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Testing Data

phospho-c-Src (Tyr-215) Peptide | SRC peptide

phospho-c-Src (Tyr-215) Blocking Peptide

Gene Names
SRC; ASV; SRC1; c-SRC; p60-Src
Synonyms
phospho-c-Src (Tyr-215) Peptide; phospho-c-Src (Tyr-215) Blocking Peptide; SRC peptide
Ordering
For Research Use Only!
Specificity
The peptide is specifically recognized by anti-c-Src (Tyr-215) phospho-specific antibody (SP1371) in ELISA, and has been shown to block the reactivity of SP1371 during Western blot. In addition, the peptide is recommended for use in blocking SP1371 reactivity in immunocytochemistry.
Form/Format
Blocking Peptide is supplied in 50ul phosphate-buffered saline and 0.05% sodium azide.
Sequence
Peptide Sequence: Phospho-c-Src (Tyr-215) synthetic peptide corresponds to amino acid residues around tyrosine 215 of human c-Src. This peptide sequence has homology to other Src kinase family members, such as hck, fyn, csk, and yes.
Application Notes
Antibody Blocking: 1 ug/ml
ELISA: 10-100 ng/well
Preparation and Storage
Store at -20 degree C. Stable for 1 year.

Testing Data

Testing Data
Related Product Information for SRC peptide
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 amino terminal cell membrane anchor followed by an SH3 domain and an SH2 domain. The activity of c-Src is regulated by tyrosine phosphorylation at multiple sites. Tyrosine 418 is autophosphorylated following c-Src activation. Tyrosine 215 in the SH-2 domain of c-Src is phosphorylated following growth factor receptor activation. Both Tyr-215 and Tyr-418 phosphorylation increases tyrosine kinase activity, while phosphorylation of Tyr-529 downregulates c-Src kinase activity. Thus, tyrosine phosphorylation of c-Src is critical for regulating its kinase activity.
References
• Stover, D.R. et al. (1996) J Biol Chem 271(21):12481.
• Vadlamudi, R.K. et al. (2003) FEBS Letters 543:76.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
UniProt Accession #
Molecular Weight
59,835 Da
NCBI Official Full Name
c-src
NCBI Official Synonym Full Names
v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian)
NCBI Official Symbol
SRC
NCBI Official Synonym Symbols
ASV; SRC1; c-SRC; p60-Src
NCBI Protein Information
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
UniProt Protein Name
Proto-oncogene tyrosine-protein kinase Src
UniProt Gene Name
SRC
UniProt Synonym Gene Names
SRC1
UniProt Entry Name
SRC_HUMAN

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]

Uniprot Description

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.

Research Articles on SRC

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Product Notes

The SRC src (Catalog #AAA474029) is a Peptide and is intended for research purposes only. The product is available for immediate purchase. Antibody Blocking: 1 ug/ml ELISA: 10-100 ng/well. Researchers should empirically determine the suitability of the SRC src for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: Peptide Sequence: Phospho-c- Src (Tyr-215) synthetic peptide correspond s to amino acid residues around tyrosine 215 of human c-Src. This peptide sequence has homology to other Src kinase family members, such as hck, fyn, csk, and yes. It is sometimes possible for the material contained within the vial of "phospho-c-Src (Tyr-215) Peptide, Peptide" 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

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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