WB, IHC, IHC-PHost:
Applications: WB, IP
Applications: WB, ELISA, PA
Human fetuin (2-Heremans-Schmid-glycoprotein or a2-HS glycoprotein) is a major plasma glycoprotein predominantly synthesized in the liver. Human fetuin is named after its bovine homolog. Fetuins are found in most mammals. Human fetuin is a negative acute-phase protein; normal circulating levels in adults (300600 g/ml) fall significantly (3050%) during injury and infection. The biological role of fetuin is unknown, although it has been implicated as an immunomodulator that can participate in stimulation of bacterial phagocytosis by neutrophils and promotion of endocytosis by mouse macrophages. Hepatocytes are the principal cell source of circulating fetuin, but it also is expressed by monocyte/macrophages. Fetuins occur in large amounts in blood and cerebrospinal fluid and accumulate to high concentrations in calcified bone. The fetuin promoter region has several potential interleukin 6-responsive elements, and its synthesis is down-regulated during injury and inflammation. Fetuin is an acidic glycoprotein with three N-linked and three O-linked oligosaccharide chains, whose terminal sugar residues are rich in sialic acid (N-acetylneuraminic acid), contributing to its net negative charge. A role for fetuin as a carrier of bioactive molecules has been proposed based on observations that it binds and carries Ca2+ ion. Fetuin is implicated in bone remodeling, immune function and may play a role in tumor progression of certain cell types. Fetuin plays a role as an anti-inflammatory agent by suppressing the release of TNF from stimulated macrophages. Fetuin also interacts with members of the matrix metalloprotease family of zinc dependent secreted transmembrane proteins that degrade basement membranes and extracellular matrix components. The biological activity of fetuin is mediated through its direct interaction with other proteins. Fetuin down-regulates a number of receptor tyrosine kinase family members. A motif within fetuin has homology to the TGF-b receptor type II. Circulating human plasma fetuin is partly phosphorylated which implies that phosphorylated fetuin may have a physiological function in vivo. Human fetuin isolated from plasma is a two-chain molecule consisting of a A-chain of 322 amino acid residues (53 kDa) and a B-chain of 27 residues (5 kDa). The carboxy terminal 40 amino acids of the A chain constitute a bridging peptide that may be removed proteolytically in vivo. A single mRNA encodes both the A and B chains. The apparent molecular weight of intact human fetuin is 58 kDa.
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