family protein tyrosine kinase specifically expressed in B-lineage cells of mice. The early onset of Blk expression during B-cell development in the bone marrow and the high expression levels of Blk in mature B cells suggest a possible important role of Blk in B-cell physiology. It is a modulator of beta-cells function, acting through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. Defects in BLK are a cause of maturity-onset diabetes of the young type 11 which is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
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TMPY-04391 | Lyn Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Tyrosine-protein kinase Lyn is a member of the Src family of protein tyrosine kinases, which is mainly expressed in hematopoietic cells, in neural tissues liver, and adipose tissue. Tyrosine-protein kinase Lyn has many functions. Lyn kinase may downregulate the expression of stem cell growth factor receptor (KIT). Lyn kinase Acts as an effector of EpoR (erythropoietin receptor) in controlling KIT expression and may play a central role in erythroid differentiation during the switch between proliferation and maturation. Lyn kinase also acts as a positive regulator of cell movement while negatively regulating adhesion to stromal cells by inhibiting the ICAM-1-binding activity of beta-2 integrins. Lyn kinase relays suppressing signals from the chemokine receptor CXCR4 to beta-2 integrin LFA-1 in hematopoietic precursors. This kinase is involved in the induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. In a word, Lyn kinase functions primarily as a negative regulator, but can also function as an activator, depending on the context. Tyrosine-protein kinase Lyn is Required for the initiation of the B-cell response, but also its down-regulation and termination. It also plays an important role in the regulation of B-cell differentiation, proliferation, survival, and apoptosis, and is important for immune self-tolerance. It has been reported that Lyn kinase plays a role in the inflammatory response to bacterial lipopolysaccharide. Lyn kinase Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils, and eosinophils.
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TMPY-04411 | YES1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Proto-oncogene tyrosine-protein kinase Yes, also known as Proto-oncogene c-Yes, p61-Yes and YES1, is a cytoplasm protein that belongs to the protein kinase superfamily, Tyr protein kinase family and SRC subfamily. YES1 / c-Yes contains one protein kinase domain, one SH2 domain and one SH3 domain. It is thought that the subcellular distribution of Src-family tyrosine kinases, including c-Yes binding to the cellular membrane, is membranous and/or cytoplasmic. YES1 / c-Yes protein tyrosine kinase is known to be related to malignant transformation. YES1 / c-Yes and c-Src are the two most closely related members of the Src family of nonreceptor tyrosine kinases. Although there is much evidence to support redundancy in signaling between these two kinases. YES1 / c-Yes promotes the formation of the tight junction by phosphorylating occludin, while c-Src signaling downregulates occludin formation in a Raf-1 dependent manner. YES1 / c-Yes has tyrosine kinase activity. It promotes infectivity of Neisseria gonorrhoeae in epithelial cells by phosphorylating MCP / CD46.
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TMPJ-00778 | HER2/ERBB2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.
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TMPY-03835 | CDCP1 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
CDCP1 contains three extracellular CUB domains. It is a putative stem cell marker that is highly expressed in some human cancer cells and both, typical and atypical (cancerous) colons. It interacts with CDH2/N-cadherin, CDH3/P-cadherin, SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. It also interacts with SRC and PRKCG/protein kinase C gamma. CDCP1 is taken as a key regulator of EGF/EGFR-induced cell migration. It has been shown that signaling via EGF/EGFR induces migration of ovarian cancer Caov3 and OVCA420 cells with concomitant up-regulation of CDCP1 mRNA and protein. Consistent with a role in cell migration CDCP1 relocates from cell-cell junctions to punctate structures on filopodia after activation of EGFR. It may be involved in cell adhesion and cell matrix association. It also may play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. It has been taken as a novel marker for leukemia diagnosis and immature hematopoietic stem cell subsets.
