Monoclonal Antibody to Ebola GP I (Clone: ABM47F9)
Fig-1: Western blot analysis of Ebola GP I. Anti-Ebola GP I antibody (Clone: ABM47F9) was tested at 0.1 µg/ml partial length recombinant protein.
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| Format : | Purified |
| Amount : | 100 µg |
| Isotype : | Mouse IgG2b Kappa |
| Purification : | Protein G Chromatography |
| Content : | 25 µg in 50 µl/100 µg in 200 µl PBS containing 0.05% BSA and 0.05% sodium azide. Sodium azide is highly toxic. |
| Storage condition : | Store the antibody at 4°C; stable for 6 months. For long-term storage; store at -20°C. Avoid repeated freeze and thaw cycles. |
The Sudan ebola virus (SUDV) glycoprotein (GP) is an envelope glycoprotein that is present on the virion surface and is involved in receptor binding and mediating viral entry. It is composed of a trimer of heterodimers (GP1/GP2), where GP1 and GP2 remain covalently linked by a disulfide bond9, and the resulting GP1-GP2 pair trimerizes to form a ~450 kDa envelope spike on the viral surface. GP is synthesized as a single polypeptide of 676 amino acids in length that is post-translationally cleaved by furin to yield two subunits, GP1 and GP2. The GP1 subunit contains two heavily glycosylated domains, the glycan cap and the mucin-like domain (MLD). The glycan cap contains only N-linked glycans, whereas the MLD contains both N- and O-linked glycans. All 15 N-glycosylation sites of GP1 could be removed without compromising the expression of GP. In the endosome, a flexible loop containing GP1 residues 190 213 is cleaved by host cathepsins. This cleavage releases the glycan cap and mucin-like domains from GP1. The GP1 subunit is responsible for receptor binding and attachment to new host cells.
Western blot analysis: 0.5-1 µg/ml
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Secreted |
| Post transnational modification: | Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into GP1 and GP2 by host cell furin in the trans Golgi, and maybe by other host proteases, to yield the mature GP1 and GP2 proteins. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R. This cleavage does not seem to be required for function. After the internalization of the virus into cell endosomes, GP1 C-terminus is removed by the endosomal proteases cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal fragment which is further digested by cathepsin B. Proteolytic processing of GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2 and leads to shedding of complexes consisting in GP1 and truncated GP2 (GP1,2delta) (By similarity). |
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