Proteins & Peptides
The product of the PRL-1 gene (alternate gene names PTP4A1 Synonyms:ÊDKFZp779M0721, hPTPCAAX1) is a protein tyrosine phosphatase also known as phosphatase of regenerating liver, Protein tyrosine phosphatase type IVA, member 1, PTPCAAX1 or Hypothetical protein DKFZp779M0721. Protein tyrosine phosphatases play important roles in the regulation of cell growth, development, and differentiation. PRL-1 is one of the most interesting immediate early growth response genes in regenerating liver. The gene encodes a novel 20-kDa nuclear protein tyrosine phosphatase. Other than the signature sequence for PTPases, PRL-1 is not homologous to either the dual specificity PTPases (cdc25 and MKP-1) or monospecific PTPases. PRL-1 is elevated throughout the major proliferative phase of liver regeneration when hepatocytes and nonparenchymal cells in the liver are rapidly proliferating. PR-1 is also expressed at high levels in other proliferating cells including tumor cell lines such as hepatomas. PRL-1-transfected cells showed altered growth characteristics, including a faster doubling time, growth to a greater saturation density, altered morphology, and evidence of anchorage-independent growth. Overexpression of human PRL-1 in epithelial cells results in tumor formation in_x000B_nude mice.
Antibody come from
Synthetic phosphopeptide corresponding to amino acid residues surrounding the phospho Thr386 of human MEK1
Provided in HEPES (pH 7.5) solution containing 150 mM NaCl, 100 µg per ml BSA and 50% glycerol .
Antigen-antibody binding interaction
PRL-1 (2-173) N termnal GST tag - Active Enzyme
Antibody is raised in
Antibody's reacts with
Antibody's reacts with these species
This antibody doesn't cross react with other species
No Data Available
Useful for the study of enzyme kinetics, regulation, to dephosphorylate target substrates and for screening inhibitors.
Antibody's suited for
Antibody should be used at a 1:1000 dilution to provide for 10 miniblots in Western blotting and dot blots. Antibody detects only phosphorylated protein and does not detect non-phosphorylated protein as shown by the lack of ability of a non-phospho peptide to block the antibody activity. Optimal concentration may be evaluated by serial dilutions.
1. Adams, J.P. and Sweatt, J.D. 'Molecular psychology: Roles for the ERK MAP kinase cascade in memory,' Annu. Rev. Pharmacol. Toxicol. 42, 135-163 (2002). _x000B__x000B_2. Ahn, N.G. 'The MAP kinase cascade. Discovery of a new signal transduction pathway,' Mol. Cell Biochem. 127-128, 201-209 (1993). _x000B__x000B_3. Ahn, N.G., et al. 'Identification of an activator of the microtubule-associated protein 2 kinases ERK1 and ERK2 in PC12 cells stimulated with nerve growth factor or bradykinin,' J. Neurochem. 59, 147-156 (1992). _x000B__x000B_4. Crews, C.M., et al. 'The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product,' Science 258, 478-480 (1992). _x000B__x000B_5. Mansour, S.J., et al. 'Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis.' J. Biochem. (Tokyo) 116, 304-314 (1994). _x000B__x000B_6. Park, S.H., et al. 'Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms,' Science 299, 1061-1064 (2003)._x000B__x000B_7. Chong H, Vikis HG, Guan KL (2003) Mechanisms of regulating the Raf kinase family. Cellular Signalling 15:463- 469._x000B__x000B_8. Kyriakis JM, Brautigan DL, Ingebritsen TS, Avruch J (1991) pp54 Microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity. J Biol Chem 266:10043-10046._x000B__x000B_9. Seger R, Ahn NG, Boulton TG, Yancopoulos GD, Panayotatos N, Radziejewska E, Ericsson L, Bratlien RL, Cobb MH, Krebs EG (1991) Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophos- phorylation on both tyrosine and threonine residues: Implications for their mechanism of activation. Proc Natl Acad Sci USA 88:6142-6146.
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.
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.