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TMPY-04298 | CDCP1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CDCP1 contains three extracellular CUB domains. It is a putative stem cell marker that is highly expressed in some human cancer cells and both, typical and atypical (cancerous) colons. It interacts with CDH2/N-cadherin, CDH3/P-cadherin, SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1. It also interacts with SRC and PRKCG/protein kinase C gamma. CDCP1 is taken as a key regulator of EGF/EGFR-induced cell migration. It has been shown that signaling via EGF/EGFR induces migration of ovarian cancer Caov3 and OVCA420 cells with concomitant up-regulation of CDCP1 mRNA and protein. Consistent with a role in cell migration CDCP1 relocates from cell-cell junctions to punctate structures on filopodia after activation of EGFR. It may be involved in cell adhesion and cell matrix association. It also may play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. It has been taken as a novel marker for leukemia diagnosis and immature hematopoietic stem cell subsets.
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TMPY-05308 | CD45 Protein, Human, Recombinant (aa 1-529, His) | Human | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexes or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.
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TMPY-05748 | CD45 Protein, Human, Recombinant (aa 26-577, His) | Human | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexes or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.
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TMPY-05566 | Siglec-2/CD22 Protein, Human, Recombinant (His, Solution) | Human | HEK293 | ||
CD22 is a member of the immunoglobulin superfamily, SIGLEC family of lectins. It is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD+. CD22 serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. In addition to its potential role as a mediator of intercellular interactions, signal transduction through CD22 can activate B cells and modulate antigen receptor signaling in vitro. The phenotype of CD22-deficient mice suggests that CD22 is primarily involved in the generation of mature B cells within the bone marrow, blood, and marginal zones of lymphoid tissues. CD22 recruits the tyrosine phosphatase Src homology 2 domain-containing phosphatase 1 (SHP-1) to immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and inhibits B-cell receptor (BCR)-induced Ca2+ signaling on normal B cells. CD22 interacts specifically with ligands carrying alpha2-6-linked sialic acids. As an inhibitory coreceptor of the B-cell receptor (BCR), CD22 plays a critical role in establishing signalling thresholds for B-cell activation. Like other coreceptors, the ability of CD22 to modulate B-cell signalling is critically dependent upon its proximity to the BCR, and this in turn is governed by the binding of its extracellular domain to alpha2,6-linked sialic acid ligands. However, genetic studies in mice reveal that some CD22 functions are regulated by ligand binding, whereas other functions are ligand-independent and may only require expression of an intact CD22 cytoplasmic domain at the B-cell surface. CD19 regulates CD22 phosphorylation by augmenting Lyn kinase activity, while CD22 inhibits CD19 phosphorylation via SHP-1.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04083 | Siglec-2/CD22 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CD22 is a member of the immunoglobulin superfamily, SIGLEC family of lectins. It is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD+. CD22 serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. In addition to its potential role as a mediator of intercellular interactions, signal transduction through CD22 can activate B cells and modulate antigen receptor signaling in vitro. The phenotype of CD22-deficient mice suggests that CD22 is primarily involved in the generation of mature B cells within the bone marrow, blood, and marginal zones of lymphoid tissues. CD22 recruits the tyrosine phosphatase Src homology 2 domain-containing phosphatase 1 (SHP-1) to immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and inhibits B-cell receptor (BCR)-induced Ca2+ signaling on normal B cells. CD22 interacts specifically with ligands carrying alpha2-6-linked sialic acids. As an inhibitory coreceptor of the B-cell receptor (BCR), CD22 plays a critical role in establishing signalling thresholds for B-cell activation. Like other coreceptors, the ability of CD22 to modulate B-cell signalling is critically dependent upon its proximity to the BCR, and this in turn is governed by the binding of its extracellular domain to alpha2,6-linked sialic acid ligands. However, genetic studies in mice reveal that some CD22 functions are regulated by ligand binding, whereas other functions are ligand-independent and may only require expression of an intact CD22 cytoplasmic domain at the B-cell surface. CD19 regulates CD22 phosphorylation by augmenting Lyn kinase activity, while CD22 inhibits CD19 phosphorylation via SHP-1.