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Mouse Anti-c-SRC Recombinant Antibody (38) (CBMAB-AP1742LY)

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
38
Antibody Isotype
IgG2b
Application
ELISA, IF, IHC, WB

Basic Information

Immunogen
Fusion protein of c-SRC
Specificity
Human, Mouse
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
SRC Proto-Oncogene, Non-Receptor Tyrosine Kinase
Introduction
This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]
Entrez Gene ID
Human6714
Mouse20779
UniProt ID
HumanP12931
MouseP05480
Alternative Names
SRC Proto-Oncogene, Non-Receptor Tyrosine Kinase; V-Src Avian Sarcoma (Schmidt-Ruppin A-2) Viral Oncogene Homolog; Proto-Oncogene C-Src; EC 2.7.10.2; P60-Src; SRC1; Proto-Oncogene Tyrosine-Protein Kinase Src; Protooncogene SRC, Rous Sarcoma;
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) (Probable). 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) (PubMed:21411625).

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 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity).

Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730).

Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953).

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 GRK2, 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 (Probable). 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 (PubMed:7853507).

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 (PubMed:8755529, PubMed:14585963).

Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910).

Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108).

Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750).

Enhances DDX58/RIG-I-elicited antiviral signaling (PubMed:19419966).

Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963).

Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723).

Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694).

Involved in anchorage-independent cell growth (PubMed:19307596).

Required for podosome formation (By similarity).

Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159).
Biological Process
Activation of protein kinase B activity Source: Ensembl
Adherens junction organization Source: Ensembl
Angiotensin-activated signaling pathway involved in heart process Source: BHF-UCL
Axon guidance Source: Reactome
Bone resorption Source: UniProtKB
Branching involved in mammary gland duct morphogenesis Source: Ensembl
Cell adhesion Source: GO_Central
Cell-cell adhesion Source: Ensembl
Cell cycle Source: UniProtKB-KW
Cell differentiation Source: GO_Central
Cell population proliferation Source: Ensembl
Cellular response to fatty acid Source: Ensembl
Cellular response to fluid shear stress Source: Ensembl
Cellular response to hydrogen peroxide Source: Ensembl
Cellular response to hypoxia Source: Ensembl
Cellular response to insulin stimulus Source: Ensembl
Cellular response to lipopolysaccharide Source: Ensembl
Cellular response to peptide hormone stimulus Source: BHF-UCL
Cellular response to platelet-derived growth factor stimulus Source: Ensembl
Cellular response to progesterone stimulus Source: BHF-UCL
Entry of bacterium into host cell Source: Reactome
Ephrin receptor signaling pathway Source: Reactome
Epidermal growth factor receptor signaling pathway Source: GO_Central
ERBB2 signaling pathway Source: Reactome
Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
Focal adhesion assembly Source: UniProtKB
Forebrain development Source: Ensembl
G protein-coupled receptor signaling pathway Source: Reactome
Innate immune response Source: GO_Central
Integrin-mediated signaling pathway Source: UniProtKB
Interleukin-6-mediated signaling pathway Source: UniProtKB
Intestinal epithelial cell development Source: UniProtKB
Intracellular signal transduction Source: ARUK-UCL
Leukocyte migration Source: Reactome
Macroautophagy Source: Reactome
Negative regulation of anoikis Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
Negative regulation of focal adhesion assembly Source: BHF-UCL
Negative regulation of inflammatory response to antigenic stimulus Source: Reactome
Negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
Negative regulation of mitochondrial depolarization Source: UniProtKB
Negative regulation of protein-containing complex assembly Source: UniProtKB
Negative regulation of telomerase activity Source: BHF-UCL
Negative regulation of telomere maintenance via telomerase Source: BHF-UCL
Negative regulation of transcription, DNA-templated Source: Ensembl
Neurotrophin TRK receptor signaling pathway Source: Ensembl
Odontogenesis Source: Ensembl
Oogenesis Source: Ensembl
Osteoclast development Source: GO_Central
Peptidyl-serine phosphorylation Source: Ensembl
Peptidyl-tyrosine autophosphorylation Source: Ensembl
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Platelet activation Source: Reactome
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of canonical Wnt signaling pathway Source: Ensembl
Positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
Positive regulation of cytokine production Source: Ensembl
Positive regulation of dephosphorylation Source: ARUK-UCL
Positive regulation of DNA biosynthetic process Source: Ensembl
Positive regulation of epithelial cell migration Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: Ensembl
Positive regulation of glucose metabolic process Source: Ensembl
Positive regulation of insulin receptor signaling pathway Source: Ensembl
Positive regulation of integrin activation Source: BHF-UCL
Positive regulation of lamellipodium morphogenesis Source: UniProtKB
Positive regulation of MAP kinase activity Source: Ensembl
Positive regulation of non-membrane spanning protein tyrosine kinase activity Source: ARUK-UCL
Positive regulation of Notch signaling pathway Source: UniProtKB
Positive regulation of ovarian follicle development Source: Ensembl
Positive regulation of peptidyl-tyrosine phosphorylation Source: ARUK-UCL
Positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
Positive regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
Positive regulation of platelet-derived growth factor receptor-beta signaling pathway Source: Ensembl
Positive regulation of podosome assembly Source: Ensembl
Positive regulation of protein autophosphorylation Source: Ensembl
Positive regulation of protein kinase B signaling Source: UniProtKB
Positive regulation of protein localization to nucleus Source: Ensembl
Positive regulation of protein processing Source: Ensembl
Positive regulation of protein serine/threonine kinase activity Source: UniProtKB
Positive regulation of protein transport Source: Ensembl
Positive regulation of small GTPase mediated signal transduction Source: ParkinsonsUK-UCL
Positive regulation of smooth muscle cell migration Source: Ensembl
Positive regulation of transcription, DNA-templated Source: Ensembl
Primary ovarian follicle growth Source: Ensembl
Progesterone receptor signaling pathway Source: BHF-UCL
Protein autophosphorylation Source: UniProtKB
Protein destabilization Source: Ensembl
Regulation of bone resorption Source: BHF-UCL
Regulation of caveolin-mediated endocytosis Source: UniProtKB
Regulation of cell-cell adhesion Source: UniProtKB
Regulation of cell projection assembly Source: Ensembl
Regulation of early endosome to late endosome transport Source: UniProtKB
Regulation of epithelial cell migration Source: UniProtKB
Regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
Regulation of postsynaptic neurotransmitter receptor activity Source: Ensembl
Regulation of protein binding Source: Ensembl
Regulation of vascular permeability Source: BHF-UCL
Response to acidic pH Source: Ensembl
Response to drug Source: Ensembl
Response to electrical stimulus Source: Ensembl
Response to interleukin-1 Source: BHF-UCL
Response to mechanical stimulus Source: Ensembl
Response to mineralocorticoid Source: Ensembl
Response to nutrient levels Source: Ensembl
Response to virus Source: Ensembl
Signal complex assembly Source: ProtInc
Signal transduction Source: ProtInc
Stimulatory C-type lectin receptor signaling pathway Source: Reactome
Stress fiber assembly Source: UniProtKB
Substrate adhesion-dependent cell spreading Source: Ensembl
T cell costimulation Source: Reactome
Transcytosis Source: Ensembl
Transforming growth factor beta receptor signaling pathway Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Uterus development Source: Ensembl
Vascular endothelial growth factor receptor signaling pathway Source: Reactome
Viral process Source: UniProtKB-KW
Cellular Location
Nucleus; Mitochondrion inner membrane; Cell membrane; Cytoskeleton; Perinuclear region; Focal adhesion. Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions (PubMed:19307596).

