Anti-PTP1B (Tyr-152), Phosphospecific Antibody

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.

Our PTP1B (Tyr-152) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat PTP1B (Tyr-152) and is antigen affinity purified. It is great for use in WB.

PTP1B (Tyr-152) synthetic peptide corresponds to amino acids surrounding Tyr-152 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.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

This antibody was cross-adsorbed to a phospho-tyrosine peptide then affinity purified with phospho-PTP1B (Tyr-152) peptide. The purified antibody detects a 50 kDa* band corresponding to PTP1B in western blots of pervanadate treated human A431 and Jurkat, as well as mouse SYF cells. This reactivity is not observed in control cells or after alkaline phosphatase treatment of blots.