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02034 | Siglec-2/CD22 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD22 is a member of the immunoglobulin superfamily, SIGLEC family of lectins. It is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD+. CD22 serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. In addition to its potential role as a mediator of intercellular interactions, signal transduction through CD22 can activate B cells and modulate antigen receptor signaling in vitro. The phenotype of CD22-deficient mice suggests that CD22 is primarily involved in the generation of mature B cells within the bone marrow, blood, and marginal zones of lymphoid tissues. CD22 recruits the tyrosine phosphatase Src homology 2 domain-containing phosphatase 1 (SHP-1) to immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and inhibits B-cell receptor (BCR)-induced Ca2+ signaling on normal B cells. CD22 interacts specifically with ligands carrying alpha2-6-linked sialic acids. As an inhibitory coreceptor of the B-cell receptor (BCR), CD22 plays a critical role in establishing signalling thresholds for B-cell activation. Like other coreceptors, the ability of CD22 to modulate B-cell signalling is critically dependent upon its proximity to the BCR, and this in turn is governed by the binding of its extracellular domain to alpha2,6-linked sialic acid ligands. However, genetic studies in mice reveal that some CD22 functions are regulated by ligand binding, whereas other functions are ligand-independent and may only require expression of an intact CD22 cytoplasmic domain at the B-cell surface. CD19 regulates CD22 phosphorylation by augmenting Lyn kinase activity, while CD22 inhibits CD19 phosphorylation via SHP-1.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04340 | Mucin-1/MUC1 Protein, Human, Recombinant | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02005 | Mucin-1/MUC1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05201 | Siglec-2/CD22 Protein, Human, Recombinant | Human | HEK293 | ||
CD22 is a member of the immunoglobulin superfamily, SIGLEC family of lectins. It is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD+. CD22 serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. In addition to its potential role as a mediator of intercellular interactions, signal transduction through CD22 can activate B cells and modulate antigen receptor signaling in vitro. The phenotype of CD22-deficient mice suggests that CD22 is primarily involved in the generation of mature B cells within the bone marrow, blood, and marginal zones of lymphoid tissues. CD22 recruits the tyrosine phosphatase Src homology 2 domain-containing phosphatase 1 (SHP-1) to immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and inhibits B-cell receptor (BCR)-induced Ca2+ signaling on normal B cells. CD22 interacts specifically with ligands carrying alpha2-6-linked sialic acids. As an inhibitory coreceptor of the B-cell receptor (BCR), CD22 plays a critical role in establishing signalling thresholds for B-cell activation. Like other coreceptors, the ability of CD22 to modulate B-cell signalling is critically dependent upon its proximity to the BCR, and this in turn is governed by the binding of its extracellular domain to alpha2,6-linked sialic acid ligands. However, genetic studies in mice reveal that some CD22 functions are regulated by ligand binding, whereas other functions are ligand-independent and may only require expression of an intact CD22 cytoplasmic domain at the B-cell surface. CD19 regulates CD22 phosphorylation by augmenting Lyn kinase activity, while CD22 inhibits CD19 phosphorylation via SHP-1.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-00375 | IL-8/CXCL8 Protein, Chicken, Recombinant (His) | Chicken | E. coli | ||
May be an autocrine factor that promotes the growth of fibroblasts and is involved in the neoplastic transformation of fibroblasts by v-Src. Chemotactic for peripheral blood mononuclear cells as well as for heterophils.
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TMPH-02278 | PTPN5 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors.
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TMPH-00376 | IL-8/CXCL8 Protein, Chicken, Recombinant | Chicken | E. coli | ||
May be an autocrine factor that promotes the growth of fibroblasts and is involved in the neoplastic transformation of fibroblasts by v-Src. Chemotactic for peripheral blood mononuclear cells as well as for heterophils.
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TMPY-02511 | PTP alpha/PTPRA Protein, Human, Recombinant (aa 174-793, His & GST) | Human | Baculovirus-Insect Cells | ||
PTPRA is reported to be involved in cancer development and progression through activating the Src family kinase (SFK) signaling pathways. The higher PTPRA level was associated with worse prognosis of SCC patients and PTPRA could promote the cell cycle progression through stimulating the c-Src signaling pathways. The PTPRA gene, which encodes the protein RPTP-alpha, is critical to neurodevelopment. Previous linkage studies, genome-wide association studies, controlled expression analyses and animal models support an association with both schizophrenia and autism spectrum disorders, both of which share a substantial portion of genetic risks.
