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Conditions of optimal PRP Protein performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
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Fax: 1-617-606-5019
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Or leave a message with a formal purchase
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Introduction
Major prion protein, also named PrP, ASCR, PrP27-30, PrP33-35C and CD230, are the proteins that are unique in their ability to reproduce on their own and become infectious which belongs to the prion family. 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.
BP001128-C164: Recombinant Human Major prion protein (PRP)
Source: E. coli-derived.
Recombinant Human Major prion protein (PRP) is expressed with sequence (Gln91-Ser231) of Human PRP.
Purity: > 95% by SEC-HPLC and reducing SDS-PAGE.
Endotoxin: < 0.1 ng/ug (1 EU/ug).
Formulation: Lyophilized from a 0.2 um filtered solution of 5 mM PB, 200 mM NaCl, pH 7.5.
Reconstitution: Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in 1X PBS. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.
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