Recombinant EBOV GP (Mucin Domain Deleted) Protein, CF

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When Recombinant Viral EBOV GP (Mucin Domain Deleted) Protein (Catalog # 10585-EB) is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human CLEC10A/CD301 Protein (4888-CL) binds with an ED50 of ...read more

Product Details

Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant EBOV GP (Mucin Domain Deleted) Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Viral EBOV GP (mucin domain deleted, Catalog # 10585-EB) is immobilized at 2 µg/mL (100 µL/well), the concentration of Recombinant Human CLEC10A/CD301 (Catalog # 4888-CL) binds with an ED50 of 1-10 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived viral EBOV GP protein
Ebola Virus GP1
(Ile33-Val311)
(Thr42Val, Thr230Val)
Accession # NP_0066246.1
Ebola Virus GP2
(Thr464-Asp632)
Accession # NP_066246.1
HHHHHH
N-terminusC-terminus
Accession #
N-terminal Sequence
Ile33 & Glu502
Protein/Peptide Type
Recombinant Proteins
Purity
>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
51 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
63-75 kDa, under non-reducing conditions

Packaging, Storage & Formulations

Storage
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 PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant EBOV GP (Mucin Domain Deleted) 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).
  1. Yang, Z.-Y. et al. (2000) Nat. Med. 6:886.
  2. de La Vega, M.-A. et al. (2015) Viral Immunol. 28:3.
  3. Volchkov, V.E. et al. (1998) Proc. Natl. Acad. Sci. USA 95:5762.
  4. Volchkov, V.E. et al. (1998) Virology 245:110.
  5. Sanchez, A. et al. (1998) J. Virol. 72:6442.
  6. Dolnik, O. et al. (2004) EMBO J. 23:2175.
  7. Takada, A. et al. (2004) J. Virol. 78:2943.
  8. Alvarez, C.P. et al. (2002) J. Virol. 76:6841.
  9. Simmons, G. et al. (2003) Virology 305:115.
  10. Schornberg, K. et al. (2006) J. Virol. 80:4174.
  11. Chandran, K. et al. (2005) Science 308:1643.
  12. Cote, M. et al. (2011) Nature 477:344.

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