Analytical Data
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Gene name
SERPINA9
- Application
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Alternative Names
Centerin (Germinal center B-cell-expressed transcript 1 protein) (GCET1) (SERPINA11)
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Species
Human
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Source
HEK293
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86WD7
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Expression Region
24-417aa
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Molecular Weight
49.1 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
SERPINA9 (serpin peptidase inhibitor, clade A, member 9) is part of the serine protease inhibitor (serpin) superfamily, known for its role in regulating various biological processes, notably in the immune response and cellular growth. Recent studies have highlighted its potential involvement in cancer progression, inflammation, and neurodegenerative diseases, making it a significant target for therapeutic intervention. The expression of SERPINA9 has been associated with tumor microenvironments and the modulation of immune cell activity, which can affect tumorigenesis and metastasis. Moreover, research indicates that SERPINA9 may play a protective role in stress-induced cellular damage, positioning it as an attractive candidate for the development of recombinant therapeutic proteins. The generation of recombinant SERPINA9 allows for detailed studies of its structure-function relationship, providing insights into its inhibitory mechanisms and therapeutic applications. Understanding the nuances of SERPINA9's biological roles could pave the way for novel strategies in disease treatment, emphasizing the importance of ongoing research in this area.
