Recombinant Human HVEM/TNFRSF14 Fc Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human BTLA
(Catalog #
9235-BT)
is immobilized at 1.00 µg/mL (100 µL/well), Biotinylated Recombinant Human HVEM/TNFRSF14 Fc Chimera Avi-tag binds with an ED 50 of 30.0-180 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human HVEM/TNFRSF14 protein
Human HVEM/TNFRSF14 (Pro37-Val202) Accession # Q92956.3 | DIEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus |
|
Accession # |
|
N-terminal Sequence |
Pro37 |
Structure / Form |
Disulfide-linked homodimer, biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
46 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
61-67 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human HVEM/TNFRSF14 Fc Avi-tag Protein, CF
Background
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.
- del Rio, M.L. et al. (2010) J. Leukoc. Biol. 87:223.
- Montgomery, R.I. et al. (1996) Cell 87:427.
- Hsu, H. et al. (1997) J. Biol. Chem. 272:13471.
- Sedy, J. R. et al. (2005) Nat. Immunol. 6:90.
- Tao, R. et al. (2008) J. Immunol. 180:6649.
- Steinberg, M.W. et al. (2013) PLoS One 8:e77992.
- de Trez, C. et al. (2008) J. Immunol. 180:238.
- Heo, S.K. et al. (2006) J. Leukoc. Biol. 79:330.
- Gonzalez, L.C. et al. (2005) Proc. Natl. Acad Sci. USA 102:1116.
- Cai, G. et al. (2008) Nat. Immunol. 9:176.
- Mauri, D.N. et al. (1998) Immunity 8:21.
- Harrop, J.A. et al. (1998) J. Biol. Chem. 273:27548.
- Wang, J. et al. (2005) J. Immunol. 174:8173.
- Ye, Q. et al. (2002) J. Exp. Med. 195:795.
- Steinberg, M.W. et al. (2008) J. Exp. Med. 205:1463.
- Shui, J.W. et al. (2012) Nature 488:222.
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