|Detection of Human/Mouse/Rat PTP1B by Western Blot. Western blot shows lysates of MCF-7 human breast cancer cell line, PC-12 rat adrenal pheochromocytoma cell line, and L-929 mouse fibroblast cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat PTP1B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF13661) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for PTP1B at approximately 50 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 1.|
Detection of Human PTP1B by Simple WesternTM. Simple Western lane view shows lysates of MCF‑7 human breast cancer cell line, loaded at 0.2 mg/mL. A specific band was detected for PTP1B at approximately 57 kDa (as indicated) using 10 µg/mL of Goat Anti-Human/Mouse/Rat PTP1B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF13661) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
Protein tyrosine phosphatase 1B (PTP1B) is an enzyme that removes phosphate groups covalently attached to tyrosine residues in proteins. This ubiquitously expressed enzyme is anchored in the endoplasmic reticulum by its C-terminal end and has its catalytic regions exposed to the cytosol. The recombinant protein lacks the C-terminal 114 amino acids but is fully active. PTP1B will dephosphorylate a wide variety of phosphoproteins, such as receptors for the growth factors insulin and epidermal growth factor (EGF), c-Src and beta -catenin. Of particular interest is the observation that PTP1B knock-out mice are resistant to high-caloric intake-induced obesity and have exaggerated insulin responses, suggesting that PTP1B may play an important role in regulating growth factor responsiveness.