Description
Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation, transformation, and synaptic strengthening.
Abbr
PTPase, Recombinant (Yersinia enterocolitica)
Species
Yersinia enterocolitica
Applications
Used to release phosphate groups specifically from phosphotyrosine residues in proteins.
Product Overview
recombinant, expressed in E. coli, > 50 kDa unit/mL, buffered aqueous glycerol solution
Form
buffered aqueous glycerol solution
Activity
> 50,000 unit/mL
Unit Definition
One unit is defined as the amount of enzyme that hydrolyzes 1 nmol of p-nitrophenyl phosphate (50 mM) in 1 minute at 30°C in a total reaction volume of 50 μl.
Buffer
Solution in 50 mM HEPESl, pH 7.0, at 25°C, 100 mM NaCl, 5 mM DTT, 0.01% Brij 35, 50% glycerol, and 2 mM Na2EDTA.
Synonyms
YOP Protein Tyrosine Phosphatase; Protein tyrosine phosphatase; Tyrosine-specific protein phosphatases; PTPase
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