RELM beta

Human RELM beta is a 19.0 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELM beta, and its molecular targets, are not fully known but, it has been suggested that it plays a regulatory role during inflammation and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly the molecular structure of RELM beta is highly homologous to that of the adipose-derived cytokine Resistin and RELMa. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant human RELM beta is a 19.0 kDa homodimer consisting of two identical 89 amino acid chains linked by a single disulfide bond.