Recombinant AMARV GP protein (His tag)
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Recombinant AMARV GP protein (His tag) is a Lake Victoria marburgvirus (strain Angola/2005) Fragment protein, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for ELISA, WB, SDS-PAGE.
View Alternative Names
Envelope glycoprotein, Virion spike glycoprotein, GP
- ELISA
Supplier Data
ELISA - Recombinant AMARV GP protein (His tag) (AB190126)
Plate was coated with ab190126 starting at 800 ng/well, serially diluted in DPBS. Washed plate was detected using one dilution of a positive control serum, followed with anti-IgG HRP conjugate and TM substrate. OD650 is reported. Background of ab190126 coated plate without positive control serum was 0.051 OD650.
- WB
Supplier Data
Western blot - Recombinant AMARV GP protein (His tag) (AB190126)
All lanes:
rabbit polyclonal antibody anti AMARV GP at 0.5 µg/mL
Lane 1:
Western blot - Recombinant AMARV GP protein (His tag) (ab190126) at 0.1 µg
Lane 2:
Western blot - Recombinant AMARV GP protein (His tag) (ab190126) at 0.5 µg
Lane 3:
Western blot - Recombinant AMARV GP protein (His tag) (ab190126) at 1 µg
Secondary
All lanes:
anti-rabbit IgG-HRP conjugate, followed by substrate.
false
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant AMARV GP protein (His tag) (AB190126)
SDS-PAGE analysis of 1 μg and 5 μg (lanes 1, 2 respectively) of ab190126 under denaturing and reducing conditions.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Specifications
Form
Liquid
Additional notes
ab190126 is affinity purified by FPLC.
General info
Function
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 (DCs), 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 (trans infection) (By similarity).. 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 (heptad repeats) 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 (By similarity).
Sequence similarities
Belongs to the filoviruses glycoprotein family.
Post-translational modifications
N-glycosylated.. O-glycosylated in the mucin-like region.. 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 (By similarity).. GP1 is phosphorylated on serine residues between residues 260 and 273.
Target data
Product promise
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