Recombinant Mouse HVEM Protein (His & Fc 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&Fc
Host Species	Mouse
Accession	NP_849262.1
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; TNFRSF20; 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 CD166 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-Gln 206) of mouse HVEM (NP_849262.1) precursor was fused with C-terminal His-tagged Fc region of human IgG1 at the C-terminus.
Source	CHO Stable Cells
Predicted N Terminal	Pro 40
AA Sequence	Met 1-Gln 206
Molecular Weight	The recombinant mouse HVEM /Fc is a disulfide-linked homodimeric Protein after removal of the signal peptide. The reduced monomer consists of 415 amino acids and predicts a molecular mass of 46.4 KDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rmHVEM/Fc monomer is approximately 65 KDa due to the glycosylation.
Purity	Greater than 85% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its binding ability in a functional ELISA.Immobilized mouse HVEM-Fc can bind biotinylated mouse BTLA-Fcï¼ŒThe EC50 of biotinylated mouse BTLA-Fc is 152-228 ng/mL.
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.

Target Details

Target Function	Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network. Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation. Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions. Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response. In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines. Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. May interact in cis (on the same cell) or in trans (on other cells) with BTLA. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Tissue Specificity	Expressed at mucosal sites including colon and pulmonary epithelial cells. Expressed in naive T cells.

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.