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Mouse Monoclonal c-Src antibody [4F1E8] (STJ97973)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:10000
Recommended protocols: check protocols
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Check alternative names for the antibodyExpand
SRC antibody, SRC1 antibody,|ASV antibody|Avian sarcoma virus antibody|c SRC antibody|CDNA FLJ14219 fis clone NT2RP3003800 highly similar to Rattus norvegicus tyrosine protein kinase pp60 c src mRNA antibody|cSrc antibody|EC 126.96.36.199 antibody|Neuronal CSRC tyrosine specific protein kinase antibody|Neuronal SRC antibody|Oncogene SRC antibody|OTTHUMP00000174476 antibody|OTTHUMP00000174477 antibody|p60 Src antibody|p60-Src antibody|p60Src antibody|pp60c src antibody|pp60c-src antibody|pp60csrc antibody|Proto oncogene tyrosine protein kinase Src antibody|Proto-oncogene c-Src antibody|Proto-oncogene tyrosine-protein kinase Src antibody|Protooncogene SRC antibody|Protooncogene SRC Rous sarcoma antibody|Src antibody|SRC Oncogene antibody|SRC proto oncogene non receptor tyrosine kinase antibody|SRC_HUMAN antibody|SRC1 antibody|Tyrosine kinase pp60c src antibody|Tyrosine protein kinase SRC 1 antibody|Tyrosine protein kinase SRC1 antibody|v src avian sarcoma (Schmidt Ruppin A2) viral oncogene homolog antibody|V src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog (avian) antibody|v src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog avian antibody|Phospho anti-SRC Family (Y418) antibody [EP503Y] (ab40660)
SCBT cat No: sc-130124|sc-130069|sc-130074|sc-8056|sc-5266|sc-19|sc-18|sc-167555|sc-383868|sc-167557|sc-393260|sc-393962|sc-393317|sc-166647|sc-16473|sc-398840|
c-Src Monoclonal Antibody
|Catalogue No.|| |
c-Src Monoclonal Antibody detects endogenous levels of c-Src protein.
Purified recombinant fragment of c-Src (aa10-193) expressed in E Coli
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:10000
c-Src Antibody was tube-contained. Ascitic fluid containing 0.03% sodium azide.
c-Src Antibody was purified using affinity purification.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Proto-oncogene tyrosine-protein kinase Src antibody, Proto-oncogene c-Src antibody, pp60c-src antibody, p60-Src antibody
|Protein names|| |
Proto-oncogene tyrosine-protein kinase Src , Proto-oncogene c-Src , pp60c-src , p60-Src
|Protein function|| |
Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at ‘Tyr-1477’. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on ‘Tyr-284’ and CBL on ‘Tyr-731’. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at ‘Tyr-9’, ‘Tyr-373’ and ‘Tyr-376’. Phosphorylates BCAR1 at ‘Tyr-128’. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at ‘Tyr-341’ activates CBLC E3 activity. Required for podosome formation (By similarity). / ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. / Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity.
|Protein tissue specificity|| |
Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.
|Involvement in disease|| |
Note: SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells.
|Protein sequence and domain|| |
The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment. / Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. / Contains 1 protein kinase domain. / Contains 1 SH2 domain. / Contains 1 SH3 domain.
|Protein post-translational modifications|| |
Myristoylated at Gly-2, and this is essential for targeting to membranes. / Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. / S-nitrosylation is important for activation of its kinase activity. / Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation.
|Protein cellular localization|| |
Cell membrane / Mitochondrion inner membrane / Nucleus / Cytoplasm > cytoskeleton
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St John’s Laboratory Ltd.
|Product type|| |
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