Recombinant Mouse Serum amyloid A-2 protein (Saa2)

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Code CSB-EP020657MO
MSDS
Size US$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 90% as determined by SDS-PAGE.
Target Names
Saa2
Uniprot No.
Research Area
Others
Alternative Names
Saa2; Serum amyloid A-2 protein [Cleaved into: Amyloid protein A; Amyloid fibril protein AA)]
Species
Mus musculus (Mouse)
Source
E.coli
Expression Region
20-122aa
Target Protein Sequence
GFFSFIGEAFQGAGDMWRAYTDMKEAGWKDGDKYFHARGNYDAAQRGPGGVWAAEKISDARESFQEFFGRGHEDTMADQEANRHGRSGKDPNYYRPPGLPAKY
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
15.6kDa
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.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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

Amino acids 20-122 constitute the expression domain of recombinant Mouse Saa2. The calculated molecular weight for this Saa2 protein is 15.6 kDa. This protein is generated in a e.coli-based system. The Saa2 coding gene included the N-terminal 6xHis tag, which simplifies the detection and purification processes of the recombinant Saa2 protein in following stages of expression and purification.

The mouse serum amyloid A-2 protein (Saa2) is a major acute-phase protein primarily produced in the liver in response to inflammatory stimuli such as infection, tissue injury, or cytokine signaling. It belongs to the serum amyloid A (SAA) family of proteins, which are involved in various immune responses and inflammatory processes. Saa2 is implicated in modulating inflammation, lipid metabolism, and the acute-phase response. Its expression is tightly regulated and can be induced by pro-inflammatory cytokines like IL-6 and TNF-α. Research on Saa2 spans areas such as inflammation, immune responses, and metabolic disorders, aiming to elucidate its role in health and disease, including its potential as a biomarker or therapeutic target for inflammatory conditions.

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Target Background

Function
Major acute phase reactant.
Gene References into Functions
  1. High level SAA expression induced amyloidosis in all mice after a short, slightly variable delay. PMID: 23959890
  2. These results suggest that the carboxy terminus of SAA, which is highly conserved among SAA sequences in all vertebrates, might play important structural roles, including modulating the folding, oligomerization, misfolding, and fibrillation of SAA.(Saa2) PMID: 22448726
  3. The nonpathogenic murine Saa2.2 spontaneously forms marginally stable amyloid fibrils at 37 degrees C that exhibit cross-beta structure, binding to thioflavin T, and fibrillation by a nucleation-dependent seeding mechanism. PMID: 21942925
  4. The ability of SAA2.2 to form different oligomeric species in vitro along with its marginal stability, suggest that the structure of SAA might be modulated in vivo to form different biologically relevant species. PMID: 21439938
  5. forms a hexamer containing a central channel in solution PMID: 12456883
  6. Only liposomes containing intact SAA2.1 or its residues 1-20 or 74-103 promoted the efflux of cholesterol in vivo PMID: 12951366
  7. SAA2.2 can form amyloid fibrils in vitro at physiological temperatures, which suggests that SAA2.2's inability to cause amyloidosis may be related to the stabilization of hexameric SAA2.2 and/or the slow kinetics of aberrant misfolding and self-assembly. PMID: 16194868
  8. Many functional and pathological roles attributed to serum amyloid A may rely on its precarious structure, modulated by its interaction with ligands under homeostasis conditions and during the acute phase response. PMID: 17425332

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Involvement in disease
Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.
Subcellular Location
Secreted.
Protein Families
SAA family
Tissue Specificity
Expressed by the liver; secreted in plasma.
Database Links
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