Recombinant Human Uteroglobin

Uteroglobin, which is a member of the Secretoglobin superfamily and is also known as Clara cell phospholipid-binding protein, is a multifunctional protein that can exert anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. The small, non-glycosylated protein named for its high levels of expression in pre-implantation embryos, where it exhibits growth stimulatory effects, is produced and secreted by the non-ciliated, non-mucous Clara cells predominant in the epithelial surfaces of pulmonary airways, as well as other non-ciliated epithelia. Members of the Secretoglobin superfamily demonstrate a high level of structural conservation and are characterized as small, secretory homo- or heterodimers. In addition to sequestering pro-inflammatory mediators and carcinogens, Uteroglobin has been implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. Recombinant Human Uteroglobin is a 16.1 kDa homodimeric protein consisting of 142 amino acid residues.