Recombinant Mouse SAA1 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10080P

Recombinant Mouse SAA1 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10080P
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Product Overview

Host Species Mouse
Accession P05366
Synonym amyloid A, serum Amyloid fibril protein AA Amyloid protein A MGC111216 PIG4 SAA SAA2 Serum amyloid A protein serum amyloid A-1 protein serum amyloid A1 TP53I4 Tumor protein p53 inducible protein 4
Description Recombinant Mouse SAA1 Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 28 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Major acute phase protein.
Subcellular Location Secreted.
Protein Families SAA family
Database References
Tissue Specificity Detected in blood plasma (at protein level). Detected in liver.

Gene Functions References

  1. Study concludes that the transfer of serum amyloid A1 protein depends on direct cell-to-cell contacts or tunneling nanotubes. PMID: 28361953
  2. High SAA1 expression in the stromal component is associated with pancreatic tumors. PMID: 29351990
  3. findings show that high-density lipoprotein binding blocks fibril formation from soluble SAA1 protein, whereas internalization into mononuclear phagocytes leads to formation of amyloid; SAA1 aggregation in the cell model disturbs the integrity of vesicular membranes and leads to lysosomal leakage and apoptotic death PMID: 28637682
  4. These findings suggest that A-SAA is functionally linked to pulmonary inflammation in this O3 exposure model and that A-SAA could be an important systemic signal of O3 exposure to the CNS.- PMID: 28533327
  5. SAA and TLR4 have a role in skin inflammation PMID: 27502577
  6. Data indicate that SAA1 overexpressing mice (TG) show significant deficits in social behaviors, including impaired social recognition and reduced social interaction. Study detected exogenous SAA1 expression in the brain of TG mice, implying that liver-derived SAA1 migrates to the brain. Results show an increase in the accumulation of the 87kDa form of Abeta in TG mice compared to wild type mice. PMID: 27608955
  7. Sustained, elevated levels of SAA1 were correlated with metabolic parameters and local cytokine expression in the liver following 16 weeks on the high-fat diet. We suggest that SAA1-derived amyloid deposition under long-term high-fat diet exposure may be associated with the complications of high-fat diet-induced obesity and metabolic disorders. PMID: 27218680
  8. Serum Amyloid A induces inflammation, proliferation and cell death in activated hepatic stellate cells. PMID: 26937641
  9. Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL PMID: 26022803
  10. Serum amyloid A1alpha induces paracrine IL-8/CXCL8 via TLR2 and directly synergizes with this chemokine via CXCR2 and formyl peptide receptor 2 to recruit neutrophils. PMID: 26297794
  11. Robust IL-17A production was restricted to the ileum, where SFB makes direct contact with the epithelium and induces serum amyloid A proteins 1 and 2 (SAA1/2), which promote local IL-17A expression in RORgammat(+) T17 cells. PMID: 26411290
  12. SAA protein levels increased in both serum and lung within 2-24h after mice were exposed to Aspergillus spores. SAA mRNA levels increased within the first hour after mice were exposed to A. fumigatus. PMID: 23603100
  13. Saa1 might be a novel inflammatory factor that acts as a chemokine modulator in hepatitis. PMID: 25847238
  14. GAGs may have an intrinsic and divergent influence on the aggregation and fibrillation of HDL-free SAA1.1 in vivo PMID: 24878279
  15. CE/J mice possess functional Saa1 and Saa2 genes with identical amino acid sequence. PMID: 24228751
  16. we find no evidence that adipose tissue-derived hSAA1 influences the development of insulin resistance or obesity-related inflammation. PMID: 23967285
  17. Its gene hold broader diversity and greater complexity and these characteristics were likely attained through gene duplication and repeated gene conversion events in the Mus lineage. PMID: 24521869
  18. The absence of endogenous SAA1.1 and 2.1 does not affect atherosclerotic lipid deposition in apolipoprotein E-deficient mice fed either normal or Western diets. PMID: 24265416
  19. SAA up-regulates Lp-PLA2 production significantly via a FPRL1/MAPKs./PPAR-gamma signaling pathway. PMID: 23623642
  20. Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2 PMID: 23223242
  21. An increase in plasma SAA directly accelerates the progression of atherosclerosis in ApoE-/- mice. PMID: 21953420
  22. SAA does not impact High Density Lipoprotein levels, apoA-I clearance, or High Density Lipoprotein size PMID: 20667817
  23. Infusions of SAA-positive cells promote renal recovery after acute renal failure and offer a potentially powerful and novel therapy of renal failure. PMID: 20534870
  24. Serum amyloid A has a role in promoting cholesterol efflux mediated by scavenger receptor B-I PMID: 16120612
  25. Plasma A-SAA elevation was due to induction of Saa1 and Saa2 expression in liver but not in adipose tissue. PMID: 18584041


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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