Analytical Data
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Gene name
SAA
- Application
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Alternative Names
SAA；Serum amyloid A-1 Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DJI8
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Expression Region
19-122aa
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AA Sequence
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISD ARENIQRFFG HGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY
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Molecular Weight
11.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SAA (serum amyloid A) proteins are a group of acute-phase reactants primarily produced by the liver in response to inflammation. Elevation of SAA levels is associated with various diseases, including rheumatoid arthritis, inflammatory bowel disease, and cardiovascular disorders, making it an important biomarker for inflammatory conditions. Research into SAA has garnered attention due to its role in the pathogenesis of amyloidosis, where misfolded SAA proteins aggregate and form amyloid fibrils, leading to tissue damage. The study of recombinant SAA proteins has advanced our understanding of their structure, function, and interactions with other molecules in the immune system. By employing recombinant DNA technology, researchers can produce specific SAA isoforms to investigate their biological activities, establish their role in disease processes, and explore their potential as therapeutic targets or biomarkers. Additionally, recombinant SAA proteins facilitate the development of diagnostic assays, contributing to early detection and personalized treatment strategies. Overall, the research on SAA recombinant proteins holds significant promise for elucidating the complexities of inflammatory diseases and improving clinical outcomes.
