Background:  Prion protein PrP 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. Two transcript variants encoding the same protein have been found for this gene. 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). Both PrPsc and PrPc are encoded within a single exon of a chromosomal gene as a protein of ~ 250 amino acids. Many mammalian PrPs have a 22 amino acid N terminal signal sequence and 23 amino acid C terminal signal sequence encoding for attachment of a glycosylphosphatidylinositol anchor. The mature protein of 209 amino acids contains one disulfide bond and has two sites of asparagine linked glycosylation.

Description: Rabbit polyclonal to Prion protein

Immunogen: KLH conjugated synthetic peptide derived from Prion protein

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 28 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/100-200;

·Immunocytochemistry: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.