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C164
Recombinant Human CD230/Major prion protein/PrP/CD230
10ug
840
756
现货
国产
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C164
Recombinant Human CD230/Major prion protein/PrP/CD230
50ug
2520
2268
现货
国产
-
C164
Recombinant Human CD230/Major prion protein/PrP/CD230
500ug
12320
11088
现货
国产
-
C164
Recombinant Human CD230/Major prion protein/PrP/CD230
1mg
17600
15840
现货
国产
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Catalog# C164 Source E.coli Description Recombinant Human Major Prion Protein/PRP is produced with our E. coli expression system. The target protein is expressed with sequence (Gln91-Ser231) of Human PRP. Names Major Prion Protein, PrP, ASCR, PrP27-30, PrP33-35C, CD230, PRNP, PRIP, PRP Accession # P04156 Formulation Lyophilized from a 0.2 μm filtered solution of 5mM PB, 200mM NaCl, pH 7.5 Shipping The product is shipped at ambient temperature. 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 μg/ml.
Dissolve the lyophilized protein in 1X PBS.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Endotoxin Less than 0.1 ng/μg (1 IEU/μg). Amino Acid Sequence MGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYVLGSAMSRPIIHFGSDYEDRYYREN MHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQY ERESQAYYQRGSSBackground 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.