Analytical Data
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Gene name
IL12A
- Application
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Alternative Names
IL12A；NKSF1；Interleukin-12 subunit alpha
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Species
Human
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Source
HEK293
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Tag
C-hFc&His tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29459
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Expression Region
23-219aa
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AA Sequence
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHE DITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMAL CLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNF NSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS
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Molecular Weight
55-65kDa
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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
Identification
Protein Description
IL12A, the alpha subunit of interleukin-12 (IL-12), plays a crucial role in the immune response by modulating T cell and natural killer (NK) cell functions. Understanding the biological activity of IL12A has significant implications for cancer immunotherapy, autoimmune diseases, and infectious diseases. The IL-12 complex, composed of IL12A and IL12B, has been shown to enhance the production of pro-inflammatory cytokines and promote Th1 cell differentiation, which are vital for effective anti-tumor immunity. Researchers have been focusing on the recombinant production of IL12A to investigate its therapeutic potential. This involves employing various expression systems, such as bacterial, yeast, or mammalian cells, to produce bioactive IL12A for both basic research and clinical applications. Analyzing the structural and functional properties of recombinant IL12A can provide insights into its mechanism of action and interactions with other components of the immune system. Moreover, the ability to produce high-purity recombinant IL12A helps in developing novel biotherapeutics that can enhance immune responses in individuals with cancer or chronic infections. Challenges in this research include optimizing production yields, ensuring proper folding and post-translational modifications, and evaluating the stability and efficacy of the protein. As studies progress, the exploration of IL12A’s potential in combination therapies and its role in vaccine development may open new avenues for enhancing immune responses against various diseases.
