Analytical Data
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Gene name
IFNA2
- Application
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Alternative Names
IFNA2;IFNA2A;IFNA2B;IFNA2C;Interferon alpha-2
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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
P01563
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Expression Region
24-188aa
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AA Sequence
MFCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQ KAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEAC VIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIM RSFSLSTNLQESLRSKE
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Molecular Weight
20 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
IFNA2, a subtype of interferon alpha, plays a crucial role in the body's immune response against viral infections and tumor growth. Its therapeutic potential has long been recognized, particularly in the treatment of various cancers and viral diseases such as hepatitis C. Given its pivotal role in mediating antiviral effects, researchers have focused on the recombinant production of IFNA2 to enhance its availability and efficacy for clinical applications. Advances in biotechnology, particularly in recombinant DNA technology, have facilitated the efficient expression and purification of IFNA2 in host systems such as bacteria, yeast, and mammalian cells. This recombinant protein not only replicates the biological activities of native IFNA2 but also allows for modifications to improve its stability and therapeutic potency. The understanding of its mechanism of action has further propelled research into its use in combination therapies, especially in oncology, where it can augment the effects of other anticancer agents. Continued investigation into IFNA2's immune-modulating properties, coupled with emerging platform technologies for its production, holds promise for the development of innovative therapeutics to combat persistent viral infections and malignancies. Ultimately, the ongoing studies aim to optimize the efficacy and safety profiles of IFNA2-based therapies, thereby expanding their use in clinical settings and improving patient outcomes.
