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Category
Proteins & Peptides
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Long description
RPTP gamma, also known as Receptor-type tyrosine-protein phosphatase gamma, R-PTP-gamma or PTPRG is a protein tyrosine phosphatase (PTP) is a candidate tumor suppressor gene since it is located on human chromosome 3p14.2-p21, a region frequently deleted in certain types of renal and lung carcinomas. In situ hybridization analysis reveals that RPTP gamma mRNA is expressed in specific regions of the brain and that the localization of RPTP gamma changes during brain development. RPTP gamma is composed of a putative extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic tyrosine phosphatase domains. The extracellular domain contains a stretch of 266 amino acids with striking homology to the zinc-containing enzyme carbonic anhydrase (CAH), indicating that RPTP gamma and RPTP beta (HPTP zeta) represent a subfamily of receptor tyrosine phosphatases. RPTP gamma may have a function other than catalysis of hydration of metabolic CO2. _x000B_ _x000B__x000B_
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Antibody come from
Sythetic peptide corresponding to amino acid residues surrounding the phospho-Ser831 of rat GluR1.
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Other description
Provided in HEPES (pH 7.5) solution containing 150 mM NaCl, 100 µg per ml BSA and 50% glycerol .
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Clone
not specified
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Antigen antibody binding interaction
RPTPgamma (801-1147) N Terminal GSTS Tag - Active Enzyme
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Antibody is raised in
E.coli
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Antibody s reacts with
Human
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Antibody s reacts with these species
This antibody doesn't cross react with other species
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Antibody s specificity
No Data Available
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Application
Study of enzyme kinetics, regulation and to dephosphorylate target substances
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Antibody s suited for
Antibody can be used for dot blot and Westen blot (1:1000 dilution). Optimal concentration should be evaluated by serial dilutions.
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Storage
-20ºC
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Relevant references
1. Hollmann M, Heinemann S (1994) Cloned glutamate receptors. Annu Rev Neurosci 17:31-108._x000B__x000B_2. KeinŠnen K, Wisden W, Sommer B, Werner P, Herb A, Verdoorn TA, Sakmann B, Seeburg PH (1990) A family of AMPA-selective glutamate receptors. Science 249:556-560._x000B__x000B_3. Mammen AL, Kameyama K, Roche KW, Huganir RL (1999) Phosphorylation of the a-amino-3-hydroxy-5- methylisoxazole-4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J Biol Chem 272:32528-32533._x000B__x000B_4. McGlade-Mcculloh E, Yamamoto H, Tan S-E, Brickey DA, Soderling TR (1993) Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II. Nature (London) 362:640-642._x000B__x000B_5. Roche KW, O'Brien RJ, Mammen AL, Bernhardt J, Huganir RL (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16:1179-1188._x000B__x000B_6. Soderling TR, Derkach VA (2000) Postsynaptic protein phosphorylation and LTP. Trends Neurosci 23:75-80.
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Protein number
see ncbi
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Warnings
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
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Description
Enzymes are cleaving the substrate. If the substrate is DNA they are called restriction enzymes. Activating enzymes will cut off the domain that is biological active to become functional.
