Analytical Data
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Gene name
TNFRSF25
- Application
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Alternative Names
TNFRSF25；TL1；Tumor necrosis factor ligand superfamily member 15
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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
Q93038
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Expression Region
25-199aa
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AA Sequence
QGGTRSPRCDCAGDFHKKIGLFCCRGCPAGHYLKAPCTEPCGNSTCLVCP QDTFLAWENHHNSECARCQACDEQASQVALENCSAVADTRCGCKPGWFVE CQVSQCVSSSPFYCQPCLDCGALHRHTRLLCSRRDTDCGTCLPGFYEHGD GCVSCPTSTLGSCPERCAAVCGWRQ
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Molecular Weight
55 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
TNFRSF25, also known as tumor necrosis factor receptor superfamily member 25, is a crucial protein involved in regulating immune responses and promoting cell survival. The receptor is predominantly expressed in lymphocytes and is implicated in various immune-related processes, including T cell activation, proliferation, and apoptosis. Dysregulation of TNFRSF25 has been linked to multiple diseases, including autoimmune disorders and cancer. Research into TNFRSF25 recombinant proteins has gained momentum as these proteins can function as therapeutic agents or as tools for studying T cell biology. Understanding the structure and function of TNFRSF25, along with its signaling pathways, can provide insights into its role in immune regulation and the potential for developing novel immunotherapeutic strategies. Recent advancements in protein engineering techniques have facilitated the production of functional recombinant TNFRSF25, paving the way for detailed investigations into its therapeutic applications and mechanism of action. As a result, TNFRSF25 represents a promising target for enhancing immune responses in cancer therapy and controlling autoimmune diseases, highlighting the importance of ongoing research in this area.
