Analytical Data
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Gene name
TNFRSF6B
- Application
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Alternative Names
TNFRSF6B；DCR3；Tumor necrosis factor receptor superfamily member 6B
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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
O95407
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Expression Region
1-246aa
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AA Sequence
MRALEGPGLS LLCLVLALPA LLPVPAVRGV AETPTYPWRD AETGERLVCA QCPPGTFVQR PCRRDSPTTC GPCPPRHYTQ FWNYLERCRY CNVLCGEREE EARACHATHN RACRCRTGFF AHAGFCLEHA SCPPGAGVIA PGTPSQNTQC QPCPPGTFSA SSSSSEQCQP HRNCTALGLA LNVPGSSSHD TLCTSCTGFP LSTRVPGAEE CERAVIDFVA FQDISIKRLQ RLLQALEAPE GWGPTP
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Molecular Weight
58 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
TNFRSF6B, also known as Death Receptor 6 (DR6), is a member of the tumor necrosis factor receptor superfamily, which plays a crucial role in regulating apoptosis, immune response, and cell survival. Unlike other members of this family, TNFRSF6B functions as a decoy receptor, binding to its ligand but lacking the capacity to transduce death signals. This unique feature makes it an essential component in modulating inflammation and preventing excessive apoptosis, which could lead to various autoimmune diseases and cancers. Research has indicated that TNFRSF6B may have potential therapeutic implications, particularly in conditions where reduced apoptosis is desired, such as in certain cancers, or where modulation of the immune response is beneficial. The exploration of TNFRSF6B as a recombinant protein enables the investigation of its structure-function relationships, binding affinities, and regulatory mechanisms. Understanding these aspects may lead to novel insights into its role in disease processes and support the development of targeted therapies that could harness its decoy receptor capabilities to modulate pathological pathways. Consequently, ongoing studies on TNFRSF6B recombinant proteins aim to elucidate their biological functions, pathways of action, and potential applications in clinical settings, paving the way for innovative strategies in the treatment of diseases characterized by dysregulated apoptosis and immune responses.
