Recombinant Marburg Virus Envelope Glycoprotein (GP), sFc-tagged
Specification
Related Products
| Cat#: |
MAR-489 |
| Product Name: |
Recombinant Marburg Virus Envelope Glycoprotein (GP), sFc-tagged |
| Description: |
Marburg virus envelope glycoprotein (GP) is a recombinant MARV protein expressed and purified from mammalian cells. The product contains both furin cleaved and uncleaved version of the protein. |
| Gene: |
Envelope Glycoprotein (GP) |
| Species: |
Marburg Virus |
| Source: |
HEK293 |
| Synonyms: |
Marburg Virus Envelope Glycoprotein (GP) |
| Formulation: |
phosphate buffered saline. |
| Notes: |
This product is intended for research and manufacturing uses only. It is not a diagnostic device. The user assumes all responsibility for care, custody and control of the material, including its disposal, in accordance with all regulations. |
| Tags: |
Fc |
| Background: |
Marburg virus (MARV) is a hemorrhagic fever virus of the Filoviridae family and a member of the species Marburg marburgvirus, genus Marburgvirus. MARV causes a form of viral hemorrhagic fever in humans and nonhuman primates and is considered to be extremely dangerous. The virus can be transmitted by exposure to Old World fruit bats or it can be transmitted between people via body fluids.
The GP gene is the fourth gene along the genome of every filovirus (Sanchez et al., 1993) and encodes a trans-membrane protein GP localized at the virus surface. Marburg virus contains only one transmembrane protein (GP) which is responsible for receptor recognition on target cells, and triggers viral attachment and entry. GP, a type I membrane protein of approximately 220 kDa, is acylated and highly glycosylated carrying N- and O-linked sugar side chains. GP is transported through the exocytotic pathway toward the plasma membrane where budding of virions takes place. In the trans-Golgi network, GP is proteolytically activated by the prohormone convertase furin into two subunits GP(1) and GP(2) (Sänger et al., 2002). The GP gene also codes for additional proteins, whose functions are not yet fully understood (Martin et al., 2016).
Viral cell entry is a critical point for infection, and as such, this step is targeted for the design of antiviral molecules. Antibodies have demonstrated that inhibitors targeting filovirus entry may provide a potent antiviral strategy (Martin et al., 2016). |
For research or industrial raw materials, not for personal medical use!
