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PTP-BL - catalytic domain

Protein tyrosine phosphatase Basophil-like

mouse, recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-308 20 μg 218,50 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Accession number: Z32740

Accession number: Z32740

Purity: > 95 % (SDS-PAGE)

Form: liquid (Supplied in 50 mM Tris-HCl pH 7.5, 100 mM NaCl and 1 mM DTT)

pH: 7.5

Activity: 11 μmol/min/mg determined with pNPP as substrate at pH 7.4 and 37°C.

Protein Tyrosin Phosphatase, catalytic domain. Protein Tyrosine Phosphatase-Basophil-like (PTP-BL)is a large nonreceptor type protein tyrosine phosphatase caracterized by the presence of a extreme N-terminal KIND domain (kinase noncatalytic C-lobe domain, a protein module identified recently that shows homology to the regulatory C-lobe of protein kinases but that lacks catalytic activity), a N-terminal FERM domain (four point one, ezrin, radixin, moesin homology domain), five PDZ (postsynaptic density protein-95, discs large, zonula occludens) regions and a C-terminal catalytically active domain. Current data suggest that PTP-BL is involved in regulation of cytoskeleton and of intracellular vesicular transport processes.

Selected References:
Hendriks et al. (1995) Molecular cloning of a mouse epithelial proteintyrosine phosphatase with similarities to submembranous proteins. J. Cell. Biochem. 59:418.
Erdmann et al. (2003) The protein tyrosine phosphatase PTPBasophil/ Basophil-like. Interacting proteins and molecular functions. Eur. J. Biochem. 270:4789.
Herrmann et al. (2003) The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. Mol. Biol. Cell. 14:230.