PTP1B (Ser-50), phospho-specific polyclonal, anti-human, mouse, rat

Background:
PTP1B is a nonreceptor type protein tyrosine phosphatase that has essential roles in insulin and leptin signaling, as well as important functions in growth factor and integrin signaling. The structure of PTP1B includes a conserved phosphatase domain, C-terminal hydrophobic residues for targeting to the cytoplasmic face of the endoplasmic reticulum, and proline-rich regions characteristic of SH3 domain binding motifs. PTP1B can interact with N-Cadherin and dephosphorylate β-catenin associated with cadherin complexes. PTP1B also interacts with Insulin and EGF receptors, and undergoes phosphorylation after receptor stimulation. Tyrosine phosphorylation at Tyr-66, Tyr-152, and Tyr-153 occurs after insulin receptor activation, and tyrosine phosphorylation of Tyr-152 may be required for interactions with N-Cadherin. In addition, Akt can phosphorylate Ser-50 and this phosphorylation can reduce PTP1B activity.

Immunogen: PTP1B (Ser-50) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Ser-50 in human PTP1B. This sequence has significant homology to the conserved site in rat and mouse PTP1B, and has homology to conserved sites in TC-PTP and MPTP, but not other protein tyrosine phosphatase family members.

Specificity: This antibody was affinity purified with phospho-PTP1B (Ser-50) peptide. The purified antibody detects a 50 kDa* doublet corresponding to PTP1B in western blots of calyculin A treated human A431 and Jurkat cells. This reactivity is observed as a weak singlet in control cells and is not observed after lambda phosphatase treatment.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.