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Description
VZVgE His Tag ProteinProduct Specification Synonyms Envelope glycoprotein E; gE Accession Q9J3M8 Amino Acid Sequence Ser31 Tyr538
Product Specification
| Synonyms | Envelope glycoprotein E; gE |
| Accession | Q9J3M8 |
| Amino Acid Sequence | Ser31-Tyr538 |
| Expression System | HEK293 |
| Molecular Weight | 58-82kDa(Reducing) |
| Purity | ＞95% by SDS-PAGE & RP-HPLC |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, PH7.4, 5% trehalose |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
| Reference | Julie K. Olson, Richard A. Santos, Charles Grose, Varicella-Zoster Virus Glycoprotein gE: Endocytosis and Trafficking of the Fc Receptor, The Journal of Infectious Diseases, Volume 178, Issue Supplement_1, November 1998, Pages S2–S6. |
Background
Varicella-zoster virus (VZV) is the prototype member of the alphaherpesvirus subgroup now designated as the Varicellovirus genus. The genome of VZV encodes at least six glyco-proteins: gB, gC, gE, gH, gI, and gL. Of the VZV glycoproteins, gE (previously designated gpI or gp98) is the most abundant virion envelope protein and the predominant VZV glycoprotein expressed on the surface of infected cells. VZV gE is a typical type I transmembrane glycoprotein, which is highly modified by N-linked and O-linked glycosylation, sialylation, and sulfation. In addition, VZV gE contains a serine/threonine casein kinase II phosphorylation site. VZV gE can also form homodimers, which are modified by tyrosine phosphorylation. During viral infection, VZV gE forms a protein complex with VZV gI. Most interestingly, VZV gE on the surface of infected cells has previously been shown to function as an Fc receptor for nonimmune IgG. Homology studies have demonstrated that gE displays a combination of structural features commonly observed in several nonviral cell surface receptors, including the Fc receptor (FcγRII) and the low-density lipoprotein (LDL) receptor.
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