|CCI Inhibition of CCL2/JE-dependent Chemotaxis and Neutralization by Viral CCI Antibody. Recombinant Viral CCI Fc Chimera (Catalog # 696-CC) inhibits Recombinant Mouse CCL2/JE (Catalog # 479-JE) induced chemotaxis in the BaF3 mouse pro‑B cell line transfected with human CCR2A in a dose-dependent manner (orange line). The amount of cells that migrated through to the lower chemotaxis chamber was measured by Resazurin (Catalog # AR002). Inhibition of Recombinant Mouse CCL2/JE (20 ng/mL) activity elicited by Recombinant Viral CCI Fc Chimera (0.4 µg/mL) is neutralized (green line) by increasing concentrations of Viral CCI Monoclonal Antibody (Catalog # MAB6961). 6 μg/mL of this antibody will neutralize 60 % Recombinant Viral CCI Fc Chimera activity.|
The family of T1/35 kDa proteins are secreted, soluble proteins encoded by the '35K' virulence gene of many poxviruses. These proteins have been shown to bind CC-chemokines with high affinity and are now termed viral chemokine inhibitor (vCCI). Viral CCI from various poxviruses share multiple stretches of identical sequence motif and eight conserved cysteine residues. The vaccinia virus (strain Lister) vCCI cDNA encodes a 258 amino acid (aa) residue protein with a putative 17 amino acid residue signal peptide. 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.
Recombinant vCCI has been shown to be a potent general inhibitor of CC-chemokine activity in vitro and blocks binding of CC chemokines to cell surface chemokine receptors. In in vivo studies using a virus mutant in which the gene encoding the CCI has been deleted, leukocyte infiltration into the virus-infected areas is increased, suggesting that CCI can modulate the influx of inflammatory cells into virus-infected tissues.
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