Analytical Data
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Gene name
Serum Amyloid A-1
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简介
Serum Amyloid A-1 Protein, a vital acute phase protein, primarily exists as a homohexamer composed of dimers of trimers.Although it can form amyloid fibrils after partial proteolysis, the native, undenatured form does not exhibit amyloid fibril formation in vitro.Serving as an apolipoprotein within the HDL complex, Serum Amyloid A-1 also shows affinity for heparin binding, highlighting its multifaceted role in biological processes.Serum Amyloid A-1 Protein, Mouse is the recombinant mouse-derived Serum Amyloid A-1 protein, expressed by E.coli , with tag free.
- Application
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Biological Activity
Measured by its ability to induce TNF-alpha secretion by J774A.1 mouse reticulum cell sarcoma macrophage cells. The ED50 for this effect is 1.0-2.5 μg/mL. Measured by its ability to induce TNF-alpha secretion by J774A.1 mouse reticulum cell sarcoma macrophage cells. The ED50 for this effect is 1.085 μg/mL. Corresponding to a specific activity is 921.659 U/mg.
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Alternative Names
Serum amyloid A-1 protein; Saa1
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Species
Mouse
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P05366
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Expression Region
G20-Y122
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Protein Length
Full Length of Mature Protein
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Molecular Weight
12 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
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Protein Description
Serum Amyloid A-1 (SAA1) is an acute-phase protein that plays a critical role in inflammatory responses and has been linked to various pathological conditions, including amyloidosis, cardiovascular diseases, and autoimmune disorders. As a major component of the acute-phase response, SAA1 is produced primarily in the liver in response to pro-inflammatory cytokines, particularly interleukin-6 (IL-6). Its levels can rise significantly during inflammation, making it a potential biomarker for monitoring disease progression and therapeutic responses. Furthermore, the aggregation of SAA1 can lead to amyloid deposition, resulting in tissue damage and organ dysfunction. The study of recombinant SAA1 proteins has gained attention as researchers seek to understand its structure-function relationships and to develop novel therapeutic strategies targeting its pathways. By generating recombinant forms of SAA1, scientists can investigate its biological functions, elucidate mechanisms of amyloid formation, and explore its interactions with other proteins and cell types in the inflammatory milieu. Additionally, recombinant SAA1 can be utilized in the development of diagnostic tools and therapeutic agents, highlighting its significance in both basic and translational research. Understanding SAA1 at the molecular level not only offers insights into its role in inflammation and amyloidogenesis but also paves the way for innovative approaches to treat conditions associated with elevated SAA levels. Overall, research into recombinant SAA1 proteins serves as a foundational step toward unraveling the complexities of inflammation and amyloid-related diseases, ultimately contributing to more effective clinical management strategies.
