Analytical Data
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Gene name
TNFRSF12A
- Application
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Alternative Names
CD 266; CD266; CD266 antigen; FGF inducible 14
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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
Q9NP84
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Expression Region
28-80aa
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AA Sequence
EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP
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Molecular Weight
5.6 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
TNFRSF12A, also known as tumor necrosis factor receptor superfamily member 12A or CD266, is a costimulatory receptor that plays a significant role in immune regulation and inflammation. It has garnered attention in the fields of immunology and oncology due to its involvement in various biological processes, including T cell activation, differentiation, and survival. Research has shown that the signaling pathways activated by TNFRSF12A can influence the immune response to tumors and infections, making it a potential therapeutic target. Recombinant protein studies of TNFRSF12A are crucial for understanding its structure-function relationships and for elucidating its role in modulating immune responses. By generating recombinant TNFRSF12A proteins, researchers aim to examine their effects on immune cell interactions, explore potential applications in cancer immunotherapy, and develop novel strategies for treating autoimmune diseases. Furthermore, studying the recombinant protein may provide insights into its mechanisms of action, leading to enhanced therapeutic approaches that harness the body's immune system more effectively. As investigations into TNFRSF12A continue to expand, its dual role in promoting and regulating immune activity positions it as an intriguing candidate for advancing both basic and applied biomedical research.
