PTEN, active

PTEN, active
by EMD Millipore, a division of Merck KGaA, Darmstadt, Germany


PTEN hydrolyzes phosphate at the 3 position on the inositol ring of PtdIns(3,4,5)P 3 , and Ins(1,3,4,5)P 4 . Although PTEN has the consensus sequence of a protein tyrosine phosphatase, it dephosphorylates p-nitrophenylphosphate and other synthetic and protein substrates poorly. The greatest catalytic activity has been observed with the highly negatively charged, multiply phosphorylated polymer of ...read more

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Description

 

PTEN hydrolyzes phosphate at the 3 position on the inositol ring of PtdIns(3,4,5)P3, and Ins(1,3,4,5)P4. Although PTEN has the consensus sequence of a protein tyrosine phosphatase, it dephosphorylates p-nitrophenylphosphate and other synthetic and protein substrates poorly. The greatest catalytic activity has been observed with the highly negatively charged, multiply phosphorylated polymer of (Glu-Tyr)n.

Product Overview

PTEN, active by EMD Millipore, a division of Merck KGaA, Darmstadt, Germany
PTEN, active

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