PTP1B, Human, Recombinant, E. coli

Research area: Cell Signaling

Recombinant, human PTP1B expressed in E. coli. PTP1B, an ubiquitous nontransmembrane protein tyrosine phosphatase, was originally identified in human placenta. This highly active enzyme is useful for the study of tyrosine phosphatase kinetics, substrate specificity, and for screening inhibitors. PTP1B comprises three domains: an N-terminal catalytic domain (1–300), a regulatory domain (301–400), and a C-terminal domain (401–435) that is accountable for directing the enzyme to the endoplasmic reticulum (ER) membrane.

Protein tyrosine phosphatase 1B (PTP1B), Human, Recombinant, E. coli has been used in the dephosphorylation assay of Glutathione S-transferase (GST) fusion proteins as well as in the in vitro kinase assays. It has also been used to construct a 66-member PTP1B library for discovery of enzyme inhibitors using click chemistry.

Protein tyrosine phosphatase 1B (PTP1B) serves as a crucial enzyme in dephosphorylating insulin receptor and its downstream signaling components. Furthermore, it participates in the negative regulation of the leptin signaling pathway by dephosphorylation of the upstream signaling molecules, leading to the suppression of the neuropeptide Y synthesis, an appetite-stimulating hormone. Improper functioning of PTP1B has been associated with a variety of human diseases, including cancer, diabetes, obesity and inflammation.

Please refer to vial label for lot-specific concentration.

Toxicity: Standard Handling (A)

One unit is defined as the amount of enzyme that will hydrolyze 1 µmol of phosphopeptide substrate (Cat. No. 539737) per min at 30°C, pH 7.2 using 150 µM of substrate.

In 50 mM HEPES, 1 mM DTT, 1 mM EDTA, 0.05% NP-40, pH 7.2.

Following initial thaw, aliquot and freeze (-70°C).

Puius, Y.A., et al. 1997. Proc. Natl. Acad. Sci. USA94, 13420.
Liu, F., et al. 1996. J. Biol. Chem.271, 31290.

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