Recombinant Mouse Serum amyloid A-1 protein (Saa1)

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Code CSB-EP020656MOa0
Abbreviation Recombinant Mouse Saa1 protein
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Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Cardiovascular
Alternative Names
Saa1; Serum amyloid A-1 protein
Species
Mus musculus (Mouse)
Source
E.coli
Expression Region
20-122aa
Target Protein Sequence
GFFSFVHEAFQGAGDMWRAYTDMKEANWKNSDKYFHARGNYDAAQRGPGGVWAAEKISDGREAFQEFFGRGHEDTIADQEANRHGRSGKDPNYYRPPGLPDKY
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
17 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Recombinant Mouse Serum amyloid A-1 protein (Saa1) gets produced in E. coli and includes the full length of the mature protein, spanning amino acids 20 to 122. The protein features an N-terminal 6xHis-tag designed to help with purification and detection. SDS-PAGE analysis shows purity levels above 85%, which appears to make it suitable for various research applications.

Serum amyloid A-1 protein likely plays a significant role in the acute phase response, getting involved in lipid metabolism and immune function regulation. It's a key component in chronic inflammation studies. Researchers often examine it in the context of amyloid fibril formation. This protein seems essential for understanding inflammatory processes and how the body responds to injury or infection.

Potential Applications

Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.

Mouse Saa1 is an acute-phase protein that requires precise folding, proper oligomerization, and specific tertiary structure for its functional activity in inflammatory responses and receptor binding. The E. coli expression system may not provide the optimal eukaryotic folding environment, and Saa1 may require specific disulfide bond formation or post-translational modifications for full functionality. The N-terminal 6xHis-tag is relatively small (∼0.8 kDa) compared to the mature protein (20-122aa, ∼12 kDa), minimizing steric interference. However, the probability of correct folding with functional bioactivity requires experimental validation, as E. coli-expressed proteins can misfold or lack native conformation.

1. In Vitro Protein-Protein Interaction Studies

This application carries a significant risk without functional validation. Saa1 interactions with receptors or partners require native conformation. If correctly folded and active (verified through binding assays), the protein may identify physiological interactions; if misfolded/unverified, there is a high risk of non-specific binding or tag-mediated artefacts.

2. Antibody Development and Validation

This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional protein folding. The full-length mature protein provides comprehensive epitope coverage for generating Saa1-specific antibodies. The high purity (>85%) ensures minimal contamination issues.

3. Structural and Biophysical Characterization

These studies are essential for determining folding status. Techniques like circular dichroism spectroscopy, dynamic light scattering, and thermal stability assays can assess protein folding, oligomerization, and stability. If correctly folded, results are valuable; if misfolded, they characterize the recombinant construct.

4. In Vitro Functional Assays

This application carries a significant risk without activity validation. Saa1's cellular effects require native conformation and receptor-binding capability. If correctly folded and active (verified), the protein may be used in dose-response studies; if misfolded/inactive, functional assays will yield biologically meaningless results.

5. Comparative Species Analysis

Meaningful comparative studies require native protein conformation and functional activity. If correctly folded and active (verified), the protein enables valid evolutionary comparisons; if misfolded/unverified, comparative analyses would yield misleading insights.

Final Recommendation & Action Plan

The E. coli-expressed Saa1 with a small His-tag has a moderate probability of correct folding due to the protein's size and minimal tag interference, but experimental validation is crucial. Begin with Application 3 (Structural and Biophysical Characterization) to assess folding quality through techniques like CD spectroscopy and SEC, and validate functionality using receptor-binding or cell-based assays. Applications 1, 4, and 5 require rigorous functional validation before proceeding. Application 2 (antibody development) can proceed immediately. For reliable Saa1 research, confirm bioactivity and consider using refolding protocols or mammalian expression systems if initial validation indicates poor functionality.

Citations

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Target Background

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