vCCI Antibody (13J-1): sc-80432

vCCI Antibody (13J-1) is a mouse monoclonal IgG1 antibody that detects the vCCI protein of viral origin by western blotting (WB) and enzyme-linked immunosorbent assay (ELISA). Anti-vCCI antibody (13J-1) is available as the non-conjugated format. vCCI protein, known as viral C-C chemokine inhibitor, plays a crucial role in modulating the immune response during viral infections. vCCI is secreted by poxviruses and functions by binding with high affinity to various C-C chemokines, effectively blocking their interaction with G protein-coupled receptors and glycosaminoglycans on immune cells. This inhibition disrupts normal chemotactic signaling pathways that would typically recruit immune cells to sites of infection, thereby allowing the virus to evade the host′s immune response and reduce inflammation. Notably, vCCI does not share amino acid sequence homology with any known cellular proteins, highlighting a unique mechanism of action and specificity. vCCI′s ability to selectively inhibit C-C chemokines while having low or no affinity for chemokines from other subfamilies underscores potential therapeutic interventions in viral infections.

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vCCI Antibody (13J-1) References:

1. Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus.  |  Carfí, A., et al. 1999. Proc Natl Acad Sci U S A. 96: 12379-83. PMID: 10535930
2. The viral CC chemokine-binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site.  |  Beck, CG., et al. 2001. J Biol Chem. 276: 43270-6. PMID: 11551937
3. Comprehensive mapping of poxvirus vCCI chemokine-binding protein. Expanded range of ligand interactions and unusual dissociation kinetics.  |  Burns, JM., et al. 2002. J Biol Chem. 277: 2785-9. PMID: 11696549
4. A soluble chemokine-binding protein from vaccinia virus reduces virus virulence and the inflammatory response to infection.  |  Reading, PC., et al. 2003. J Immunol. 170: 1435-42. PMID: 12538705
5. [Phylogenetic analysis of chemokine-binding protein gene from orthopoxviruses].  |  Mikheev, MV., et al. 2004. Mol Gen Mikrobiol Virusol. 29-36. PMID: 15025002
6. Rat aortic MCP-1 and its receptor CCR2 increase with age and alter vascular smooth muscle cell function.  |  Spinetti, G., et al. 2004. Arterioscler Thromb Vasc Biol. 24: 1397-402. PMID: 15178559
7. Resonance assignments and secondary structure of vCCI, a 26 kDa CC chemokine inhibitor from rabbitpox virus.  |  Derider, ML., et al. 2006. J Biomol NMR. 36 Suppl 1: 22. PMID: 16534540
8. Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta.  |  Zhang, L., et al. 2006. Proc Natl Acad Sci U S A. 103: 13985-90. PMID: 16963564
9. Poxvirus genomes encode a secreted, soluble protein that preferentially inhibits beta chemokine activity yet lacks sequence homology to known chemokine receptors.  |  Smith, CA., et al. 1997. Virology. 236: 316-27. PMID: 9325239