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TMPJ-00712 | MPZL1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Myelin protein zero-like protein 1(MPZL1) is encoded by the MPZL1 gene, which is a single-pass type I membrane protein. It is widely expressed with highest levels in heart, placenta, kidney and pancreas. As cell surface receptor, it involved in signal transduction processes. MPZL1 recruits PTPN11/SHP-2 to the cell membrane and subsequently activate/phosphorylate Src kinase at Tyr426, promoting phosphorylation of cortactin and migration of HCC cells. MPZL1also is a major receptor for concanavalin-A (ConA) and involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases.
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TMPH-01581 | KRT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.
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TMPH-00228 | BMP-4 Protein, Bovine, Recombinant (GST) | Bovine | E. coli | ||
Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt, or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response.
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TMPJ-00185 | CD20 Protein, Human, Recombinant (His & Flag) | Human | Human Cells | ||
CD20 is a 33-37 kDa non-glycosylated protein expressed on the surface of normal and malignant B lymphocytes, and belongs to the MS4A (membrane-spanning 4-domain family A) protein family. CD20 protein consists of four hydrophobic transmembrane domains, one intracellular and two extracellular domains (large and small loops) with both N- and C- termini residing within the cytosol. CD20 is also known to be physically coupled to major histocompatibility complex class II (MHCII), CD40 molecule, BCR, and the C-terminal src kinase-binding protein (CBP) that interacts with Src kinases such as LYN, FYN, and LCK. CD20 deficiency resulted in a reduced number of circulating memory B cells, reduced isotype switching of Ig, and decreased IgG antibody levels. In agreement with this observation, challenging the patient’s primary B cells in vitro using T-dependent and Tindependent antigens led to the normal proliferation and secretion of IgM but reduced production of IgG.
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TMPH-01017 | BMP-4 Protein, Human, Recombinant (His) | Human | E. coli | ||
Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis. Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt, or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response.
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TMPK-00499 | HGFR/c-Met Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
c-Met, also called tyrosine-protein kinase Met or hepatocyte growth factor receptor (HGFR), is a protein that in humans is encoded by the MET gene.The protein possesses tyrosine kinase activity. The primary single chain precursor protein is post-translationally cleaved to produce the alpha and beta subunits, which are disulfide linked to form the mature receptor. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.
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TMPJ-00184 | CD20 Protein, Human, Recombinant (Flag) | Human | Human Cells | ||
CD20 is a 33-37 kDa non-glycosylated protein expressed on the surface of normal and malignant B lymphocytes, and belongs to the MS4A (membrane-spanning 4-domain family A) protein family. CD20 protein consists of four hydrophobic transmembrane domains, one intracellular and two extracellular domains (large and small loops) with both N- and C- termini residing within the cytosol. CD20 is also known to be physically coupled to major histocompatibility complex class II (MHCII), CD40 molecule, BCR, and the C-terminal src kinase-binding protein (CBP) that interacts with Src kinases such as LYN, FYN, and LCK. CD20 deficiency resulted in a reduced number of circulating memory B cells, reduced isotype switching of Ig, and decreased IgG antibody levels. In agreement with this observation, challenging the patient’s primary B cells in vitro using T-dependent and Tindependent antigens led to the normal proliferation and secretion of IgM but reduced production of IgG.
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TMPK-00423 | CD45 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
PTPRC (also known as CD45),T cells require the protein tyrosine phosphatase CD45 to detect and respond to antigen because it activates the Src family kinase Lck, which phosphorylates the T cell antigen receptor (TCR) complex. CD45 ativates Lck by opposing the negative regulatory kinase Csk. Paradoxically, CD45 has also been implicated in suppressing TCR signaling by dephosphorylating the same signaling motifs within the TCR complex upon which Lck acts.
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TMPK-00447 | CD45 Protein, Human, Recombinant (aa 26-577, hFc) | Human | HEK293 | ||
PTPRC (also known as CD45),T cells require the protein tyrosine phosphatase CD45 to detect and respond to antigen because it activates the Src family kinase Lck, which phosphorylates the T cell antigen receptor (TCR) complex. CD45 ativates Lck by opposing the negative regulatory kinase Csk. Paradoxically, CD45 has also been implicated in suppressing TCR signaling by dephosphorylating the same signaling motifs within the TCR complex upon which Lck acts.
