Major Prion Protein; PrP; ASCR; PrP27-30; PrP33-35C; CD230; PRNP; PRIP; PRP

For Research Use Only. Not for use in diagnostic procedures.

E Coli

>90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 mum filtered solution of 5mM PB, 200mM NaCl, pH 7.5.

Lyophilized protein should be stored at < -20 degree C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.

Manufactured in an ISO 9001:2015 Certified Laboratory.

Small volumes of PRP/CD230 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Major Prion Protein is unique in its ability to reproduce on its own and become infectious. The discovery of prion proteins as infectious agents began in the 1980s with an outbreak of mad cow disease in the United Kingdom. They are found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases. They can occur in two forms called PrP-sen and PrP-res. The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. Contains an N-terminal region composed of octamer repeats. Diseases caused by prions are known as spongiform diseases, because the brain tissue in infected individuals is filled with holes, giving it a sponge-like appearance. Although prions are found throughout the brain, the symptoms of spongiform diseases vary according to the regions. There are currently no effective treatments for spongiform diseases and all are fatal. Prions cannot be destroyed by boiling, alcohol, acid, standard autoclaving methods, or radiation. In fact, infected brains that have been sitting in formaldehyde for decades can still transmit spongiform disease.

Molecular Mass: 16.3 kDa
Actual Protein Molecular Mass: 15 kDa

prion protein

major prion protein; alternative prion protein

Major prion protein

ALTPRP; PRIP; PRP; PrP??[Similar Products]

The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2014]

Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains ().

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