Rabbit Recombinant Monoclonal SRC antibody - conjugated to APC.
IgG
Rabbit
APC
Ex: 650nm, Em: 660nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
Liquid
Monoclonal
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
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).
Proto-oncogene tyrosine-protein kinase Src, Proto-oncogene c-Src, pp60c-src, p60-Src, SRC1, SRC
Rabbit Recombinant Monoclonal SRC antibody - conjugated to APC.
Proto-oncogene tyrosine-protein kinase Src, Proto-oncogene c-Src, pp60c-src, p60-Src, SRC1, SRC
IgG
Rabbit
APC
Ex: 650nm, Em: 660nm
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
Liquid
Monoclonal
EGTR103
Affinity purification Protein A
Blue Ice
1-2 weeks
+4°C
+4°C
Upon delivery aliquot
Avoid freeze / thaw cycle, Store in the dark
This product is a recombinant monoclonal antibody, which offers several advantages including:
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Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
This supplementary information is collated from multiple sources and compiled automatically.
Src also known as c-Src is a protein-tyrosine kinase involved in the regulation of many cellular processes. The molecular weight of Src is approximately 60 kDa. Src is ubiquitously expressed in human tissues but shows increased expression in specific tissues like the brain and epithelial cells. This protein has several important roles in cellular signal transduction particularly influencing cell growth differentiation and survival.
The Src protein interacts with other proteins to modulate cell adhesion motility and angiogenesis forming part of larger protein complexes. Src phosphorylates specific tyrosine residues on its substrates altering their activity interaction or stability. This activity positions Src as an important factor in managing cell communication and structural organization. Src's interaction with focal adhesion complexes emphasizes its functionality in cellular structural integrity and intracellular communication pathways.
Src plays a critical role in the integrin and growth factor receptor signaling pathways mediating cross-talk between cell surface receptors and intricate signaling cascades. It closely associates with focal adhesion kinase (FAK) within these pathways influencing cytoskeletal rearrangements and cell movement. Src's function in the epidermal growth factor receptor (EGFR) signaling pathway likewise demonstrates its importance in regulating cellular proliferation and survival mechanisms.
Src has significant implications in oncogenesis particularly in colorectal and breast cancers. Overexpression or abnormal activity of Src associates with tumor progression and metastasis. Within these cancers Src cooperates with various proteins like the EGFR amplifying aberrant cell signaling that contributes to uncontrolled cell growth. Investigating Src's role and regulation could offer insights into novel therapeutic strategies for controlling Src activity in cancer treatment.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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