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TMPK-00424 | CD45 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
PTPRC (also known as CD45),T cells require the protein tyrosine phosphatase CD45 to detect and respond to antigen because it activates the Src family kinase Lck, which phosphorylates the T cell antigen receptor (TCR) complex. CD45 ativates Lck by opposing the negative regulatory kinase Csk. Paradoxically, CD45 has also been implicated in suppressing TCR signaling by dephosphorylating the same signaling motifs within the TCR complex upon which Lck acts.
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TMPK-00457 | HGFR/c-Met Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
c-Met, also called tyrosine-protein kinase Met or hepatocyte growth factor receptor (HGFR), is a protein that in humans is encoded by the MET gene.The protein possesses tyrosine kinase activity. The primary single chain precursor protein is post-translationally cleaved to produce the alpha and beta subunits, which are disulfide linked to form the mature receptor. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1.
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TMPY-02761 | Rack1 Protein, Human, Recombinant (His & MBP) | Human | E. coli | ||
The scaffolding protein, Rack1, is a seven-WD-domain-containing protein that has been implicated in binding to integrin beta subunit cytoplasmic domains and to members of two kinase families (src and protein kinase C, PKC) that mediate integrin bidirectional signaling.Rack1 may link protein kinase C directly to integrins and participate in the regulation of integrin functions.Rack1 regulates the localization of an essential PCP protein and acts as a molecular switch to promote PCP signaling.
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TMPY-03510 | Cbl-c Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
CBL proteins, such as Cbl-c, are phosphorylated upon activation of a variety of receptors that signal via protein tyrosine kinases. Through interactions with proteins containing SRC homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling. Cbl-c is a member of the Cbl family of E3 ubiquitin ligases. Expression of Cbl-c gene may be restricted to epithelial cells, and alternatively spliced transcript variants encoding multiple isoforms have been observed for Cbl-c gene.
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TMPY-03296 | SHP-1 Protein, Mouse, Recombinant (aa 207-597, His & GST) | Mouse | Baculovirus-Insect Cells | ||
PTPN6 is an enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of PTPN6 contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of PTPN6 with its substrates. PTPN6 is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. It has been shown that PTPN6 interacts with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling.
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TMPJ-00396 | SEMA4D Protein, Human, Recombinant (aa 22-734, His) | Human | Human Cells | ||
Semaphorin-4D is also known as A8,BB18, GR3, CD100. Semaphorin-4D belongs to the semaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domain. It is the cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. It promotes the migration of cerebellar granule cells and of endothelial cells, regulates dendrite and axon branching and morphogenesis. Semaphorin-4D Plays a role in the immune system; Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.
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TMPJ-00326 | CD122/IL2RB Protein, Human, Recombinant (aa 27-239, His & Avi), Biotinylated | Human | Human Cells | ||
Human IL-2RB, also known asinterleukin-2 receptor subunit beta,is the receptor for interleukin-2. IL2 receptor complex is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. IL2 receptor complex has three forms with respect to ability to bind IL2. IL-2RB is belonged to a type I membrane protein,and has a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. IL-2RB is the subunit critical for receptor-mediated signaling via physically or functionally coupling to other signaling molecules, such as the Jak-STAT and Src-family protein tyrosine kinase although it lacks apparent catalytic motifs.
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TMPY-02435 | CD43 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
CD43 is an abundantly expressed molecule on the T-cell surface that shows distinct localization to the migrating T-cell uropod and the distal pole complex (DPC) opposite the immunological synapse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins. CD43 has a 235-amino acid (aa) extracellular domain, a 23-aa transmembrane domain, and a 123-aa cytoplasmic domain, all encoded by a single exon. The intracytoplasmic region of the protein is necessary to transduce signals; it is rich in potentially phosphorylable threonines and serines but lacks tyrosine residues as well as catalytic activity. CD43 engagement on human peripheral blood T cells and monocytes leads to cell activation and proliferation through the generation of second messengers such as diacylglycerol and inositol phosphates, protein kinase C (PKC) activation and Ca2+mobilization. Besides, CD43 ligation on human T cells induces the association of CD43 with Src family kinases, presumably through the interaction of their Src homology 3 domain with a proline-rich region of the CD43 intracytoplasmic tail. This molecule has been implicated in T cell activation, enhancing T cell response to allogeneic or mitogenic stimulation and CD43-specific signals have been reported to be sufficient to activate T cells in the absence of T cell receptor (TCR) engagement. In summary, CD43 regulates multiple T-cell functions, including T-cell activation, proliferation, apoptosis, and migration.
