MEG-2 (285-593)/PTPN9 - Active Enzyme


Catalog number


Full name

MEG-2 (285-593)/PTPN9 - Active Enzyme


20 μg


426.00 €

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Proteins & Peptides

Long description

MEG-2 also known as PTPN9 is a protein-tyrosine phosphatase originally isolated from peripheral neutrophilic polymorphonuclear leukocytes (PMN). MEG2 is predominantly cytosolic with components present in secondary and tertiary granules and secretory vesicles. MEG2 activity is inhibited after exposure of cells to opsonized zymosan or to phorbol 12-myristate 13-acetate but largely unaffected by the f-met-leu-phe (N-formyl-methionyl-leucyl-phenyalanine). Cysteine 515 is essential for catalytic activity of MEG-2, whereas the noncatalytic (N-terminal) domain of MEG2 negatively regulates the enzymatic activity of the C-terminal phosphatase domain. The activity of MEG2 is enhanced by specific polyphosphoinositides. MEG2 associates at an early stage with nascent phagosomes. MEG2 is a polyphosphoinositide-activated tyrosine phosphatase that may be involved in signaling events regulating phagocytosis, and essential antimicrobial function in the immune response.

Antibody come from

Synthetic phosphopeptide corresponding to amino acid residues surrounding the phosphorylated Ser383 of human Elk-1

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

MEG-2 (285-593)/PTPN9 - 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


Study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Antibody's suited for

Antibody can be used for Western blot and dot blot (1:1000 dilution). Optimal concentration should be evaluated by serial dilutions.



Relevant references

1. Hill, C.S. and Treisman, R. 'Transcriptional regulation by extracellular signals: mechanisms and specificity,' Cell 80, 199-211 (1995)._x000B__x000B_2. Li, Q.J., et al. 'MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the coactivator p300,' EMBO J. 22, 281-291 (2003)._x000B__x000B_3. Thiels, E., et al. 'Long-term depression in the adult hippocampus in vivo involves activation of extracellular signal-regulated kinase and phosphorylation of Elk-1,' J. Neurosci. 22, 2054-2062 (2002).

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.