NDLI: Antiaggregating Antibody Raised Against Human PrP 106-126 Recognizes Pathological and Normal Isoforms of the Whole Prion Protein

Content Provider	Springer Nature Link
Author	Hanan, Eilat Priola, Suzette A. Solomon, Beka
Copyright Year	2001
Abstract	Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity when challenged with PrP from diverse species. We have produced an antibody [monoclonal antibody (mAb) 2-40] raised against a synthetic peptide corresponding to residues (106-126 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (i.e., sheep, hamsters, and mice). Together with the fact that it recognizes the whole PrP in both cellular and scrapie isoforms, mAb 2-40 may be helpful in studying conformational changes of the PrP, as well as establishing a possible connection between human and animal diseases.
Starting Page	693
Ending Page	703
Page Count	11
File Format	PDF
ISSN	02724340
Journal	Cellular and Molecular Neurobiology
Volume Number	21
Issue Number	6
e-ISSN	15736830
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2001-01-01
Publisher Place	New York
Access Restriction	Subscribed
Subject Keyword	Neurosciences Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Cellular and Molecular Neuroscience

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