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Cytokeratin 20 is a type I keratin which is primarily expressed in gastric and intestinal epithelium, urothelium, and Merkel-cells. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Their genes are clustered in a region of chromosome 17q12-q21. Cytokeratin 20 is a major

Napsin A is an aspartic proteinase that belongs to the peptidase A1 family and plays a role in pneumocyte surfactant processing. It is a 420-amino acid polypeptide consisting of a 24-residue signal peptide, a 40-amino acid propart, the mature enzyme of 336 amino acids, and a C-terminal extension of 18 residues. The mature Napsin A protein contains 3 predicted disulfide bonds, 3 potential N-linked oligosaccharide attachment sites, an RGD motif, a recognition motif for integrin binding, in the

This gene encodes a member of the keratin family, the most diverse group of intermediate filaments. This gene product, a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11. [provided by RefSeq].

This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, e

Renin catalyzes the first step in the activation pathway of angiotensinogen--a cascade that can result in aldosterone release,vasoconstriction, and increase in blood pressure. Renin, an aspartyl protease, cleaves angiotensinogen to form angiotensin I, which is converted to angiotensin II by angiotensin I converting enzyme, an important regulator of blood pressure and electrolyte balance. Transcript variants that encode different protein isoforms and that arise from alternative splicing ａn

Monomeric IgA constitutes 5-15 % of the serum immunoglobulins whereas dimeric IgA is localized to mucosa surfaces such as saliva, gastrointestinal secretion, bronchial fluids and milk. Mucosal IgA plays a major role in host defence by neutralising infectious agents at mucosal surfaces. The production is usually local and antigen specific IgA producing B-cells can be found in regions under the lamina propria where they mature into dimeric IgA producing plasma cells. IgA deficiency is the most