Phospho-CDCP1 (Tyr707) Antibody recognizes endogenous levels of CDCP1 protein only when phosphorylated at Tyr707. This antibody does not cross-react with CDCP1 phosphorylated at Tyr734, Tyr743, or Tyr806, but may cross react with other phospho-tyrosine containing proteins. The identity of the 80 kDa band in the Cub1 antibody treated ZR-75-1 cell extract is not known.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr707 of human CDCP1 protein. Antibodies are purified by protein A and peptide affinity chromatography
Background
CUB domain containing protein 1 (CDCP1, SIMA135) is a putative stem cell marker shown in research studies to be highly expressed in some human cancer cells and in both typical and atypical (cancerous) colons (1). Expression of CDCP1 may be epigenetically regulated, as methylation of promoter CpG sequences results in decreasedCDCP1 expression (2). The correspondingCDCP1gene encodes a glycoprotein that acts as a complex, multidomain transmembrane antigen. CDCP1 has three extracellular CUB domains that may be involved in cell adhesion or extracellular matrix interactions (1,3). Src-family kinases may phosphorylate CDCP1 at five tyrosine residues within its cytoplasmic domain to provide a potential binding site for SH2 domain-containing proteins (3). CDCP1 is a putative hematopoietic stem cell marker (4,5).