SRP5079
PTPRC (592-end), active, GST tagged from mouse
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
B220, CD45R, Cd45, Ly-5, Lyt-4, T200, loc
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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Specific activity:
8,415-11,385 nmol/min·mg
Assay:
≥70% (SDS-PAGE)
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
8,415-11,385 nmol/min·mg
mol wt
~116 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
mouse ... Ptprc(19264)
General description
Protein tyrosine phosphatase, receptor type, C (PTPRC) or CD45 contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus belongs to receptor type PTP. This gene is specifically expressed in hematopoietic cells.
Biochem/physiol Actions
Protein tyrosine phosphatase, receptor type, C (PTPRC) has been shown to be an essential regulator of T- and B-cell antigen receptor signaling. It functions through either direct interaction with components of the antigen receptor complexes, or by activating various Src family kinases required for the antigen receptor signaling.
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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E H Fischer et al.
Science (New York, N.Y.), 253(5018), 401-406 (1991-07-26)
Protein tyrosine phosphatases (PTPs) represent a diverse family of enzymes that exist as integral membrane and nonreceptor forms. The PTPs, with specific activities in vitro 10 to 1000 times greater than those of the protein tyrosine kinases would be expected
S J Ralph et al.
The EMBO journal, 6(5), 1251-1257 (1987-05-01)
Structural variation in the primary structure of human T200 glycoprotein has been detected. Three cDNA variants have been characterized each of which encode T200 molecules that differ in size as a result of sequence differences in their amino-terminal regions. The
Mutation in the CD45 Inhibitory Wedge Modulates Integrin Activation and Leukocyte Recruitment during Inflammation
Giulia Germena
Journal of Immunology (2015)