SAA Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,766 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
SAA was lyophilized from 0.01M HCl (pH 2.0).
It is recommended to reconstitute the lyophilized SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Greater than 95.0% as determined by SDS-PAGE.
Safety Data Sheet
Serum Amyloid A (SAA), an acute-phase protein initially identified for its role in amyloidosis, has emerged as a versatile biomolecule with diverse functions in health and disease. As a major player in the acute-phase response, SAA is crucial for regulating inflammation, tissue repair, and lipid metabolism. The study of SAA Recombinant Protein has not only deepened our understanding of inflammatory processes but has also opened new avenues in diagnostics, therapeutics, and research. This research delves into the multifaceted world of SAA, exploring its molecular intricacies, physiological roles, and its implications in various biological contexts.
SAA, a family of apolipoproteins, exhibits remarkable structural diversity. Upon stimulation, hepatic cells secrete SAA into circulation, where it undergoes conformational changes and associates with high-density lipoproteins (HDL). This transformation is essential for its roles in cholesterol transport, immune modulation, and tissue regeneration, making SAA a key mediator in both normal physiology and pathological conditions.