antibody

c-Src (Tyr-215), phospho-specific [Conserved site]

MBS472018

0.1 mL

380 USD

polyclonal

rabbit

nonconjugated

phosphorylated

human, mouse, rat

western blot, ELISA

Antibody

c-Src (Tyr-215), phospho-specific [Conserved site]

c-Src (Tyr-215)

c-Src (Tyr-215); phospho-specific; Src

c-src; Proto-oncogene tyrosine-protein kinase Src; proto-oncogene tyrosine-protein kinase Src; OTTHUMP00000174476; OTTHUMP00000174477; OTTHUMP00000174478; proto-oncogene c-Src; tyrosine kinase pp60c-src; tyrosine-protein kinase SRC-1; protooncogene SRC, Rous sarcoma; v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian); Proto-oncogene c-Src; pp60c-src

SRC; SRC; ASV; SRC1; c-SRC; p60-Src; SRC1

SRC_HUMAN

Polyclonal

Rabbit

Human, Rat, Mouse

This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose then affinity purified using phospho-c-Src (Tyr-215) peptide (without carrier). The antibody detects a 60 kDa* protein on SDS-PAGE immunoblots of mouse SYF cells transformed with c-Src and human A431 cells that have been treated with pervanadate.

Affinity Purified

Rabbit polyclonal, affinity-purified antibody is supplied in 100 ul phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

Store at -20 degree C. Do not aliquot. Stable for 1 year.

ELISA, Western Blot

ELISA: 1:2000. Western Blot: 1:1000

Immunogen: c-Src (Tyr-215) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 215 of human c-Src. This sequence has homology to the conserved site in other Src family members, such as hck, fyn, csk, and yes.

Buffer: Rabbit polyclonal, affinity-purified antibody is supplied in 1001-11 phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

c-Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family is composed of nine members in vertebrates, including c-Src, Yes, Fgr, Yrk, Fyn, Lyn, Hck, Lck, and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility, and adhesion. Src-family kinases contain an N-terminal cell membrane anchor followed by SH3 and SH2 domains. The activity of c- Src is regulated by tyrosine phosphorylation at multiple sites. Tyrosine 419 is autophosphorylated following c-Src activation. Tyrosine 215 in the SH2 domain of c-Src is phosphorylated following growth factor receptor activation. Both Tyr-215 and Tyr-419 phosphorylation increases tyrosine kinase activity, while phosphorylation of Tyr-530 downregulates c-Src kinase activity. Thus, tyrosine phosphorylation of c-Src is critical for regulating its kinase activity.

Stover, D.R. et al. (1996) J Biol Chem 271(21):12481. Vadlamudi, R.K. et al. (2003) FEBS Letters 543:76.

1848077

P12931

59,835 Da

ADP Signalling Through P2Y Purinoceptor 1 Pathway (161061); Adaptive Immunity Signaling Pathway (366160); Adherens Junction Pathway (83070); Adherens Junction Pathway (481); Alpha-synuclein Signaling Pathway (137913); Alpha6-Beta4 Integrin Signaling Pathway (198807); Androgen Receptor Signaling Pathway (198806); Arf6 Signaling Events Pathway (138034); Atypical NF-kappaB Pathway (137946); Axon Guidance Pathway (105688)

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]

Function: Non-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. Ref.18 Ref.30 Ref.35 Ref.37. Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Enzyme regulation: Heme regulates its activity by enhancing the phosphorylation on Tyr-530. Ref.34. Subunit structure: Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1. By similarity. Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with HEV ORF3 protein; via the SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with ARRB1 and ARRB2. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PI3K (alpha and/or beta), PTK2, ESR1 (dimethylated on arginine) and FAK. Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B. By similarity. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domin) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.29 Ref.30 Ref.35 Ref.36 Ref.37. Subcellular location: Cell membrane. Mitochondrion inner membrane Ref.18. Post-translational modification: Dephosphorylated 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. Ref.23 Ref.25 Ref.26 Ref.28 Ref.31 Ref.32 Ref.33S-nitrosylation is important for activation of its kinase activity. Sequence similarities: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.Contains 1 protein kinase domain.Contains 1 SH2 domain.Contains 1 SH3 domain.

0.1 mL

380 USD