Analytical Data
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Gene name
TNFRSF6
- Application
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Alternative Names
TNFRSF6；APT1；Tumor necrosis factor receptor superfamily member 6
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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
P25445
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Expression Region
26-173aa
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AA Sequence
QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTV NGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNT KCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSN
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Molecular Weight
43 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
TNFRSF6, also known as Tumor Necrosis Factor Receptor Superfamily Member 6 or CD95, is a crucial protein involved in immune regulation and apoptosis. Its primary role is to mediate programmed cell death in response to various stimuli, which is essential for maintaining cellular homeostasis and immune system function. Dysregulation of TNFRSF6 has been implicated in numerous diseases, including autoimmune disorders, cancer, and neurodegenerative conditions. Research on recombinant TNFRSF6 proteins has garnered significant attention due to their potential therapeutic applications. By utilizing recombinant DNA technology, scientists can produce large quantities of the TNFRSF6 protein to study its structure-function relationships, signaling pathways, and interactions with ligands such as Fas ligand (FasL). Furthermore, these recombinant proteins can be explored as potential treatment modalities for diseases characterized by excessive cell proliferation or insufficient apoptosis. In cancer therapy, for instance, enhancing the apoptotic signaling through TNFRSF6 may improve the efficacy of existing treatments. Moreover, studying TNFRSF6 in the context of autoimmune diseases could reveal innovative strategies for modulation of immune responses. Thus, the investigation of TNFRSF6 recombinant proteins not only advances our understanding of fundamental biological processes but also holds promise for developing novel therapeutic interventions across various medical fields.
