Recombinant Mouse Serum Amyloid A2 Protein, CF
Recombinant Mouse Serum Amyloid A2 Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in Tris.|
|Reconstitution||Reconstitute at 250 μg/mL in sterile water.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Serum Amyloid A2
Mouse Serum Amyloid A2 (SAA2) is a multifunctional apolipoprotein produced by hepatocytes in response to pro-inflammatory cytokines (1, 2). It is secreted as a 12 kDa, non-glycosylated protein and circulates as part of the HDL complex (3, 4). The SAA2 gene is one of five SAA genes in mouse (5). SAA2 and SAA1 are categorized as acute phase (A)-SAA proteins based on their structural similarity and inducible expression during chronic inflammation. Mature mouse SAA2 shares 70% amino acid (aa) sequence identity with human SAA2 and 92% sequence identity with mouse SAA1. Secretion of SAA2 is increased during inflammation with amounts of total A-SAA increasing up to 1000-fold (6, 7). Increased levels of A-SAA in serum are indicative of inflammatory disease (8). When highly expressed, SAA can displace ApoA1 as the major apolipoprotein in HDL complexes, weakening the function of HDL as a reverse (lipid clearing) cholesterol transporter (2). A highly charged region of SAA2 and SAA1 (aa 36-68) contains putative fibronectin- and laminin-binding motifs (5). This region also binds heparin sulfate proteoglycans at mildly acidic pH and promotes aggregation of A-SAA (9, 10). Persistent production of A-SAA results in amyloid A amyloidosis, a chronic inflammatory condition that culminates in renal failure (10-12). Amyloidosis is triggered by tissue damage, infection, or other insults that result in prolonged inflammatory cytokine activity. SAA2 selectively accumulates in amyloid fibril deposits during amyloidosis. Circulating levels of total A-SAA decrease during active amyloidosis due to the sequestration of SAA2 into amyloid depositions (13, 14). Mouse strains can differ in SAA sequence, expression and amyloid formation (15).
- Thorn, C.F. and A.S. Whitehead (2002) Amyloid 9:229.
- Benditt, E.P. et al. (1979) Proc. Natl. Acad. Sci. U.S.A. 76:4092.
- Hoffman, J.S. et al. (1984) J. Exp. Med. 159:641.
- Uhlar, C.M. and A.S. Whitehead (1999) Eur. J. Biochem. 265:501.
- van der Westhuyzen, D.R. et al. (2007) Curr. Opin. Lipidol. 18:147.
- Hebert, L. and F. Gervais (1990) Scand. J. Immunol. 31:167.
- Kluve-Beckerman, B. et al. (1997) Biochem. J. 322(Pt 2):663.
- Lu, J. et al. (2014) Proc. Natl. Acad. Sci. U.S.A. 111:5189.
- Elimova, E. et al. (2009) FASEB J. 23:3436.
- Yu, J. et al. (2000) Lab. Invest. 80:1797.
- Jaffe, R.H. (2001) Arch. Pathol. Lab. Med. 125:25.
- Yu, J. et al. (2000) Amyloid 7:32.
- Meek, R.L. et al. (1986) J. Exp. Med. 163:499.
- Simons, J.P. et al. (2013) Proc. Natl. Acad. Sci. U.S.A. 110:16115.
- Mori, M. et al. (2014) Exp. Anim. 63:99.
Citation for Recombinant Mouse Serum Amyloid A2 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
High-density lipoprotein inhibits serum amyloid A-mediated reactive-oxygen species generation and NLRP3 inflammasome activation
Authors: P Shridas, MC De Beer, NR Webb
J. Biol. Chem., 2018;0(0):.
Sample Types: Whole Cells
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