Anti-CXCL14

CXCL14/BRAK, also named MIP-2 gamma, KEC (kidney-expressed chemokine), and BMAC (B cell and monocyte-activating chemokine), is a member of the CXC chemokine superfamily. The deduced 99 amino acid (aa) residue precursor has a 22 aa putative signal peptide that is cleaved to produce the 77 aa mature protein. Mature human and mouse CXCL14 differ by only 2 residues. Mouse CXCL14 shares approximately 30% aa sequence identity with mouse MIP-2. Unlike MIP-2, CXCL14 lacks the ELR domain preceding the CXC motif. CXCL14 transcripts are constitutively expressed at high levels in the basal layer of epidermal keratinocytes and dermal fibroblasts of skin tissues as well as lamina propria cells in normal intestinal tissues. CXCL14 has been shown to be a highly selective chemoattractant for monocytes that have been treated with prostaglandin E2 or forskolin, agents that activate adenylate cyclase. CXCL14 has been proposed to be important in regulating the trafficking of macrophage precursor to regions in skin and mucosal tissues that support their development. Consistent with this hypothesis, macrophages were frequently found to co-localize with CXCL14-producing cells in the dermis and lamina propria. Protein function: Chemotactic for CESS B-cells and THP-1 monocytes, but not T- cells. [The UniProt Consortium]