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Description
VZVgE Flag Tag ProteinProduct Specification Synonyms Envelope glycoprotein E; gE; HHV 3 gE; glycoprotein E Protein Accession Q9J3M8 Amino Acid Sequence Ser31 Tyr538
Product Specification
| Synonyms | Envelope glycoprotein E; gE; HHV-3 gE; glycoprotein E Protein |
| 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 | Flag 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) serves as the prototype for the alphaherpesvirus subgroup, classified under the Varicellovirus genus. The VZV genome encodes a minimum of six glycoproteins: gB, gC, gE, gH, gI, and gL. Among these, gE (formerly known as gpI or gp98) is the most abundant in the virion envelope and is the primary glycoprotein present on the surface of infected cells.
VZV gE is a classic type I transmembrane glycoprotein, extensively modified by N-linked and O-linked glycosylation, sialylation, and sulfation. It also features a phosphorylation site for serine/threonine casein kinase II. Additionally, gE has the capacity to form homodimers that undergo tyrosine phosphorylation.
During infection, VZV gE interacts with VZV gI to form a protein complex. Notably, gE on the surface of infected cells has been identified as an Fc receptor for nonimmune IgG. Homology studies indicate that gE exhibits structural characteristics akin to those of several nonviral cell surface receptors, such as the Fc receptor (FcγRII) and the low-density lipoprotein (LDL) receptor.
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