antibody

Ebola GP I; GP

MBS668203

0.1 mg

290 USD

monoclonal

mouse

nonconjugated

[ABM47F9]

Antibody

Ebola GP I; GP

[Ebola GP I]

[spike glycoprotein; Envelope glycoprotein; spike glycoprotein; small secreted glycoprotein; second secreted glycoprotein; GP1,2; GP]

[GP]

[GP; GP; GP]

VGP_EBOSU

Monoclonal

IgG2b, Kappa

[ABM47F9]

Mouse

676

Protein G Chromatography

Purified

Store the antibody at 4 degree C, stable for 6 months. For long-term storage, store at -20 degree C. Avoid repeated freeze and thaw cycles.

Western Blot (WB)

Western Blot analysis: 0.5-1ug/ml

Western Blot (WB)

Immunogen: A partial length recombinant GP I protein of Sudan Ebola virus was used as an immunogen for this antibody. Content: 25ug in 50ul/100ug in 200ul PBS containing 0.05% BSA and 0.05% sodium azide.Sodium azide is highly toxic.

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 ap and mucin-like domains from GP1. The GP1 subunit is responsible for receptor binding and attachment to new host cells.

55770812

YP_138523.1

NC_006432.1

Q7T9D9

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). Binding to the macrophage specific lectin CLEC10A also seem to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably induces a conformational change of GP2, allowing its binding to the host entry receptor NPC1 and unmasking its fusion peptide to initiate membranes fusion.

0.1 mg

290 USD