Measured by its binding ability in a functional ELISA. When Recombinant Viral EBOV GP is
immobilized at 2 µg/mL
(100 µL/well), the concentration of
Recombinant Human CLEC10A/CD301 (Catalog # 4888-CL)
that
produces 50% of the optimal binding response is approximately 20-100
ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived viral EBOV GP protein
Z. ebolavirus GP1 (Ile33-Arg501) Accession # Q05320
Z. ebolavirus
GP2 (Glu502-Gln650) Accession # Q05320
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
69 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
17-24 kDa and 105-120 kDa, reducing conditions
Publications
Read Publications using 9016-EB in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant EBOV GP Protein, CF
bovGP
EBOV GP
second secreted glycoprotein
small secreted glycoprotein
Spike glycoprotein
Background
The GP glycoprotein encoded by the genome of Ebola family viruses is a critical molecule for the pathogenicity of Ebolavirus hemorrhagic viruses (1, 2). It is processed into distinct forms for virus capsule or cell surface presentation or release from virus infected cells. The GP precursor protein is cleaved by furin at a multibasic site to yield a 140 kDa N-terminal fragment (GP1) and a 26 kDa C-terminal fragment (GP2) which remain disulfide linked (3). GP1 is entirely extracellular while GP2 is a transmembrane protein (4). Heterodimers of GP1-GP2 can further associate into trimers (5). GP expressed on virus infected cells can be shed by TACE mediated cleavage, liberating a disulfide linked complex of soluble GP1 and truncated GP2 (4-6). GP binds to multiple C-type lectins on target cell surfaces, including CLEC10A/MGL, DC-SIGN, and DC-SIGNR (7-9). Following internalization, GP1 is cleaved by Cathepsin B and Cathepsin L and then interacts with Niemann-Pick C1 (NPC1) in the endosomal membrane (10-12).
Yang, Z.-Y. et al. (2000) Nat. Med. 6:886.
de La Vega, M.-A. et al. (2015) Viral Immunol. 28:3.
Volchkov, V.E. et al. (1998) Proc. Natl. Acad. Sci. USA 95:5762.
Volchkov, V.E. et al. (1998) Virology 245:110.
Sanchez, A. et al. (1998) J. Virol. 72:6442.
Dolnik, O. et al. (2004) EMBO J. 23:2175.
Takada, A. et al. (2004) J. Virol. 78:2943.
Alvarez, C.P. et al. (2002) J. Virol. 76:6841.
Simmons, G. et al. (2003) Virology 305:115.
Schornberg, K. et al. (2006) J. Virol. 80:4174.
Chandran, K. et al. (2005) Science 308:1643.
Cote, M. et al. (2011) Nature 477:344.
Publications for EBOV GP (9016-EB)(3)
We have publications tested in 2 confirmed species: Human, Rhesus Macaque.
We have publications tested in 3 applications: ELISA Capture, ELISA Control, In Vivo Control.
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