Analytical Data
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Gene name
TNFRSF14
- Application
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Alternative Names
TNFRSF14；HVEA；Tumor necrosis factor receptor superfamily member 14
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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
Q92956
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Expression Region
39-202aa
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AA Sequence
LPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLN GLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAAC RAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWL VTKAGAGTSSSHWV
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Molecular Weight
19 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
TNFRSF14, also known as herpesvirus entry mediator (HVEM), is a member of the tumor necrosis factor receptor superfamily (TNFRSF) that plays a crucial role in immune regulation and inflammation. The receptor is predominantly expressed on various immune cells, including T cells, B cells, and dendritic cells, and is involved in multiple signaling pathways that modulate lymphocyte activation, survival, and apoptosis. Dysregulation of TNFRSF14 has been implicated in several autoimmune diseases and cancers, making it a potential therapeutic target. Research on recombinant TNFRSF14 proteins has gained traction as scientists seek to understand the mechanistic roles this receptor plays in immune responses and its interactions with ligands such as LIGHT and CD160. The development of recombinant proteins allows for detailed structural and functional studies, enabling the identification of potential binding partners and downstream signaling events. Furthermore, understanding the specific interactions mediated by TNFRSF14 can shed light on its dual roles in promoting or inhibiting immune responses, thus aiding in the design of novel immunotherapeutic strategies. Overall, the study of TNFRSF14 recombinant proteins holds promise for uncovering new insights into immune regulation and developing interventions for related diseases.
