Cytokeratin 19 (Keratin, type I cytoskeletal 19, also KRT-19, CK19 and Keratin-19) is a 40-45 kDa, acidic Class I keratin member of the intermediate filament family of proteins. Individual keratins are always expressed in tandem with a second keratin, and these are found in all epithelial cells. The class I KRT-19 heterodimerizes/polymerizes with 50-52 kDa class II KRT-8 (plus KRT-5 and-7) to form 8-10 nm filaments in epidermal stem cells, secretory gland (sweat, mammary, bile duct) simple epithelium, and neuroendocrine epidermal Merkel cells. It may represent a viable marker for skin stem cells. In skin, Cytokeratin 19 forms filaments in the fetal epithelium, and then progressively decreases with age, being virtually absent by age 17. Human Cytokeratin 19 is 400 amino acids (aa) in length. It contains an N-terminal "head" region (aa 1-79) and a subsequent "rod" region (aa 80-387), but is absent a typical C-terminal tail region. Cytokeratin 19 possesses at least 5 utilized phosphorylation sites plus one acetylated Lys residue. Based on other keratins, and the presence of an Asp at position 238, there may be caspase cleavage-generated isoforms. Full length human Cytokeratin 19 (aa 2-400) shares 82% aa sequence identity with mouse Cytokeratin 19.
Cytomegalovirus (CMV) (human herpesvirus 5) glycoprotein B, also referred as CMV gB or gB, which belongs to the herpesviridae glycoprotein B family. It is a 97-amino acid glycoprotein encoded by the ORF of UL55. Cytomegalovirus Glycoprotein B protein is the most abundant component of the envelope, a target of neutralizing antibodies with at least two defined neutralizing epitopes and an essential replication component. Cytomegalovirus Glycoprotein B protein plays important roles in HCMV entry, cell-cell spread of internal virions, and fusion of infected cells. In addition, Cytomegalovirus Glycoprotein B protein is one envelope protein capable of heparin binding. It forms a physical association with host cell annexin II independent of the presence of calcium.
D-Amino-Acid Oxidase (DAO) belongs to the DAMOX/DASOX family. DAO is a peroxisomal enzyme which founctions as a homodimer to oxidizes D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. D-amino-acid oxidase regulates the level of the neuromodulator D-serine in the brain, has a high activity towards D-DOPA and contributes to dopamine synthesis. D-amino-acid oxidase could act as a detoxifying agent which removes D-amino acids accumulated during aging. It also acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups.
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