Key features and details
- Sensitivity: 10.7 ng/ml
- Range: 31.25 ng/ml - 2000 ng/ml
- Sample type: Plasma, Serum
- Detection method: Colorimetric
- Assay type: Sandwich (quantitative)
- Reacts with: Mouse
Product nameMouse SAA ELISA Kit
Intra-assay Sample n Mean SD CV% Overall < 10% Inter-assay Sample n Mean SD CV% Overall < 10%
Sample typeSerum, Plasma
Assay typeSandwich (quantitative)
Range31.25 ng/ml - 2000 ng/ml
Sample specific recovery Sample type Average % Range Serum > 85 % - %
Assay durationMultiple steps standard assay
Species reactivityReacts with: Mouse
Mouse SAA 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 SAA present in samples reacts with the anti-SAA antibodies which have been adsorbed to the surface of polystyrene microtitre wells. After the removal of unbound proteins by washing, anti-SAA 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 SAA 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 SAA in the test sample can be interpolated from the standard curve constructed from the standards, and corrected for sample dilution.
Storage instructionsStore at +4°C. Please refer to protocols.
Components 1 x 96 tests 100X HRP-conjugated anti-mouse SAA antibody 1 x 150µl 20X Wash Buffer Concentrate 1 x 50ml 5X Diluent Concentrate 1 x 50ml Chromogen Substrate Solution 1 x 12ml Mouse SAA Calibrator (lyophilized) 1 vial Mouse SAA ELISA Microplate 1 unit Stop Solution 1 x 12ml
RelevanceThe 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.
- Amyloid fibril protein AA
- Amyloid protein A
ab157723 has been referenced in 11 publications.
- Larsen IS et al. Human Paneth cell a-defensin 5 treatment reverses dyslipidemia and improves glucoregulatory capacity in diet-induced obese mice. Am J Physiol Endocrinol Metab N/A:N/A (2019). PubMed: 30860877
- Meng X et al. DNA damage repair alterations modulate M2 polarization of microglia to remodel the tumor microenvironment via the p53-mediated MDK expression in glioma. EBioMedicine 41:185-199 (2019). PubMed: 30773478
- Burgess SL et al. Intestinal parasitic infection alters bone marrow derived dendritic cell inflammatory cytokine production in response to bacterial endotoxin in a diet-dependent manner. PLoS Negl Trop Dis 13:e0007515 (2019). PubMed: 31260452
- Ganeshan K et al. Energetic Trade-Offs and Hypometabolic States Promote Disease Tolerance. Cell 177:399-413.e12 (2019). PubMed: 30853215
- Wilson PG et al. Serum Amyloid A Is an Exchangeable Apolipoprotein. Arterioscler Thromb Vasc Biol 38:1890-1900 (2018). PubMed: 29976766