Analytical Data
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Gene name
TRAF1
- Application
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Alternative Names
EBI6; Epstein-Barr Virus Induced Protein 6
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13077
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Expression Region
Gly131~Ala381
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Molecular Weight
58kDa
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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
TRAF1 (TNF receptor-associated factor 1) is an essential adaptor protein predominantly involved in the signaling pathways of various members of the tumor necrosis factor (TNF) receptor superfamily. Its role in mediating cellular responses such as inflammation, immune cell activation, and apoptosis has garnered significant interest in both basic and clinical research. TRAF1's interaction with multiple receptors, including TNF receptors and interleukin receptors, highlights its importance in both innate and adaptive immune responses. Abnormal expression or mutations in TRAF1 have been linked to several diseases, including autoimmune disorders and cancers, making it a potential therapeutic target. Recent studies have focused on the structural characterization of TRAF1 and its complexes to better understand its diverse functions. Recombinant TRAF1 proteins are increasingly being used to elucidate its role in cellular signaling pathways, assess the functional consequences of TRAF1 interactions, and explore its potential as a biomarker for disease states. This research could lead to novel therapeutic strategies aimed at modulating TRAF1 activity to treat immune-related conditions. The recombinant production of TRAF1 protein plays a vital role in these studies, enabling researchers to investigate its biochemical properties and interactions in detail.
