Anti-Phospho-Src antibody (200-300) {Biotin}

Clonality:	Polyclonal
Conjugation:	Biotin
Isotype:	IgG
Purification:	Affinity Purified
Concentration:	0.65-1.25 µg/µl
Dilution Range:	WB: 1:500 DB: 1:10, 000 ELISA: 1:10, 000 IP: 1:200
Storage Instruction:	Store at-20°C for long term storage. Avoid freeze-thaw cycles.

Gene Symbol:	SRC
Gene ID:	6714
Uniprot ID:	SRC_HUMAN
Immunogen Region:	200-300
Immunogen:	N-epitope phosphorylated synthetic peptide taken within amino acid region 200-300 on human Src protein. Phosphorylated Tyr-215 residue.

Tissue Specificity	Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues. Isoform 1: Expressed in spleen and liver. Isoform 2: Expressed in brain. Isoform 3: Expressed in brain.
Post Translational Modifications	Myristoylated at Gly-2, and this is essential for targeting to membranes. Dephosphorylated at Tyr-530 by PTPRJ. 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. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated. Isoform 1: Displays reduced levels of autophosphorylation at Tyr-419 compared to isoforms 2 and 3. Isoform 2: Displays enhanced levels of autophosphorylation at Tyr-419 compared to isoform 1. Isoform 3: Displays enhanced levels of autophosphorylation at Tyr-419 compared to isoform 1. Shows reduced phosphorylation at Tyr-527 compared to isoforms 1 and 2. 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.
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). 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. 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 (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. 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 RIGI-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. Phosphorylates synaptic vesicle protein synaptophysin (SYP). Involved in anchorage-independent cell growth. Required for podosome formation. Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration. Phosphorylates OTUB1, promoting deubiquitination of RPTOR. Isoform 1: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. Isoform 2: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation. The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity. Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs. Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth. Isoform 3: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation. The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity. Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs. Plays a role in neurite elongation.
Protein Name	Proto-Oncogene Tyrosine-Protein Kinase Src Proto-Oncogene C-Src Pp60c-Src P60-Src
Database Links	Reactome: R-HSA-1227986 Reactome: R-HSA-1251985 Reactome: R-HSA-1253288 Reactome: R-HSA-1257604 Reactome: R-HSA-1295596 P12931-1 Reactome: R-HSA-1433557 P12931-1 Reactome: R-HSA-1433559 P12931-1 Reactome: R-HSA-171007 P12931-1 Reactome: R-HSA-177929 P12931-1 Reactome: R-HSA-180292 Reactome: R-HSA-186763 Reactome: R-HSA-191650 P12931-2 Reactome: R-HSA-201556 P12931-1 Reactome: R-HSA-2029481 P12931-1 Reactome: R-HSA-210990 P12931-1 Reactome: R-HSA-2219530 Reactome: R-HSA-2682334 P12931-1 Reactome: R-HSA-354192 Reactome: R-HSA-354194 Reactome: R-HSA-372708 Reactome: R-HSA-375165 P12931-1 Reactome: R-HSA-389356 P12931-1 Reactome: R-HSA-389513 P12931-1 Reactome: R-HSA-391160 P12931-1 Reactome: R-HSA-3928662 P12931-1 Reactome: R-HSA-3928663 P12931-1 Reactome: R-HSA-3928664 P12931-1 Reactome: R-HSA-3928665 P12931-1 Reactome: R-HSA-418555 Reactome: R-HSA-418592 P12931-1 Reactome: R-HSA-418594 Reactome: R-HSA-418885 Reactome: R-HSA-418886 Reactome: R-HSA-428542 Reactome: R-HSA-430116 P12931-1 Reactome: R-HSA-437239 P12931-1 Reactome: R-HSA-4420097 P12931-1 Reactome: R-HSA-456926 P12931-1 Reactome: R-HSA-5218921 P12931-1 Reactome: R-HSA-5607764 P12931-1 Reactome: R-HSA-5663220 P12931-1 Reactome: R-HSA-5673000 Reactome: R-HSA-5674135 Reactome: R-HSA-6802946 Reactome: R-HSA-6802948 Reactome: R-HSA-6802952 Reactome: R-HSA-6802955 Reactome: R-HSA-6811558 Reactome: R-HSA-69231 P12931-1 Reactome: R-HSA-8853659 P12931-1 Reactome: R-HSA-8874081 Reactome: R-HSA-8876493 Reactome: R-HSA-8934593 Reactome: R-HSA-8934903 P12931-1 Reactome: R-HSA-8940973 Reactome: R-HSA-8941858 Reactome: R-HSA-9009391 Reactome: R-HSA-9013420 Reactome: R-HSA-9032500 Reactome: R-HSA-9603381 Reactome: R-HSA-9620244 Reactome: R-HSA-9634597 Reactome: R-HSA-9649948 Reactome: R-HSA-9656223 Reactome: R-HSA-9664323 P12931-1 Reactome: R-HSA-9664422 P12931-1 Reactome: R-HSA-9670439 P12931-1 Reactome: R-HSA-9680350
Cellular Localisation	Cell Membrane Lipid-Anchor Mitochondrion Inner Membrane Nucleus Cytoplasm Cytoskeleton Perinuclear Region Cell Junction Focal Adhesion Localizes To Focal Adhesion Sites Following Integrin Engagement Localization To Focal Adhesion Sites Requires Myristoylation And The Sh3 Domain Colocalizes With Pdlim4 At The Perinuclear Region But Not At Focal Adhesions
Alternative Antibody Names	Anti-Proto-Oncogene Tyrosine-Protein Kinase Src antibody Anti-Proto-Oncogene C-Src antibody Anti-Pp60c-Src antibody Anti-P60-Src antibody Anti-SRC antibody Anti-SRC1 antibody

Information sourced from Uniprot.org

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