Antibody type
Monoclonal antibodies
Immunogen
Purified recombinant human CrkII protein fragments expressed in E.coli.
Specificity
This antibody detects endogenous levels of CrkII and does not cross-react with related proteins.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification process
The antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen.
Other name
Adapter molecule crk;Avian sarcoma virus CT10 (v crk) oncogene homolog;CRK;CRK isoform 2;CRK isoform II;CRK_HUMAN;CRKII;FLJ38130;OTTHUMP00000115366;OTTHUMP00000198330;p38; Proto oncogene C crk;Proto-oncogene C-crk;v crk avian sarcoma virus CT10 oncogene homolog;v crk sarcoma virus CT10 oncogene homolog;v crk sarcoma virus CT10 oncogene homolog (avian).
Background
This gene encodes a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described. [provided by RefSeq, Jul 2008],
Function
domain:The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.,domain:The SH2 domain mediates interaction with SHB.,function:The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4.,PTM:Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.,PTM:P
