Rabbit anti-Human SRC Polyclonal Antibody | anti-SRC antibody

SRC Antibody

Cat. Num. AAA7136193

• Gene Names: SRC; ASV; SRC1; c-SRC; p60-Src
• Reactivity: Human
• Applications: ELISA, Immunohistochemistry
• Purity: >95%, Protein G purified
• Synonyms: SRC; Polyclonal Antibody; SRC Antibody; Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src); SRC1; anti-SRC antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: >95%, Protein G purified
• Form/Format: Liquid; Preservative: 0.03% Proclin 300; Constituents: 50% Glycerol, 0.01M PBS, PH7.4

• Applicable Applications for anti-SRC antibody: ELISA (EIA), Immunohistochemistry (IHC)
• Application Notes: IHC: 1:200-1:500
• Conjugation: Non-conjugated
• Immunogen: Recombinant Human Proto-oncogene tyrosine-protein kinase Src protein (2-100AA)
• Preparation and Storage: Upon receipt, store at -20 degree C or -80 degree C. Avoid repeated freeze.

Immunohistochemistry (IHC)

(IHC image diluted at 1:200 and staining in paraffin-embedded human breast cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4 degree C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.)

Related Product Information for anti-SRC antibody

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 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. 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).

Product Categories/Family for anti-SRC antibody

Signal Transduction

NCBI and Uniprot Product Information

• NCBI GI #: 4885609
• NCBI GeneID: 6714
• NCBI Accession #: NP_005408.1
• NCBI GenBank Nucleotide #: NM_005417.3
• UniProt Accession #: P12931; Q76P87; Q86VB9; Q9H5A8; E1P5V4
• Molecular Weight: 59,835 Da
• NCBI Official Full Name: proto-oncogene tyrosine-protein kinase Src
• NCBI Official Synonym Full Names: v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)
• NCBI Official Symbol: SRC
• NCBI Official Synonym Symbols: ASV; SRC1; c-SRC; p60-Src
• NCBI Protein Information: proto-oncogene tyrosine-protein kinase Src; proto-oncogene c-Src; tyrosine kinase pp60c-src; tyrosine-protein kinase SRC-1; protooncogene SRC, Rous sarcoma
• UniProt Protein Name: Proto-oncogene tyrosine-protein kinase Src
• Protein Family: Src-like-adapter
• UniProt Gene Name: SRC
• UniProt Synonym Gene Names: SRC1; p60-Src
• UniProt Entry Name: SRC_HUMAN

NCBI Description

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]

Uniprot Description

Src: proto-oncogenic cytoplasmic tyrosine kinase of the SRC family. Highly expressed in certain fully differentiated cells such as neurons, platelets and macrophages. Phosphorylation of an activation loop tyrosine activates the enzyme; phosphorylation of a tyrosine in the C-terminus by Csk inhibits the enzyme. Two alternatively spliced isoforms have been described.

Protein type: Protein kinase, TK; EC 2.7.10.2; Kinase, protein; Oncoprotein; Protein kinase, tyrosine (non-receptor); TK group; Src family

Chromosomal Location of Human Ortholog: 20q12-q13

Cellular Component: neuron projection; mitochondrion; lysosome; postsynaptic density; actin filament; caveola; cytosol; extrinsic to internal side of plasma membrane; perinuclear region of cytoplasm; late endosome; mitochondrial inner membrane; cytoplasm; plasma membrane; nucleus

Molecular Function: protein C-terminus binding; ephrin receptor binding; non-membrane spanning protein tyrosine kinase activity; phosphoprotein binding; insulin receptor binding; protein kinase activity; integrin binding; protein binding; enzyme binding; SH3/SH2 adaptor activity; protein kinase C binding; protein-tyrosine kinase activity; heme binding; estrogen receptor binding; SH2 domain binding; kinase activity; ATP binding; hormone receptor binding; receptor binding

Biological Process: oogenesis; regulation of estrogen receptor signaling pathway; progesterone receptor signaling pathway; central nervous system development; positive regulation of cyclin-dependent protein kinase activity; estrogen receptor signaling pathway; viral reproduction; nerve growth factor receptor signaling pathway; positive regulation of apoptosis; regulation of cell cycle; positive regulation of transcription, DNA-dependent; uterus development; negative regulation of mitochondrial depolarization; negative regulation of protein homooligomerization; positive regulation of MAP kinase activity; cell-cell adhesion; transforming growth factor beta receptor signaling pathway; cell adhesion; response to electrical stimulus; bone resorption; response to drug; platelet activation; fibroblast growth factor receptor signaling pathway; activation of protein kinase B; response to virus; transcytosis; positive regulation of integrin activation; positive regulation of protein amino acid autophosphorylation; cellular response to insulin stimulus; response to mechanical stimulus; T cell costimulation; regulation of vascular permeability; negative regulation of transcription, DNA-dependent; leukocyte migration; negative regulation of apoptosis; axon guidance; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; platelet-derived growth factor receptor signaling pathway; negative regulation of caspase activity; signal transduction; positive regulation of smooth muscle cell migration; regulation of cell-cell adhesion; forebrain development; ephrin receptor signaling pathway; epidermal growth factor receptor signaling pathway; integrin-mediated signaling pathway; response to nutrient levels; regulation of bone resorption; negative regulation of focal adhesion formation; signal complex assembly; positive regulation of phosphoinositide 3-kinase activity; response to mineralocorticoid stimulus; cell cycle; regulation of cell proliferation; cell proliferation; positive regulation of protein kinase B signaling cascade; peptidyl-serine phosphorylation; response to hydrogen peroxide; regulation of protein binding; Ras protein signal transduction; stress fiber formation; innate immune response; response to acidity; positive regulation of insulin receptor signaling pathway; vascular endothelial growth factor receptor signaling pathway; blood coagulation; positive regulation of cytokine secretion