Recombinant Human HVEM/TNFRSF14 Fc Avi-tag Protein, CF
Recombinant Human HVEM/TNFRSF14 Fc Avi-tag Protein, CF SummaryLearn more about Avi-tag Biotinylated Proteins
Accession # Q92956.3
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human BTLA (9235-BT) is immobilized at 1.00 µg/mL (100 µL/well), Biotinylated Recombinant Human HVEM/TNFRSF14 Fc Chimera Avi-tag binds with an ED50 of 30.0-180 ng/mL.
2 μg/lane of Biotinylated Recombinant Human HVEM/TNFRSF14 Fc Chimera Avi-tag (Catalog # AVI10726) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 61-67 kDa and 120-130 kDa, respectively.
HVEM (herpesvirus entry mediator), also known as TNFRSF14 and CD270, is a type I membrane protein in the TNF receptor superfamily, and it can both promote and inhibit T cell activity (1). Mature human HVEM consists of a 164 amino acid (aa) extracellular domain (ECD) with three cysteine-rich domains (CRD), a 21 aa transmembrane segment, and a 60 aa cytoplasmic tail with a TRAF interaction domain (2, 3). Within the ECD, human HVEM shares 55% aa sequence identity with mouse and rat HVEM. Alternative splicing generates an additional isoform with a substitution of the N-terminal 10 amino acids including the signal peptide. HVEM is highly expressed on naïve CD4+ T cells, CD8+ T memory cells, regulatory T cells, dendritic cells, monocytes, and neutrophils (4-8). Its expression declines during effector T cell activation but is up-regulated during T reg activation (4, 5). HVEM functions as a receptor for BTLA, CD160, LIGHT/TNFSF14, and Lymphotoxin-alpha (4, 9‑12). Ligation of HVEM by LIGHT triggers T cell, monocyte, and neutrophil activation (8, 10) and contributes to Th1 inflammation and cardiac allograft rejection (13, 14). In contrast, HVEM binding to CD160 or BTLA suppresses T cell and dendritic cell activation (4, 7, 9, 10) and dampens intestinal inflammation (15). HVEM enhances the development of CD8+ T cell memory and T reg function (5, 6). It is additionally expressed on intestinal epithelial cells, where its binding by intraepithelial lymphocyte (IEL) expressed CD160 promotes epitheilal integrity and host defense (16). The herpesvirus envelope glycoprotein gD, which binds HVEM to initiate membrane fusion, can antagonize both BTLA and LIGHT binding (2, 9, 11). Our Avi-tag Biotinylated Human HVEM features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is uncharged so there is no interference in the protein's bioactivity.
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