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Category
Proteins & Peptides
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Long description
PTP beta, also known as Receptor-type tyrosine-protein phosphatase beta [Precursor], Protein-tyrosine phosphatase beta,R-PTP-beta, PTPRB or PTPB is a protein tyrosine phosphatase and is overexpressed in glioblastoma tumors. PTP beta plays a n important functional role in tumor cell migration and adhesion. Glioblastomas express at least three splice variants of PTPbeta, including long and short receptor forms. The short form of PTPbeta lacks exon 12, which encodes 860 amino acids located in the extracellular domain. In normal brain tissue and graded astrocytomas the long and short PTPbeta forms have an overlapping expression pattern. U87 stable cell lines overexpressing long or short PTPbeta migrate faster and adhere more robustly than parental U87 cells. The involvement of long and short PTPbeta in glioma tumor cell biology also contributes to the value of PTPbeta as a cancer target.
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Antibody come from
Synthetic phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser58 of tryptophan hydroxylase.
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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
PTPbeta (1675-1996) N Terminal GST 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
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
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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. Banik, U., et al. 'Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins,' J. Biol. Chem. 272 (1997) 26,219 Ð 26,225._x000B__x000B_2. Jiang, G.C., et al. 'Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling,' J. Mol. Biol. 302 (2000) 1005 - 1017._x000B__x000B_3. Johansen, P.A., et al. 'Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A,' J. Neurochem. 66 (1996) 817 - 823._x000B__x000B_4. Johansen, P.A., et al. 'Tryptophan hydroxylase is phosphorylated by protein kinase A,' J. Neurochem. 65 (1995) 882 - 888._x000B__x000B_5. Kuhn, D.M., et al. 'Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A,' J. Neurochem. 68 (1997) 2220 - 2223._x000B__x000B_6. Kumer, S.C., et al. 'Amino-terminal analysis of tryptophan hydroxylase: protein kinase phosphorylation occurs at serine-58,' J. Neurochem. 69 (1997) 1738 - 1745._x000B__x000B_7. Martinez, A., et al. 'A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis,' Curr. Med. Chem. 8 (2001) 1077 - 1091.
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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.
