Human SHP-1 Antibody

Src-Homology 2 domain Phosphatase-1 (SHP-1), also known as Protein Tyrosine Phosphatase 1C (PTP1C), PTPN6, and Hematopoetic Cell Phosphatase (HCPH), is an enzyme that selectively dephosphorylates tyrosine residues in proteins. Spontaneous point mutations in the SHP-1 gene in mice produce the “motheaten” and "motheaten viable” phenotypes that are severely autoimmune and immunodeficient (1). The enzyme is highly expressed in leukocyte cell types (2). SHP-1 has a regulatory region containing two Src homology 2 (SH2) domains that are critical for its binding to ITIM domains in inhibitory immunoreceptors (3). Deletion of the SH2 domains, as in this product, causes a marked increase in phosphatase activity (4). SHP-1 will dephosphorylate a wide variety of proteins, including the EGF receptor (5). A phosphopeptide containing the EGFR (Y992) sequence (R&D Systems, Catalog # ES006) can be used to measure the activity of SHP-1 by detecting the release of phosphate (R&D Systems, Catalog # DY996).