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HSV 2 (strain HG52) Glycoprotein E/gE Protein (His)

Catalog No. TMPY-06900

Herpes simplex virus type 2 (HSV-2) is the predominant cause of genital ulcer disease in human. Glycoprotein E (gE) and glycoprotein I (gI) are expressed as a heterodimer on the surface of Herpes simplex virus (HSV). Glycoprotein E binds Fc domain of immunoglobulin G (IgG) and inhibits activities mediated by the IgG Fc domain, contributing to immune evasion by HSV.

HSV 2 (strain HG52) Glycoprotein E/gE Protein (His)

HSV 2 (strain HG52) Glycoprotein E/gE Protein (His)

Catalog No. TMPY-06900
Herpes simplex virus type 2 (HSV-2) is the predominant cause of genital ulcer disease in human. Glycoprotein E (gE) and glycoprotein I (gI) are expressed as a heterodimer on the surface of Herpes simplex virus (HSV). Glycoprotein E binds Fc domain of immunoglobulin G (IgG) and inhibits activities mediated by the IgG Fc domain, contributing to immune evasion by HSV.
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100 μg$7007-10 days
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Product Information

Biological Activity
Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Herpes simplex virus type 2 (HSV-2) is the predominant cause of genital ulcer disease in human. Glycoprotein E (gE) and glycoprotein I (gI) are expressed as a heterodimer on the surface of Herpes simplex virus (HSV). Glycoprotein E binds Fc domain of immunoglobulin G (IgG) and inhibits activities mediated by the IgG Fc domain, contributing to immune evasion by HSV.
Species
HSV2
Expression System
Baculovirus Insect Cells
TagC-His
Accession NumberP89475
Construction
A DNA sequence encoding the HSV 2 ((strain HG52) (HSV2)) gE/glycoprotein E (translated amino acids of P89475) (Met1-Arg414) was expressed with a polyhistidine tag at the C-terminus. Predicted N terminal: Ala 21
Protein Purity
≥ 90 % as determined by SDS-PAGE.
Molecular Weight44.53 kDa (predicted); 49.31 kDa (reducing conditions)
Endotoxin< 1.0 EU/μg of the protein as determined by the LAL method.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris, 250 mM Nacl, 10% glycerol, pH 8.0.Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice.
Research Background
Herpes simplex virus type 2 (HSV-2) is the predominant cause of genital ulcer disease in human. Glycoprotein E (gE) and glycoprotein I (gI) are expressed as a heterodimer on the surface of Herpes simplex virus (HSV). Glycoprotein E binds Fc domain of immunoglobulin G (IgG) and inhibits activities mediated by the IgG Fc domain, contributing to immune evasion by HSV.

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