The serum amyloid A (SAA) family comprises a number of differentially expressed apolipoproteins, acute-phase SAA1 and SAA2, the former being the major component in plasma, and constitutive SAAs (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 stressed its 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. Recently, a broader view of SAA expression and function has been emerging. Expression studies show production of SAA proteins in histologically normal, atherosclerotic, Alzheimer, inflammatory, and tumor tissues. SAA has been found to have binding sites for high density lipoproteins, calcium, laminin, and heparin/heparan-sulfate. Also adhesion motifs were identified and new functions, affecting cell adhesion, migration, proliferation and aggregation discovered. These findings emphasize the importance of SAA in various physiological and pathological processes, including inflammation, atherosclerosis, thrombosis, AA-amyloidosis, rheumatoid arthritis, and neoplasia.
Applications:
Suitable for use in ELISA and Western Blot. Other applications not tested.
Recommended Dilutions:
Western Blot: 0.1-0.5ug/ml allows visualization of 100ng/lane of rhSAA.
Optimal dilutions to be determined by the researcher.
Hybridoma:
Sp2/0-Ag14 myeloma cells with spleen cells from Balb/c mice.
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.