Analytical Data
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Gene name
TNFAIP3
- Application
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Alternative Names
A20; OTUD7C; TNFA1P2; OTU domain-containing protein 7C; Putative DNA-binding protein A20; Zinc finger protein A20
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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 95% as determined by SDS-PAGE.
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Uniprot
P21580
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Expression Region
Met1~Glu300
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Molecular Weight
39kDa
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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
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Protein Description
TNFAIP3, also known as A20, is a potent anti-inflammatory protein that plays a crucial role in the regulation of the immune response and the maintenance of cellular homeostasis. Functioning primarily as a negative regulator of the NF-κB signaling pathway, TNFAIP3 modulates inflammation and apoptosis by promoting ubiquitination and degradation of signaling molecules. Dysregulation of TNFAIP3 has been implicated in various autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, and inflammatory bowel disease, where its reduced expression or dysfunctional mutations contribute to chronic inflammation. The therapeutic potential of TNFAIP3 and its reconstitution has garnered significant interest in the biomedical field. Researchers are investigating the recombinant expression of TNFAIP3 to better understand its structure-function relationship, elucidate its mechanistic role in signaling pathways, and develop novel therapeutic strategies aimed at restoring its function in disease contexts. By studying the restructured protein, scientists aim to address the challenges posed by its complex regulation and interactions, enabling advancements in targeted therapies that could mitigate autoimmune conditions and enhance overall immune system balance. This line of research holds promise for developing innovative treatments that can harness the protective effects of TNFAIP3, underscoring its importance in both fundamental immunology and clinical applications.
