Prion Proteins & Peptides

Prion Diseases, or transmissible spongiform encephalopathies (TSEs), are a group of progressive neurodegenerative disorders of the CNS. Rare but fatal, common TSEs in animals are Bovine Spongiform Encephalopathy and Chronic Wasting Disease; examples in humans include Creutzfeldt-Jakob disease and Kuru. The disease is thought to develop when abnormal protein molecules (prions) accumulate in the brain, causing convulsions, ataxia, dementia, and death. TSEs are difficult to diagnose, and lead to dead tissue and sponge-like holes in the brain. Scientists are trying to determine the normal role of prions in the brain, as well as the mechanisms by which they become misshapen and accumulate. TSEs are currently incurable, but the goal is to find ways to block the conversion of normal prion protein to the abnormal form.

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SML1515 Anle138b ≥98% (HPLC)
SML1905 KR7 trifluoroacetate salt ≥98% (HPLC)
P3615 Prion Protein Fragment 106-126 Human ≥90% (HPLC), solid
P4238 Prion Protein Fragment 106-126 Scrambled Human ≥85% (HPLC), solid
P2990 Prion PrP N-Terminal Peptide Fragment 79-97 solid