Recombinant Mouse Serum amyloid A-2 protein(Saa2)

Code CSB-EP020657MO
Size US$2466
Image
  • (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. P05367
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
Protein FAQs
Storage Condition Store at -20°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 Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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.

Target Data

Function Major acute phase reactant. Apolipoprotein of the HDL complex.
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

KEGG: mmu:20209

STRING: 10090.ENSMUSP00000075365

UniGene: Mm.200941

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