SRP5081
PTPRM (764-1452), GST tagged human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Sinónimos:
PTPRL1, R-PTP-MU, RPTPM, RPTPU, hR-PTPu
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About This Item
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~110 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PTPRM(5797)
General description
PTPRM is a member of the protein tyrosine phosphatase family and can participate in a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPRM has been shown to mediate cell-cell aggregation through the interaction with another molecule of PTPRM on an adjacent cell. PTPRM can interact with scaffolding protein RACK1/GNB2L1 and this interaction may be necessary for downstream signaling in response to cell-cell adhesion. PTPRM has been shown to be expressed in human pulmonary vascular endothelia where it directly binds to VE-cadherin and regulates both the tyrosine phosphorylation state of VE-cadherin and barrier integrity.
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_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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The Journal of biological chemistry, 281(8), 4903-4910 (2005-12-29)
The receptor protein-tyrosine phosphatase PTPmu is a member of the Ig superfamily of cell adhesion molecules. The extracellular domain of PTPmu contains motifs commonly found in cell adhesion molecules. The intracellular domain of PTPmu contains two conserved catalytic domains, only
The International journal of developmental biology, 47(5), 345-354 (2003-08-05)
The receptor-like protein tyrosine phosphatase mu (RPTPmu) belongs to the subfamily of meprin, A5, RPTPmu (MAM) domain-containing RPTPs, which are thought to play an important role in cell-cell adhesion mediated processes. The current study was designed to examine the expression
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