Product nameRecombinant Human PTPRE protein
See all PTPRE proteins and peptides
Protein lengthProtein fragment
Amino Acid Sequence
Amino acids511 to 600
TagsGST tag N-Terminus
Our Abpromise guarantee covers the use of ab159287 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesProtein concentration is above or equal to 0.05 mg/ml.
This product was previously labelled as PTP epsilon
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
FunctionIsoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function.
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+).
Tissue specificityExpressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells).
Sequence similaritiesBelongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily.
Contains 2 tyrosine-protein phosphatase domains.
DomainThe tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity.
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.
Cellular localizationCytoplasm; Cell membrane and Cytoplasm. Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane.
- Information by UniProt
ab159287 has not yet been referenced specifically in any publications.