Src blocking peptide

Mouse Src Antibody (N-term) Blocking Peptide

• Gene Names: Src; AW259666; pp60c-src
• Synonyms: Src; Mouse Src Antibody (N-term) Blocking Peptide; Neuronal proto-oncogene tyrosine-protein kinase Src; Proto-oncogene c-Src; pp60c-src; p60-Src; Src blocking peptide

• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 541

• Cellular Location: Cell membrane. Mitochondrion inner membrane Nucleus. Cytoplasm, cytoskeleton. Note: Localizes to focal adhesion sites after integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for Src blocking peptide

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- 132'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity.

NCBI and Uniprot Product Information

• NCBI GI #: 341942278
• NCBI GeneID: 20779
• UniProt Accession #: P05480; Q2M4I4
• Molecular Weight: 60,645 Da
• NCBI Official Full Name: Neuronal proto-oncogene tyrosine-protein kinase Src
• NCBI Official Synonym Full Names: Rous sarcoma oncogene
• NCBI Official Symbol: Src
• NCBI Official Synonym Symbols: AW259666; pp60c-src
• NCBI Protein Information: neuronal proto-oncogene tyrosine-protein kinase Src
• UniProt Protein Name: Neuronal proto-oncogene tyrosine-protein kinase Src
• Protein Family: Src-like-adapter
• UniProt Gene Name: Src
• UniProt Synonym Gene Names: p60-Src
• UniProt Entry Name: SRC_MOUSE

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

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

Molecular Function: cell adhesion molecule binding; enzyme binding; ephrin receptor binding; estrogen receptor binding; heme binding; hormone receptor binding; insulin receptor binding; kinase activity; kinase binding; non-membrane spanning protein tyrosine kinase activity; phosphoprotein binding; protein binding; protein C-terminus binding; protein complex binding; protein domain specific binding; protein kinase activity; protein kinase binding; protein kinase C binding; protein-tyrosine kinase activity; receptor binding; SH2 domain binding

Biological Process: activation of protein kinase B; bone resorption; cell migration; cell proliferation; epidermal growth factor receptor signaling pathway; forebrain development; innate immune response; integrin-mediated signaling pathway; negative regulation of apoptosis; negative regulation of caspase activity; negative regulation of focal adhesion formation; negative regulation of mitochondrial depolarization; negative regulation of protein homooligomerization; negative regulation of telomerase activity; negative regulation of telomere maintenance via telomerase; negative regulation of transcription, DNA-dependent; nerve growth factor receptor signaling pathway; oogenesis; peptidyl-serine phosphorylation; peptidyl-tyrosine phosphorylation; phosphorylation; platelet-derived growth factor receptor signaling pathway; positive regulation of apoptosis; positive regulation of cell adhesion; positive regulation of cyclin-dependent protein kinase activity; positive regulation of cytokine secretion; positive regulation of insulin receptor signaling pathway; positive regulation of MAP kinase activity; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase activity; positive regulation of protein amino acid autophosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of protein transport; positive regulation of smooth muscle cell migration; positive regulation of transcription, DNA-dependent; progesterone receptor signaling pathway; protein amino acid autophosphorylation; protein amino acid phosphorylation; protein destabilization; regulation of cell cycle; regulation of cell proliferation; regulation of cell-cell adhesion; regulation of estrogen receptor signaling pathway; regulation of protein binding; stress fiber formation; transcytosis; transforming growth factor beta receptor signaling pathway; uterus development