Abcam’s Serum Amyloid A (SAA) Mouse ELISA kit is an in vitro enzyme-linked immunosorbent assay (ELISA) for the quantitative measurement of Serum Amyloid A in mouse samples.
In this assay the Serum Amyloid A present in samples reacts with the anti-Serum Amyloid A antibodies which have been adsorbed to the surface of polystyrene microtitre wells. After the removal of unbound proteins by washing, anti-Serum Amyloid A antibodies conjugated with horseradish peroxidase (HRP), are added. These enzyme-labeled antibodies form complexes with the previously bound Serum Amyloid A. Following another washing step, the enzyme bound to the immunosorbent is assayed by the addition of a chromogenic substrate, 3,3’,5,5’-tetramethylbenzidine (TMB). The quantity of bound enzyme varies directly with the concentration of Serum Amyloid A in the sample tested; thus, the absorbance, at 450 nm, is a measure of the concentration of Serum Amyloid A in the test sample. The quantity of Serum Amyloid A in the test sample can be interpolated from the standard curve constructed from the standards, and corrected for sample dilution.
The serum amyloid A (SAA) family comprises a number of differentially expressed lipoproteins, acute phase SAA1 and SAA2, the former being a major component in plasma, and constitutive SAA's (C-SAAs). Although the liver is the primary site of synthesis of both SAA types, extrahepatic production has been reported. The in vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed it's importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations. SAA rises earlier and more sharply than CRP.
SAA enhances the binding of HDL's to macrophages and thus helps the delivery of lipid to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease process. In addition, recent experiments suggest that SAA may play a "houekeeping" role in normal human tissues. Elevated levels of SAA over time predispose secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissues and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid artheritis.
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