Analytical Data
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Gene name
TNF RI/TNFRSF1A
- Application
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Alternative Names
CD120A; P55; TNFRSF1A; TBP1; FPF; TNF-R; TNF-R-I; TNF-R55; TNFAR; TNFR55; TNFR60; P55-R; P60; Tumor necrosis factor receptor 1; Tumor necrosis factor-binding protein 1
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 97% as determined by reducing SDS-PAGE.
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Uniprot
P22934
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Expression Region
Leu43~Leu194
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Molecular Weight
20kDa
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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
Tumor necrosis factor receptor 1 (TNFRSF1A), also known as TNF receptor type 1 (TNF RI), is a critical component of the TNF superfamily, playing a pivotal role in mediating various biological responses, including inflammation, cell proliferation, and apoptosis. Dysregulation of TNF RI signaling is implicated in several pathological conditions, such as autoimmune diseases, cancer, and chronic inflammatory disorders. Given its significance, recombinant TNFRSF1A proteins have been a focus of research for their potential therapeutic applications. These recombinant proteins can be utilized to better understand the receptor's functional mechanisms, screen for novel drug candidates, and develop targeted therapies aimed at modulating TNF signaling pathways. The study of TNFRSF1A is crucial not only for its role in fundamental biology but also for its therapeutic potential in treating diseases associated with aberrant TNF signaling. Advances in recombinant DNA technology have facilitated the production of these proteins, enabling detailed structural and functional characterization. By exploring the interactions of TNFRSF1A with its ligands and downstream signaling pathways, researchers aim to uncover new insights that could lead to innovative treatments for a variety of diseases, thus underscoring the importance of continued investigation into this vital receptor.
