Specification
| Organism | Lake Victoria marburgvirus (strain Popp-67) (MARV) (Marburg virus (strain West Germany/Popp/1967)) |
| Expression Host | Baculovirus |
| Tag Info | N-terminal 10xHis-tagged and C-terminal Myc-tagged |
| Purity | Greater than 85% by SDS-PAGE |
| Uniprot ID | P35254 |
| Gene Names | GP |
| Alternative Names | GP1,2 (GP) (Virion spike glycoprotein) |
| Expression Region | Partial(436-681aa ) |
| Molecular Weight | 31.3 kDa |
| Protein Sequence | SILWREGDMFPFLDGLINAPIDFDPVPNTKTIFDESSSSGASAEEDQHASPNISLTLSYFPNINENTAYSGENENDCDAELRIWSVQEDDLAAGLSWIPFFGPGIEGLYTAGLIKNQNNLVCRLRRLANQTAKSLELLLRVTTEERTFSLINRHAIDFLLTRWGGTCKVLGPDCCIGIEDLSRNISEQIDQIKKDEQKEGTGWGLGGKWWTSDWGVLTNLGILLLLSIAVLIALSCICRIFTKYIG |
| Form | Liquid or Lyophilization |
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| Relevance | GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells, and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection GP2 acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide. |
| Involvement in Disease | |
| Subcellular Location | GP2: Virion membrane, Single-pass type I membrane protein, Host cell membrane, Single-pass type I membrane protein, Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site, SUBCELLULAR LOCATION: GP1: Virion membrane, Peripheral membrane protein, Host cell membrane, Peripheral membrane protein |
| Protein Families | Filoviruses glycoprotein family |
| Tissue Specificity | GP |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |