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c-PLA2 (N499) pAb

c-PLA2 (N499) pAb

Cat no: BS1434

Supplier: Bioworld Technology, Inc.
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Phospholipase A2s (PLA2s) constitute a family of esterases that hydrolyze the sn-2-acyl ester bond in glycerophospholipid molecules. These enzymes are generally calcium-dependent and have been found both intra- and extracellularly. By hydrolyzing the sn-2 bond in glycerophospholipids, PLA2s release fatty acids. One such fatty acid, arachidonic acid, generates the substrates for the initiation of the arachidonic acid cascade that produces various eicosanoids (i.e. prostaglandins, leukotrienes and thromboxanes), many of which are potent mediators of inflammation. PLA2s include both the relatively low molecular weight type I and type II enzymes and the form known as cytoplasmic PLA2 (cPLA2). cPLA2 is present in the cytosol of various cells and tissues including platelets, macrophages and monoblasts; and preferentially hydrolyzes the sn-2 position of phospholipid molecules, releasing free arachidonate.
Catalogue number: BS1434
Reactivities: Human, Mouse, Rat
Hosts: Rabbit
Applications: Immunofluorescence, Immunohistochemistry, Western Blot
Size: 100ug/100ul
Swiss prot: P47712
Dilutions: WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Form: liquid
Storage buffer: 1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Concentration: 1ug/ul
Antigen: Synthetic peptide, corresponding to amino acids 480-530 of Human c-PLA2.
Species: c-PLA2 (N499) pAb detects endogenous levels of c-PLA2 protein.
Molecular weight: ~ 100 kDa
Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage temp: Store at 4 degrees C short term. Aliquot and store at -20 degrees C long term. Avoid freeze-thaw cycles.
Alternative names: CPLA 2; cPLA2 alpha; cPLA2; Cytosolic phospholipase A2; Phospholipase A2 group IVA; PhospholipaseA2; PLA2G4; Pla2g4a;
Additional info: For research use only, not for use in diagnostic procedure.

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