
Human RELMβ is a 19.0 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMβ 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 RELMβ is highly homologous to that of the adipose-derived cytokine Resistin and RELMα. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X<sub>11</sub>-C-X<sub>8</sub>-C-X-C-X<sub>3</sub>-C-X<sub>10</sub>-C-X-C-X-C-X<sub>9</sub>-C-C. Recombinant Human RELMβ is a disulfide-linked homodimer with a total molecular weight of 19.0 kDa, consisting of two 89 amino acid residue chains.
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