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
Q9Y4K3
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Expression Region
1-522aa
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AA Sequence
MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDAGV
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Molecular Weight
59.6 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 key cytokine involved in inflammation and immune regulation, playing a significant role in various pathological conditions, including autoimmune diseases, cancer, and infectious diseases. Research into TNF and its recombinant proteins has gained considerable traction due to their therapeutic potential. TNF signals through two main receptors, TNFR1 and TNFR2, leading to diverse biological responses, from promoting apoptosis to stimulating inflammation. The dysregulation of TNF signaling is implicated in several diseases, making it a prime target for therapeutic intervention. Recombinant TNF proteins are engineered to enhance our understanding of its biological functions and to develop targeted therapies, particularly in conditions like rheumatoid arthritis and tumor therapies. Advances in biotechnology have facilitated the production of TNF fusion proteins with improved stability and bioactivity, paving the way for innovative treatments. Moreover, the study of TNF's structure and function can provide insights into the development of novel drugs that modulate its activity, offering hope in the management of diseases characterized by TNF overexpression or deficiency. Overall, the research on TNF recombinant proteins is a dynamic and evolving field that aims to translate basic scientific findings into clinical applications for better patient outcomes.