Belli, S., Esposito, D., Servetto, A., Pesapane, A., Formisano, L., & Bianco, R. (2020). c-Src and EGFR inhibition in molecular cancer therapy: what else can we improve?. Cancers, 12(6), 1489.

Torrisi, F., Vicario, N., Spitale, F. M., Cammarata, F. P., Minafra, L., Salvatorelli, L., ... & Parenti, R. (2020). The role of hypoxia and SRC tyrosine kinase in glioblastoma invasiveness and radioresistance. Cancers, 12(10), 2860.

Jha, V., Macchia, M., Tuccinardi, T., & Poli, G. (2020). Three-dimensional interactions analysis of the anticancer target c-src kinase with its inhibitors. Cancers, 12(8), 2327.

Lee, G. W., Park, J. B., Park, S. Y., Seo, J., Shin, S. H., Park, J. W., ... & Chun, Y. S. (2018). The E3 ligase C-CBL inhibits cancer cell migration by neddylating the proto-oncogene c-Src. Oncogene, 37(41), 5552-5568.

Zhou, P., Hou, S., Bai, Z., Li, Z., Wang, H., Chen, Z., & Meng, Y. (2018). Disrupting the intramolecular interaction between proto-oncogene c-Src SH3 domain and its self-binding peptide PPII with rationally designed peptide ligands. Artificial Cells, Nanomedicine, and Biotechnology, 46(6), 1122-1131.

Molinari, A., Fallacara, A. L., Di Maria, S., Zamperini, C., Poggialini, F., Musumeci, F., ... & Botta, M. (2018). Efficient optimization of pyrazolo [3, 4-d] pyrimidines derivatives as c-Src kinase inhibitors in neuroblastoma treatment. Bioorganic & Medicinal Chemistry Letters, 28(21), 3454-3457.

Yoon, H. J., Lee, S., Park, S. J., & Wu, S. (2018). Network approach of the conformational change of c-Src, a tyrosine kinase, by molecular dynamics simulation. Scientific reports, 8(1), 1-10.

Kim, J. H., Kim, K., Kim, I., Seong, S., & Kim, N. (2018). c-Src–Dependent and–Independent Functions of Matk in Osteoclasts and Osteoblasts. The Journal of Immunology, 200(7), 2455-2463.

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For research use only. Not intended for any clinical use.

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