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Recombinant Bundibugyo ebolavirus GP Protein, C-His-tagged

Cat.No. : GP-08E
Product Overview : Recombinant Ebolavirus BDBV (subtype Bundibugyo,strain Uganda 2007) secreted Glycoprotein (sGP) produced in HEK293 cells, incorporating a C-terminal 6x His-tag.
  • Specification
  • Gene Information
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Description : The virulence of EBOV may be partially attributed to the Ebola virus secreted glycoprotein (sGP), which is the main product transcribed from its GP gene. Ebola virus secreted glycoprotein is secreted from infected cells and can be readily detected in the serum of EBOV-infected hosts. Mature sGP is produced from a precursor by proteolytic cleavage by host cell proteases such as furin. sGP monomers bind to each other to form a homodimer. The role of Ebola virus secreted glycoprotein in EBOV pathogenesis is unclear, but is examined in detail by de la Vega et al (2015).
EBOV envelope glycoproteins (GPs) are known to function as one of the crucial factors that determine the differential virulence across the five different EBOV species (Zaire ebolavirus, Sudan ebolavirus, Bundibugyo ebolavirus, Tai Forest ebolavirus, and Reston ebolavirus). GPs are type I transmembrane glycoproteins composed of GP1 and GP2 and all filoviruses display multiple copies of this single membrane-anchored glycoprotein (GP) projecting from their envelopes. GP is a trimer in which each monomer is a disulfide-bonded complex of a receptor binding subunit (GP1) and a fusion subunit (GP2). The Ebola virus GP has been the target of multiple neutralizing antibodies (Ab), several of which are effective in preventing the onset of disease in nonhuman primates when administered as part of a monoclonal Ab (MAb) cocktail 1 or 2 days after viral exposure (reviewed in Baseler et al., 2017).
Ebola virus envelope glycoprotein GP1 mucin-like region (Emuc) is a highly glycosylated region located at the apex and the sides of each glycoprotein monomer (Tran et al., 2014); it is dispensable for EBOV infections in vitro and not highly conserved. It can induce morphological change of adherent cells in vitro and causes distinct cell and tissue damage and acute inflammation in mouse muscles in vivo (Ning et al., 2018). It is believed to have various functions including influencing GP structure, enhancing viral attachment to target cell surfaces, protecting conserved regions of GP, such the receptor binding site, from antibody recognition, and masking immune regulatory molecules, such as major histocompatibility complex 1 (MHC1), on infected cell surfaces. Emuc may also have a cytotoxic function and could be involved in binding to human CLEC10A. It was reported to be essential to the infectivity of ZEBOV (Yang et al., 2000). As such, neutralizing antibodies are often directed against Emuc for potential therapeutic use.
Source : HEK293
Species : Bundibugyo ebolavirus
Tag : His
Form : Lyophilised
Molecular Mass : A calculated MW of 34.3 kDa. DTT-reduced Protein migrates as 40-55 kDa in SDS-PAGE.
Protein Length : 33-324aa
Purity : >90% pure by SDS-PAGE.
Stability : Stability before reconstitution:
At ambient temperature: 1 month; At 4 centigrade: 12 months; At <-20 centigrade: 24 months
Stability after reconstitution: At -80°C: 3 months
Freezing: Can be frozen, but avoid multiple freeze/thaw cycles
Storage : Store lyophilised product at 4 centigrade for short term, or frozen at -20 centigrade to -80 centigrade for long term. Product is shipped at ambient temperature.
Concentration : Dependent upon reconstitution volume.
Storage Buffer : DPBS pH 7.4.
Reconstitution : It is recommended to reconstitute the protein by adding 500 μL sterile PBS, pH7 to a stock solution of 200μg/mL. Solubilize for 30 to 60 minutes at room temperature with occasional gentle mixing. We recommend the addition of carrier protein (0.1% (w/v) BSA) for further dilution and long term storage.

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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