Key features and details
- Rabbit polyclonal to Src (phospho Y529)
- Suitable for: WB
- Reacts with: Mouse, Rat, Chicken, Human
- Isotype: IgG
Product nameAnti-Src (phospho Y529) antibody
See all Src primary antibodies
DescriptionRabbit polyclonal to Src (phospho Y529)
SpecificityFyn and Yes (92%homologous) were not tested.
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Mouse, Rat, Chicken, Human
Synthetic peptide (Human) derived from the region of Src that contains tyrosine 529, based on the human sequence. The sequence is conserved in mouse (tyrosine 534), chicken (tyrosine 527) and frog (tyrosine 525).
- Chicken Embryo Fibroblast (CEF) cells expressing Src protein and plated on fibronectin.
Src (also known as pp60src) is a non-receptor tyrosine kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. Tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of the catalytic domain residue (tyrosine 418 in the human sequence), thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylatedleading to full activation.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage bufferpH: 7.30
Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol, 0.1% BSA
Concentration information loading...
PurityImmunogen affinity purified
Purification notesPurified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using (i) a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated Src, and (ii) a generic tyrosine phosphorylated peptide to remove antibody that is reactive with phosphotyrosine, irrespective of the sequence. The final product is generated by affinity chromatography using a Src-derived peptide that is phosphorylated at tyrosine 529.
Primary antibody notesSrc (also known as pp60src) is a non-receptor tyrosine kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. Tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of the catalytic domain residue (tyrosine 418 in the human sequence), thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylatedleading to full activation.
Our Abpromise guarantee covers the use of ab4817 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000. Detects a band of approximately 62 kDa (predicted molecular weight: 62 kDa).|
FunctionNon-receptor protein tyrosine kinase that plays pivotal roles in numerous cellular processes such as proliferation, migration, and transformation. In concert with PTK2B, plays an important role in osteoclastic bone resorption. Both the formation of a SRC-PTK2B complex, and SRC kinase activity are necessary for this function. Once it is recruited to the activated integrins, by PTK2B, it phosphorylates 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 RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
Contains 1 protein kinase domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain.
modificationsDephosphorylated at Tyr-530 by PTPRJ (By similarity). 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.
S-nitrosylation is important for activation of its kinase activity.
Cellular localizationCell membrane. Mitochondrion inner membrane.
- Information by UniProt
FormThis protein is known to be similar in amino acid sequence to HCK (P08631), LCK (P06239), FYN (P06241), YES1 (P07947), and LYN (P07948). Therefore, cross-reactivity with these homologous proteins may be observed. We would be happy to provide immunogen alignment information upon request.
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Western blot detection of Src phosphorylation in extracts of chick embryo fibroblasts expressing wild-type (lanes 2,4,6) or mutant (lanes 1,3,5) pp60src. Truncation of Src at position 518 eliminated phosphorylation at the negative regulatory site [pY529], while increasing phosphorylation at the catalytic site [pY418].
ab4817 has been referenced in 3 publications.
- Yuan M et al. SRC and MEK Co-inhibition Synergistically Enhances the Anti-tumor Effect in Both Non-small-cell Lung Cancer (NSCLC) and Erlotinib-Resistant NSCLC. Front Oncol 9:586 (2019). PubMed: 31428570
- Hilmarsdottir B et al. Inhibition of PTP1B disrupts cell-cell adhesion and induces anoikis in breast epithelial cells. Cell Death Dis 8:e2769 (2017). WB ; Human . PubMed: 28492548
- Xiao X et al. c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution. Am J Physiol Endocrinol Metab 304:E145-59 (2013). WB ; Rat . PubMed: 23169788