Recombinant Human HVEM Protein (His Tag)

Collections: Co-inhibitory receptors, Co-stimulatory receptors, Cytokines and growth factors, Featured immune checkpoint protein molecules, Immune checkpoint proteins, Recombinant proteins, Tumor necrosis factors and receptors (tnfs)

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Product Overview

Tag	His
Host Species	Human
Accession	NP_003811.2
Synonym	HVEM Tumor Necrosis Factor Receptor Superfamily Member 14; Herpes Virus Entry Mediator A; Herpesvirus Entry Mediator A; HveA; Tumor Necrosis Factor Receptor-Like 2; TR2; CD270; TNFRSF17; HVEA; HVEM
Background	Herpesvirus entry mediator (HVEM) is a type I membrane protein in the TNF receptor superfamily, and it can both promote and inhibit T cell activity. HVEM is highly expressed on naive CD4+ T cells, CD8+ T memory cells, regulatory T cells, dendritic cells, monocytes, and neutrophils. It functions as a receptor for BTLA, CD160, LIGHT/TNFSF14, and Lymphotoxin-alpha. Ligation of HVEM by LIGHT triggers T cell, monocyte, and neutrophil activation and contributes to Th1 inflammation and cardiac allograft rejection. In contrast, HVEM binding to CD160 or BTLA suppresses T cell and dendritic cell activation and dampens intestinal inflammation. HVEM enhances the development of CD8+ T cell memory and Treg function. It is additionally expressed on intestinal epithelial cells, where its binding by intraepithelial lymphocyte (IEL) expressed CD163 promotes epitheilal integrity and host defense. The herpesvirus envelope glycoprotein gD, which binds HVEM to initiate membrane fusion, can antagonize both BTLA and LIGHT binding.
Description	A DNA sequence encoding the extracellular domain (Met 1-Val 202) of human HVEM (NP_003811.2) was produced, fused with a C-terminal His tag.
Source	HEK293
Predicted N Terminal	Pro 37
AA Sequence	Met 1-Val 202
Molecular Weight	The secreted recombinant human HVEM consists of 177 amino acids and predicts a molecular mass of 19 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rhHVEM is approximately 33-38 kDa due to glycosylation.
Purity	Greater than 90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4
Stability	Recombinnat Proteins are stable for up to 1 year from date of receipt at -70°C
Usage	For Research Use Only
Storage	Store recombinant protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.