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|Tested species reactivity||Human|
|Host / Isotype||E.coli|
|Storage buffer||TBS, pH 8.0, with 50% glycerol, 3mM DTT, 0.01M L-glutathione, 1.4mM KCl|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Control (Ctrl)||Assay dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
MEG2; protein-tyrosine phosphatase MEG2; PTPase MEG2; PTPase-MEG2; PTPN9
MEG2; PTPMEG2; PTPN9