Recombinant humaan PRNP-eiwit

Prion protein, also known as PRNP, is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, collectively known as Transmissible Spongiform Encephalopathies (TSE) . This protein contains a highly unstable region of five tandem octapeptide repeat. 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. Recombinant human PRNP protein, fused to His-tag at N-terminus, was expressed in E. coli.

Prion protein preproprotein, Prion protein preproprotein, ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc

E.coli

Human

His-Tag

SDS-PAGE, Denatured

0.25 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

25 kDa (229aa)

PRNP, ATGP2013-10 µg, ATGP2013-20 µg, ATGP2013-50 µg, ATGP2013-100 µg, ATGP2013-250 µg, ATGP2013-500 µg, ATGP2013-1 mg, ATGP2013-10, ATGP2013-20, ATGP2013-50, ATGP2013-100, ATGP2013-250, ATGP2013-500, ATGP2013-1

Weiss S., et al. (1996) Biochem Biophys Res Commun. 219:173-179.; ; Lee I Y., et al. (1998) Genome Res. 8:1022-1037.;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 0.4M urea, 10% glycerol

Neuroscience

AAH12844

P04156

Human

KKRPKPGGW NTGGSRYPGQ GSPGGNRYPP QGGGGWGQPH GGGWGQPHGG GWGQPHGGGW GQPHGGGWGQ GGGTHSQWNK PSKPKTNMKH MAGAAAAGAV VGGLGGYVLG SAMSRPIIHF GSDYEDRYYR ENMHRYPNQV YYRPMDEYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET DVKMMERVVE QMCITQYERE SQAYYQRGS