Recombinant Viral CCI Fc Chimera (CHO-expressed) Protein, CF

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Measured by its ability to inhibit JE-induced chemotaxis of BaF3 mouse proB cells transfected with human CCR2A. The ED50 for this effect is 0.06 -0.3 μg/mL in the presence of 20 ng/mL of Recombinant Mouse ...read more

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Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Viral CCI Fc Chimera (CHO-expressed) Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit JE-induced chemotaxis of BaF3 mouse pro‑B cells transfected with human CCR2A. The ED50 for this effect is 0.06-0.3 μg/mL in the presence of 20 ng/mL of Recombinant Mouse CCL2/JE/MCP-1 (Catalog # 479-JE).
Source
Chinese Hamster Ovary cell line, CHO-derived viral CCI protein
Viral CCI
(Met1-Val258)
Accession # P19063
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Met17
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
52.6 kDa (monomer).
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
60-66 kDa, 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 under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 Viral CCI Fc Chimera (CHO-expressed) Protein, CF

  • CCI

Background

The family of T1/35 kDa proteins are encoded by the '35K' virulence gene of many poxviruses and are secreted from virus-infected cells. These proteins bind
CC-chemokines with high affinity and are termed viral chemokine inhibitor (vCCI). Viral CCI from various poxviruses share multiple stretches of sequence identity and eight conserved cysteine residues (1). The vaccinia virus (strain Lister) vCCI cDNA encodes a 258 amino acid (aa) protein with a putative 17 aa signal peptide (2). Vaccinia virus (strain Lister) vCCI shows greater than 90% aa sequence identity with vCCI from other orthopoxviruses and approximately 40% aa sequence identity with the leporipoxvirus T-1 proteins. vCCI binds with high affinity to many human, mouse, and rat CC-chemokines (1, 3-5). It binds to the same surfaces of these chemokines that are involved in chemokine receptor interactions (4-7). Some CC-chemokines utilize common binding surfaces on vCCI, while others interact with distinct sites on vCCI (8). vCCI inhibits CC-chemokine induced monocyte chemotaxis in vitro but does not block cellular effects induced by CXCL5/ENA-78, CXCL8/IL-8, or CXCL10/IP-10 (3-5). In vivo, vCCI restricts the infiltration of  immune cells into sites of inflammation (3, 9, 10) and also the CC-chemokine induced migration of arterial vascular smooth muscle cells (11).
  1. Graham, K.A. et al. (1997) Virology 229:12.
  2. Patel, A.H. et al. (1990) J. Gen. Virol. 71:2013.
  3. Buatois, V. et al. (2010) J. Immunol. 185:2544.
  4. Smith, C.A. et al. (1997) Virology 236:316.
  5. Lalani, A.S. et al. (1998) Virology 250:173.
  6. Beck, C.G. et al. (2001) J. Biol. Chem. 276:43270.
  7. Seet, B.T. et al. (2001) Proc. Natl. Acad. Sci. 98:9008.
  8. Burns, J.M. et al. (2002) J. Biol. Chem. 277:2785.
  9. Dabbagh, K. et al. (2000) J. Immunol. 165:3418.
  10. Reading, P.C. et al. (2003) J. Immunol. 170:1435.
  11. Spinetti, G. et al. (2004) Arterioscler. Throm. Vasc. Biol. 24:1397.

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