|Other Names||Major prion protein, PrP, ASCR, PrP27-30, PrP33-35C, CD230, PRNP, ALTPRP, PRIP, PRP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2865c was selected from the Center region of human PRNP. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||ALTPRP, PRIP, PRP|
|Function||May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).|
|Cellular Location||Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of CU(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis|
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Provided below are standard protocols that you may find useful for product applications.
PRNP is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. This protein contains a highly unstable region of five tandem octapeptide repeats. Mutations in the repeat region as well as elsewhere in PRNP gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.
Cervenakova L., Buetefisch C., Lee H.S., Taller I., Stone G., Gibbs C.J. Jr., Brown P., Hallett M., Goldfarb L.G.Am. J. Med. Genet. 88:653-656(1999) Perry R.T., Go R.C., Harrell L.E., Acton R.T.Am. J. Med. Genet. 60:12-18(1995)NMR structures of three single-residue variants of the human prion protein.Proc. Natl. Acad. Sci. U.S.A. 97:8340-8345(2000)
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