The antiserum was produced against synthesized peptide derived from human CrkII around the phosphorylation site of Tyr221. AA range:187-236

Phospho-Crk II (Y221) Polyclonal Antibody detects endogenous levels of Crk II protein only when phosphorylated at Y221.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):GPyAQ

CRK

Adapter molecule crk

CRK ;
Adapter molecule crk ;
Proto-oncogene c-Crk ;
p38

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],

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:Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form.,similarity:Contains 1 SH2 domain.,similarity:Contains 1 SH3 domain.,similarity:Contains 2 SH3 domains.,subcellular location:Translocated to the plasma membrane upon cell adhesion.,subunit:Interacts with ABL1, C3G, SOS, MAP4K1, MAPK8 and DOCK3 via its first SH3 domain. Interacts with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 via its SH2 domain upon stimulus-induced tyrosine phosphorylation. Interacts with several tyrosine-phosphorylated growth factor receptors such as EGFR, PDGFR and INSR via its SH2 domain (By similarity). Interacts with DOCK1 and DOCK4. Interacts with SHB.,

Cytoplasm . Cell membrane . Translocated to the plasma membrane upon cell adhesion. .

>>MAPK signaling pathway ;
>>ErbB signaling pathway ;
>>Rap1 signaling pathway ;
>>Chemokine signaling pathway ;
>>Focal adhesion ;
>>Fc gamma R-mediated phagocytosis ;
>>Neurotrophin signaling pathway ;
>>Regulation of actin cytoskeleton ;
>>Insulin signaling pathway ;
>>Growth hormone synthesis, secretion and action ;
>>Bacterial invasion of epithelial cells ;
>>Shigellosis ;
>>Yersinia infection ;
>>Human cytomegalovirus infection ;
>>Human immunodeficiency virus 1 infection ;
>>Pathways in cancer ;
>>MicroRNAs in cancer ;
>>Renal cell carcinoma ;
>>Chronic myeloid leukemia