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Testing Data
(HTRF assay for SRC protein activity 1 uM TK substrate was incubated with different concentrations of SRC protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT and 100 uM ATP for 1 hour. The detection reagents were added and incubated with the reactions for 1 hr. All the operations and reactions were performed at room temperature, and HTRF KinASE TK assay was used to detect the enzymatic activity.)
Testing Data
(HTRF assay for SRC protein activity 1 uM TK substrate was incubated with different concentrations of SRC protein in 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT and 100 uM ATP for 1 hour. The detection reagents were added and incubated with the reactions for 1 hr. All the operations and reactions were performed at room temperature, and HTRF KinASE TK assay was used to detect the enzymatic activity.)
Background: SRC (SRC Proto-Oncogene) is a 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. It 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. 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. 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. It also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. SRC plays a role in EGF-mediated calcium-activated chloride channel activation. It also has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor.
NCBI and Uniprot Product Information
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
Research Articles on SRC
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Product Notes
The SRC src (Catalog #AAA389172) is a Recombinant Protein produced from Baculovirus and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "SRC, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
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