Analytical Data
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Gene name
TNF.
- Application
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Alternative Names
TNF.；AITRL；GITRL；TL6；Tumor necrosis factor ligand superfamily member 18
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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
P01375
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Expression Region
77-233aa
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AA Sequence
VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
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Molecular Weight
19.4 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
Tumor Necrosis Factor (TNF) is a pivotal cytokine involved in inflammation and immune responses. Its discovery dates back to the 1970s when it was recognized for its ability to induce necrosis in tumors. TNF exists in two forms: TNF-alpha, the most studied, primarily produced by activated macrophages, and TNF-beta, produced by lymphocytes. Due to its central role in regulating immune reactions, TNF has been implicated in various pathological conditions, including autoimmune diseases, inflammatory disorders, and cancer. The recombinant protein technology has allowed researchers to produce TNF in substantial quantities, facilitating deeper studies on its structure, function, and potential therapeutic applications. For example, recombinant TNF-alpha has been explored for its use in cancer therapy, leveraging its cytotoxic effects on tumor cells. However, its use is complicated by potential side effects, including severe inflammatory responses. Therefore, ongoing research focuses on understanding its signaling pathways, optimizing dosage, and developing TNF inhibitors to mitigate adverse effects while harnessing its therapeutic potential. This has spurred significant advancements in biotechnology and pharmacology, paving the way for novel treatments that target TNF-related pathways in diverse diseases.
