PTP epsilon protein (Active) (ab128555)
Constituents: 0.31% Glutathione, 0.02% PMSF, 0.004% DTT, 0.79% Tris HCl, 0.003% EDTA, 25% Glycerol, 0.88% Sodium chloride
Our Abpromise guarantee covers the use of ab128555 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||WB: Use at an assay dependent dilution. Predicted molecular weight: 81 kDa.|
|Functional Studies||FuncS: Use at an assay dependent concentration.|
|SDS-PAGE||SDS-PAGE: Use at an assay dependent concentration.|
- HPTPEProtein tyrosine phosphatase epsilonProtein tyrosine phosphatase receptor type EProtein tyrosine phosphatase receptor type epsilonProtein tyrosine phosphatase receptor type epsilon polypeptideProtein-tyrosine phosphatase epsilonPTPEPtprePTPRE_HUMANR PTP EpsilonR-PTP-epsilonReceptor-type tyrosine-protein phosphatase epsilon
Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake.
Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).
Contains 2 tyrosine-protein phosphatase domains.
modificationsA catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.
Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu.
Isoform 1 is glycosylated.
PTP epsilon protein (Active) images
SDS Page analysis of ab128555
The specific activity of ab128555 was determined to be 8,600 nmol/min/mg.
References for PTP epsilon protein (Active) (ab128555)
ab128555 has not yet been referenced specifically in any publications.