PRND Human
Description
Product Specs
Product Science Overview
Prion proteins are a unique class of proteins that have garnered significant attention due to their role in neurodegenerative diseases. The term “prion” was first coined by Stanley Prusiner in 1982 to describe “proteinaceous infectious particles” responsible for diseases such as scrapie, Creutzfeldt-Jakob disease (CJD), and kuru . Prion Protein 2 (Human Recombinant) is a synthetic version of the human prion protein, produced using recombinant DNA technology.
The prion protein (PrP) is encoded by the PRNP gene located on chromosome 20 in humans . The normal cellular form of the prion protein, known as PrP^C, is predominantly α-helical and is anchored to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor . PrP^C is expressed at high levels in the brain and is involved in various cellular processes, including cell signaling and protection against oxidative stress .
Prion diseases are caused by the conformational conversion of the normal cellular prion protein (PrP^C) into its misfolded, pathogenic isoform, known as scrapie prion protein (PrP^Sc) . This misfolded form is rich in β-sheets and has the ability to self-replicate by templating the conversion of PrP^C into PrP^Sc . The accumulation of PrP^Sc in the brain leads to neurodegeneration and the characteristic symptoms of prion diseases .
Recombinant prion proteins are produced using recombinant DNA technology, which involves inserting the gene encoding the prion protein into a suitable expression system, such as bacteria or yeast . This allows for the production of large quantities of the protein for research purposes. Recombinant prion proteins are used to study the structure, function, and pathogenic mechanisms of prion proteins, as well as to develop potential therapeutic strategies .
Research on prion proteins has provided valuable insights into the mechanisms of protein misfolding and aggregation, which are also relevant to other neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease . Understanding the structure and function of prion proteins has led to the development of novel therapeutic strategies aimed at preventing or reversing the misfolding of prion proteins .
