SRP5078
PTPRA (174-802), active, GST tagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
HEPTP, HLPR, HPTPα, HPTPA, PTPA, PTPRL2, R-PTP-α, RPTPA
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About This Item
recombinant
expressed in E. coli
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
1799-2435 nmol/min·mg
mol wt
~96 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PTPRA(5786)
General description
PTPRA (also known as LRP) is a member of the protein tyrosine phosphatase family and contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. PTPRA dephosphorylates SRC family kinases, potassium channels and NMDA receptors and exists as three alternatively spliced variants which encode two distinct isoforms. Absence of PTPRA compromises correct positioning of pyramidal neurons during development of mouse hippocampus.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Proceedings of the National Academy of Sciences of the United States of America, 87(12), 4444-4448 (1990-06-01)
Protein-tyrosine-phosphatases (protein-tyrosine-phosphate phosphohydrolase, EC 3.13.48) have been implicated in the regulation of cell growth; however, to date few tyrosine phosphatases have been characterized. To identify additional family members, the cDNA for the human tyrosine phosphatase leukocyte common antigen (LCA; CD45)
The EMBO journal, 22(16), 4121-4131 (2003-08-13)
Despite clear indications of their importance in lower organisms, the contributions of protein tyrosine phosphatases (PTPs) to development or function of the mammalian nervous system have been poorly explored. In vitro studies have indicated that receptor protein tyrosine phosphatase alpha
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