Prion diseases Related Peptides
Bio-Synthesis offers a new line of Prion related peptides. Prion Protein Fragment 106-126 Human. This peptide is used as model to investigate neurodegeneration in prion diseases. Prion fragment 106-126 scarmbled Human, used as a control in the study of the biological activity of prion protein. N-terminal fragment of the protease resistant prion protein (PrP), Prion PrP N-terminal Peptide fragment 79-97.
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response.
The causative agents of TSEs are believed to be prions. The term "prions" refers to abnormal, pathogenic agents that are transmissible and are able to induce abnormal folding of specific normal cellular proteins called prion proteins that are found most abundantly in the brain. The functions of these normal prion proteins are still not completely understood. The abnormal folding of the prion proteins leads to brain damage and the characteristic signs and symptoms of the disease. Prion diseases are usually rapidly progressive and always fatal.
Familial prion diseases of humans include classic Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal insomnia (FI). These conditions form a spectrum of diseases with overlapping signs and symptoms.