Analytical Data
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Gene name
TNFRSF12A
- Application
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Alternative Names
CD266; TNFRSF12-A; FN14; TWEAKR; Tumour Necrosis Factor Related Weak Inducer Of Apoptosis; Fibroblast growth factor-inducible immediate-early response protein 14
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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 85% as determined by SDS-PAGE.
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Uniprot
Q9NP84
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Expression Region
Ser24~Ala126
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Molecular Weight
44kDa
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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 the tumor necrosis factor receptor superfamily member 12A or TRAF receptor-associated factor 2 (TRAF2), has emerged as a significant focus in immunological and cancer research. This receptor is primarily expressed in immune cells and plays a pivotal role in regulating various biological processes, including cell proliferation, survival, and apoptosis. Its involvement in the modulation of inflammatory responses and immune system regulation has placed TNFRSF12A at the center of studies concerning autoimmune diseases and malignancies. Research has shown that the dysregulation of TNFRSF12A signaling pathways can contribute to the progression of several cancers, making it a potential therapeutic target. As a consequence, the development of TNFRSF12A recombinant proteins has gained traction to better understand its functional mechanisms and to explore its potential in therapeutic applications. These recombinant proteins facilitate the elucidation of TNFRSF12A's role in immune modulation and tumorigenesis, thus paving the way for novel treatment strategies that harness the immune system to combat cancer and other related diseases. The ongoing investigations into the biochemical properties and interactions of TNFRSF12A continue to provide insights that are crucial for developing targeted therapies aimed at enhancing immune responses while minimizing side effects associated with conventional treatments.