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TMPY-03824 | CD43 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
CD43 is an abundantly expressed molecule on the T-cell surface that shows distinct localization to the migrating T-cell uropod and the distal pole complex (DPC) opposite the immunological synapse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins. CD43 has a 235-amino acid (aa) extracellular domain, a 23-aa transmembrane domain, and a 123-aa cytoplasmic domain, all encoded by a single exon. The intracytoplasmic region of the protein is necessary to transduce signals; it is rich in potentially phosphorylable threonines and serines but lacks tyrosine residues as well as catalytic activity. CD43 engagement on human peripheral blood T cells and monocytes leads to cell activation and proliferation through the generation of second messengers such as diacylglycerol and inositol phosphates, protein kinase C (PKC) activation and Ca2+mobilization. Besides, CD43 ligation on human T cells induces the association of CD43 with Src family kinases, presumably through the interaction of their Src homology 3 domain with a proline-rich region of the CD43 intracytoplasmic tail. This molecule has been implicated in T cell activation, enhancing T cell response to allogeneic or mitogenic stimulation and CD43-specific signals have been reported to be sufficient to activate T cells in the absence of T cell receptor (TCR) engagement. In summary, CD43 regulates multiple T-cell functions, including T-cell activation, proliferation, apoptosis, and migration.
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TMPY-02191 | BLNK Protein, Human, Recombinant (His) | Human | HEK293 | ||
B-cell linker protein, also known as B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65 and BLNK, is a cytoplasm and cell membrane protein which contains oneSH2 domain. BLNK is expressed in B-cell lineage and fibroblast cell lines. Highest levels of expression is in the spleen, with lower levels in the liver, kidney, pancreas, small intestines and colon. BLNK functions as a central linker protein that bridges kinases associated with the B-cell receptor (BCR) with a multitude of signaling pathways, regulating biological outcomes of B-cell function and development. BLNK plays a role in the activation of ERK / EPHB2, MAP kinase p38 and JNK. BLNK modulates AP1 activation. It is important for the activation of NF-kappa-B and NFAT. BLNK plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca2+mobilization and is required for trafficking of the BCR to late endosomes. BLNK may be required for the RAC1-JNK pathway. It plays a critical role in orchestrating the pro-B cell to pre-B cell transition. BLNK also plays an important role in BCR-induced B-cell apoptosis.Defects in BLNK are the cause of agammaglobulinemia type 4 (AGM4) which is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development.
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TMPH-01297 | DDR1 Protein, Human, Recombinant (aa 21-417, His) | Human | HEK293 | ||
Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11.
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TMPH-02435 | CD3G Protein, Cynomolgus, Recombinant (His) | Cynomolgus | Yeast | ||
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G.
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TMPH-02924 | CD3 epsilon/CD3e Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development. Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region.
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TMPH-02925 | CD3 epsilon/CD3e Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development. Participates also in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region.
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TMPH-02182 | CD3G Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface. Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G.
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TMPJ-00329 | CD19 Protein, Rhesus macaque, Recombinant (hFc) | Rhesus macaque | Human Cells | ||
CD19 is a single-pass type I membrane protein containing 2 Ig-like C2-type (immunoglobulin-like) domains. CD19 is expressed on follicular dendritic cells and B cells. In fact, it is present on B cells from earliest recognizable B-lineage cells during development to B-cell blasts but is lost on maturation to plasma cells. CD19 primarily acts as a B cell co-receptor in conjunction with CD21 and CD81. Upon activation, the cytoplasmic tail of CD19 becomes phosphorylated, which leads to binding by Src-family kinases and recruitment of PI-3 kinase. CD19 Assembles with the antigen receptor of B lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation. Defects in CD19 are the cause of immunodeficiency common variable type 3 (CVID3) which is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen.
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TMPJ-00776 | HER2/ERBB2 Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | Human Cells | ||
Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.
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