
Background
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 RELM-alpha. 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 disulfide-linked homodimer with a total molecular weight of 19.0 kDa, consisting of two 89 amino acid residue chains.
Specifications