Analytical Data
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Gene name
TNF-α
- Application
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Alternative Names
TNF-α；
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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
VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVV PSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSP CQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQV YFGIIAL
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Molecular Weight
17 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-alpha (TNF-α) is a crucial cytokine involved in systemic inflammation and plays a significant role in the immune response. It is primarily produced by activated macrophages and has a variety of effects on cells, including the regulation of apoptosis, cell proliferation, and differentiation. Over the years, research has revealed its dual role in both promoting and inhibiting tumor growth, making it a target of interest in cancer therapy. Additionally, TNF-α is implicated in various inflammatory diseases such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. The advent of recombinant DNA technology has enabled the production of TNF-α recombinant proteins, facilitating detailed studies on its structure and function, and allowing researchers to investigate its potential therapeutic applications. These recombinant proteins have been used in experimental settings to elucidate TNF-α's signaling pathways and to develop anti-inflammatory drugs and monoclonal antibodies. This research background underscores the importance of understanding TNF-α at a molecular level to harness its therapeutic potential while mitigating adverse effects associated with excessive inflammation and immune activation. As investigations continue, the development of TNF-α modulators may offer novel avenues for treating a range of diseases characterized by aberrant cytokine activity.
