Product nameRecombinant human Src protein
See all Src proteins and peptides
Protein lengthFull length protein
SourceBaculovirus infected Sf9 cells
Amino Acid Sequence
TagsHis tag N-Terminus
Our Abpromise guarantee covers the use of ab79635 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Biological activitySpecific Activity: 205 pmol/min/µg.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Preservative: 0.851% Imidazole
Constituents: 0.04627% DTT, 0.394% Tris HCl, 50% Glycerol, 0.403% Sodium chloride, 0.01006% Potassium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Avian sarcoma virus
- c SRC
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
ab79635 has not yet been referenced specifically in any publications.