Analytical Data
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Gene name
SERPINA7
- Application
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Alternative Names
Thyroxine-binding globulin. Serpin A7. T4-binding globulin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05543
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Expression Region
1-415 aa
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AA Sequence
MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA
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Molecular Weight
72.7 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
SERPINA7, also known as serpin peptidase inhibitor, clade A, member 7, is a member of the serpin superfamily, which plays a crucial role in regulating serine proteases and modulating various physiological processes, including coagulation, inflammation, and tissue remodeling. Research into SERPINA7 has garnered attention due to its potential implications in pathological conditions such as cancer, cardiovascular diseases, and neurodegenerative disorders. The protein is predominantly expressed in the liver and is known to have anti-inflammatory properties, specifically by inhibiting inflammatory proteases. Additionally, it has been implicated in the regulation of insulin signaling and metabolic processes, linking it to disorders such as obesity and diabetes. The recombinant form of SERPINA7 is being studied for its therapeutic potential and as a biomarker for various diseases. The characterization of this recombinant protein allows for a better understanding of its biological functions, mechanisms of action, and interactions with other molecules. This research is essential for developing targeted therapies that harness its protective effects while minimizing adverse outcomes associated with its dysregulation. Thus, the study of SERPINA7 recombinant protein is critical for uncovering its roles in health and disease, paving the way for novel treatment strategies in related disorders.
