Protein Tyrosine Phosphatase 1B human

Protein Tyrosine Phosphatase 1B (PTP1B) human has been used in treating cell lysate prior to immunoprecipitation and protein pull-down studies. It has also been used in PTP1B activity assay and also for the evaluation of inhibitors like betulinic acid (BA) and sodium orthovanadate (Na3VO4), and 6-chloro-3-formyl-7-methylchromone (CFM) on PTP1B.

Protein tyrosine phosphatase 1B (PTP1B) is a pharmaceutical target used to study the treatment of various diseases such as obesity, cancer and type II diabetes mellitus.

The inhibitory effect of 8-(4-chlorophenylthio)-cAMP and 8-(4-chlorophenylthio)-cGMP on protein tyrosine phosphatase-1B has been assayed.

PTP-1B is a recombinant, non-transmembrane protein expressed in E. coli containing amino acid residues 1-322 of human PTP-1B. It has a molecular mass of 37.4 kDa. It is an abundant intracellular enzyme that is thought to act as a negative regulator of certain signaling pathways. It dephosphorylates tyrosine-phosphorylated proteins and peptides, and is usually localized in the cytostolic domain of the ER.

PTP1B dephosphorylates c-Src in several human breast cancer cell lines has a regulatory role for PTP1B in the control of c-Src kinase activity. PTP1B is regulates the cardiovascular effects of leptin. PTP1B controls the JAK/STAT signaling pathway by dephosphorylation of JAK2.

Polymorphism in the gene PTPN1 is associated with type 2 diabetes and obesity.

Protein tyrosine phosphatase 1B human (PTP1B) is encoded by the gene PTPN1. In human chromosome, the gene PTPN1 is localized on 20q13.13. The protein has 37 kDa catalytic domain and the C-terminal hydrophobic residues targets the protein to the cytoplasmic side of the endoplasmic reticulum membrane.

One unit will hydrolyze 1.0 μmole of a phosphopeptide, EGFR fragment 988-998, per minute at pH 7.2 at 30 °C

Supplied as a solution in 50 mM HEPES (pH 7.2), 1 mM EDTA, 5 mM DTT, and 0.05% NP-40