Analytical Data
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Gene name
IgA1
- Application
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Alternative Names
IGHA1; Immunoglobulin heavy constant alpha 1; Ig alpha-1 chain C region
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01876
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Expression Region
Ala1~Tyr353
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Molecular Weight
44kDa
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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
Immunoglobulin A1 (IgA1) is a key antibody isotype predominantly found in mucosal areas, playing a crucial role in the immune defense of mucosal surfaces against pathogens. It comprises a heavy chain (IgA1) andlight chain, and is essential for neutralizing toxins and viruses, as well as forming immune complexes. However, the biological activity and applications of IgA1 are often limited by its production challenges and structural complexities. The focus of research on recombinant IgA1 proteins involves the use of genetic engineering techniques to produce them in various expression systems, which offers the potential for enhanced yield, purity, and functional specificity. Moreover, recombinant IgA1 proteins have emerged as promising tools in therapeutic applications, such as vaccine development and treatment of diseases linked to mucosal immunity, like respiratory infections and gastrointestinal disorders. By investigating the structure-function relationships of IgA1, scientists aim to optimize its properties for better stability and efficacy. Ultimately, the development of recombinant IgA1 could pave the way for new strategies in boosting mucosal immunity and creating innovative therapies for infectious diseases.
