The Monocyte Chemoattractant Protein -1 (MCP1/CCL2) belongs to C-C family of chemokines is a key regulator of migration and infiltration of monoctes/macrophages into the tissue. We amplified and cloned the cDNA encoding MCP-1 from the dromedary camel to understand the role of this chemokine in camel immunology. The 395 bp fragment amplified from lung cDNA contained an ORF of 300 bp coding for 99 amino acid protein. The predicted MCP-1 protein shared 86%,82%,81 % and 72% amino acid identity with the porcine, bovine, human and murine equivalents. A 23 amino acid signal peptide was predicted in the N terminal end leaving the mature protein of 77 amino acids long with an estimated molecular weight of 8. 7 kDa. The predicted secondary structure for the mature protein had the three beta sheets and one alpha helix characteristic of the chemokine. There are four cysteine residues in the mature MCP-1 sequence of which the first two were adjacent to the N terminal, characteristic of CC chemokine. The two disuplhide bonds (Cys 11-cys 36 and Cys 12-Cys 52) are predicted between four Cysteine residues. The key residues involved in dimer formation and receptor binding was found to be conserved. CCL2 mRNA transcripts were detected in heart, kidney, liver, lung, lymph node, PBMCs and spleen. To understand the genomic organization of the CCL2 gene we amplified the entire CCL 2 sequence of 1487 bp from genomic DNA that contained three exons separated two introns. The identified camel MCP-1/CCL2 can be further used to develop species specific reagents or therapeutics for diagnosis and management of infections in camels.