Anti-Prion Protein Antibody, clone 12D6.1

Descrição detalhada : Major prion protein (UniProt P04156; also known as ASCR, CD230, PrP, PrP27-30, PrP33-35C) is encoded by the PRNP (also known as ALTPRP, CJD, GSD, HDL1, KURU, PRIP, PRP, SENF) gene (Gene ID 5621) in human. The major prion protein (PrP) is synthesized with an N-terminal signal peptide (a.a. 1-22) and a C-terminal proptptide (a.a. 231-253) sequence, which are posttranslationally removed to yield the mature (a.a. 23-230) N-glycosylated, glycosylphosphatidylinositol (GPI)-anchored cell surface protein. Structurally, PrP consists of a long, disordered, flexible NH2-proximal region and a globular COOH-proximal domain linked together by a hydrophobic core (HC) region (a,a. 111-134) that is considered as a key region in both physiological and disease related processes involving the prion protein. The N-terminal region is composed of five octapeptide (PHGGGWGQ) repeats (a.a. 51-91) sandwiched between two positively charged clusters, CC1 & CC2 (a.a. 23-27 & 95-110). The exact physiological function of PrP is not known, although various biological functions have been suggested for this protein, including signal transduction, neurotransmitter metabolism, cell adhesion, antioxidant activity, neurogenesis, immune cell activation, copper metabolism and homeostasis of trace elements. Transmissible spongiform encephalopathies (TSEs) represent a family of rare and fatal neurodegenerative disorders, including Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome, fatal familial insomnia and kuru in human, bovine spongiform encephalopathy in cattle, and scrapie in sheep. It is widely accepted that the conformational transition of the native and predominantly α-helical cellular PrP (PrPC) to a β-sheet-rich pathogenic scrapie isoform (PrPSc) is responsible for the accumulation of PrPSc aggregates.
Sinónimos : Major prion protein, ASCR, CD230, PrP, PrP27-30, PrP33-35C
Armazenamento : +2°C to +8°C
Embalagem : 1X1EA