CCL21 antibody

Human 6Ckine is a beta or C-C chemokine identified in the Expressed Sequence Tag (EST) database by three independent groups. Known also as Exodus2 and secondary lymphoid-tissue chemokine (SLC), 6Ckine contains four conserved cysteine (C) residues which are characteristic of beta-chemokines. Two additional conserved cysteine residues have been found in its unusually long carboxy-terminal domain and consequently the name 6Ckine. Human and mouse 6Ckine are highly conserved and show 86% amino acid homology. Human 6Ckine cDNA encodes a 134 amino acid precursor protein, a 23 amino acid signal peptide and a 111 amino acid mature protein. This protein shares 21 % to 33 % homology with other human C-C chemokines. Comparatively, mouse 6Ckine cDNA encodes a 133 amino acid precursor protein, a 23 amino acid signal peptide and a 110 amino acid mature protein. Recombinant human 6Ckine has a predicted molecular mass of approximately 12 kDa (mature protein). In SDS-PAGE under reducing and non-reducing conditions, the recombinant protein migrates with an apparent molecular mass of 16 kDa to 17 kDa. The human 6Ckine gene has been mapped to chromosome 9p13. The expression of human 6Ckine has been detected primarily in lymphoid tissues but also in the gastrointestinal tract. Recombinant human 6Ckine is chemotactic for some human T-cell lines, resting peripheral blood lymphocytes, and normal cultured T-cells treated with PHA and IL2. Unlike other C-C chemokines, 6Ckine is not chemotactic for monocytes and neutrophils. A growing body of work suggests that 6Ckine influences lymphocyte homing to secondary lymphoid organs, integrin-mediated lymphocyte adhesion, and may act via the EBI1 ligand chemokine (ELC) receptor, CCR7.