Human HVEM, His Tag (HVM-H52E9) is expressed from human 293 cells (HEK293). It contains AA Leu 39 - Val 202 (Accession # Q92956-1).
Predicted N-terminus: Leu 39
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 19.2 kDa. The protein migrates as 33-40 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Less than 1.0 EU per μg by the LAL method.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human HVEM, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Immobilized Human LIGHT, Mouse IgG2a Fc Tag, low endotoxin (Cat. No. LIT-H5256) at 2 μg/mL (100 μL/well) can bind Human HVEM, His Tag (Cat. No. HVM-H52E9) with a linear range of 0.04-0.6 μg/mL (QC tested).
Immobilized Human HVEM, His Tag (Cat. No. HVM-H52E9) at 5 μg/mL (100 μL/well) can bind Human BTLA, Fc Tag (Cat. No. BTA-H5256) with a linear range of 0.2-2.5 μg/mL (Routinely tested).
Immobilized Human HVEM, His Tag (Cat. No. HVM-H52E9) at 0.5 μg/mL (100 μL/well) can bind Human BTLA, Fc Tag (Cat. No. BTA-H5255) with a linear range of 0.078-2.5 μg/mL (Routinely tested).
Authors: M Szymczak, et al
Journal: Protein Expr Purif 43655
Herpesvirus entry mediator (HVEM) is also known as TNFRSF14, TR2 (TNF receptorlike molecule) and ATAR (another TRAF associated receptor), is a type I membrane protein belonging to the TNF/NGF receptor superfamily. HVEM expression has been detected in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. The extracellular domain of HVEM has been shown to interact directly with the herpes simplex virus envelope glycoprotein D (gD). Two TNF superfamily ligands, including the secreted TNFβ (lymphotoxin α) and the membrane protein LIGHT (lymphotoxins, exhibits inducible expression, and competes with HSV glycoprotein D for HVEM, a receptor expressed by T lymphocytes), have been shown to be the cellular ligands for HVEM. Besides HVEM, LIGHT can also interact with LTβR, the receptor for lymphotoxin αβ heterotrimer. The role of the HVEM LIGHT /LTβ receptor ligand pair in immune function and herpesvirus pathobiology remains to be elucidated.