PRL-2 (2-167) - Active Enzyme


Catalog number


Full name

PRL-2 (2-167) - Active Enzyme


10 μg


426.00 €

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Proteins & Peptides

Long description

Mouse PRL-2, also known as Protein tyrosine phosphatase 4a2 (Ptp4a2) is a unique nuclear protein tyrosine phosphatase (PTP) that plays a central role in regulating diverse cellular processes. PRL-1 is induced in mitogen-stimulated cells and regenerating liver. Mouse PRL-2 exhibit 87% identity to mouse PRL-1 in their amino acid sequences. All mouse PRL proteins contain a C-terminal consensus sequence for prenylation. All PRL proteins bear significant sequence homology to Cdc14p and the tumor suppressor PTEN/MMAC1. PRL-2 is preferentially expressed in skeletal muscle. PRL-2 is also expressed at lower levels in other tissues

Antibody come from

Synthetic phosphopeptide corresponding to amino acid residues surrounding the phospho Ser218/222 of human MEK1/2

Other description

Provided in HEPES (pH 7.5) solution containing 150 mM NaCl, 100 µg per ml BSA and 50% glycerol


not specified

Antigen-antibody binding interaction

PRL-2 (2-167) - 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

Antibody's specificity

No Data Available


Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

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.



Relevant references

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., 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_3. Ahn, N.G. 'The MAP kinase cascade. Discovery of a new signal transduction pathway,' Mol. Cell Biochem. 127-128, 201-209 (1993). _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. Park, S.H., et al. 'Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms,' Science 299, 1061-1064 (2003)._x000B__x000B_6. Chong H, Vikis HG, Guan KL (2003) Mechanisms of regulating the Raf kinase family. Cellular Signalling 15:463- 469._x000B__x000B_7. 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_8. 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.

Protein number

see ncbi


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.