Prion Protein, recombinant

The PrPc appears as a single band of about 27 kD by SDS-PAGE

Antigen in standard immunochemical detection of BSE.

Optimal working dilution must be determined by the end user.

Research Category
Neuroscience

Research Sub Category
Neurodegenerative Diseases

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Histidine-tagged full-length mature part of bovine PrP (25-244) is expressed in E. Coli BL21, solubilized from inclusion bodies in 6 M guanidine-HCl, and purified by Ni(II)-nitriloacetate agarose chromatography followed by reversed-phase HPLC (C4 column)

Prion diseases or transmissible spongiform encephalopathies are neurodegenerative diseases that affect both humans and animals (Prusiner 1998). All prion diseases share the same molecular pathogenic mechanism that involves conversion of normal cellular prion protein (PrPc) into a form that is insoluble in non ionic detergent and partially resistant to proteases (PrPSc) (Pan et al. 1993). Both PrPSc and PrPc are encoded within a single exon of a chromosomal gene as a protein of ~ 250 amino acids (Basler et al. 1986). Many mammalian PrPs have a 22 amino acid N-terminal signal sequence (Hope et al. 1986; Turk et al. 1988) and 23 amino acid C-terminal signal sequence encoding for attachment of a glycosylphosphatidylinositol anchor (Stahl et al. 1987, 1990). The mature protein of 209 amino acids contains one disulfide bond (Turk et al. 1988) and has two sites of asparagine-linked glycosylation (Endo et al. 1989; Oesch et al. 1995).

Liquid in 10 mM sodium acetate buffer, pH 4.0, containing 0.01% sodium azide.

Maintain at -20°C in undiluted aliquots for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles.

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