Information
Catalog number
X1662E
Full name
MEG-2 (285-593)/PTPN9 - Active Enzyme
Size
20 μg
Price
426.00 €
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Category
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 .
Clone
not specified
Antigen-antibody binding interaction
MEG-2 (285-593)/PTPN9 - Active Enzyme
Antibody is raised in
E.coli
Antibody's reacts with
Human
Antibody's reacts with these species
This antibody doesn't cross react with other species
Antibody's specificity
No Data Available
Application
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.
Storage
-20ºC
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
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.
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.