Conformation-Specific Antibodies

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An antibody that recognizes a specific, three-dimensional antigenic conformation offers greater insight to biological processes. We developed and commercialized a number of important conformation-specific antibodies to support Alzheimer’s, Parkinson’s and Prion protein targets. Researchers choose conformation-specific antibodies for their studies because 3-dimensional structure of proteins is critical for their functional studies. Merck provides antibodies to identify particular conformational states or protein-protein interactions.

Journal and Article Publications

Alzheimer's Disease Related

TargetSpecificityMethodCatalog No.
Amyloid-ß This antibody recognizes amyloid-ß and not APP (amyloid precursor protein). Specifically, clone 6C3 recognizes unaggregated, oligomeric, and fibrillar forms of Aß42 and Aß40. Eptide MABN254
Amyloid beta oligomers This antibody recognizes all types of amyloid oligomer but not normal native proteins, amyloidogenic monomer or mature amyloid fibrils. Recombinant protein aggregates AB9234
Amyloid fibrils This antibody recognizes amyloid fibrils, not oligomers or monomers Engineered camelid fragment MABN687
Amyloid fibrils These antibodies recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Recombinant protein aggregates AB2286
Amyloid fibrils These antibodies recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. Recombinant protein aggregates AB2287
Amyloid B fibrils This antibody recognizes a specific conformation of residues 2-7 of the amyloid Aß peptide sequence (AEFRHD) found in amyloid fibrils. It does not detectably react with APP, IAPP, a-synuclein or polyQ fibrils Recombinant protein aggregates MABN640
Tau - oligomeric This antibody is specific for oligomeric Tau, not with monomer Tau or fibril Tau. This ab neutralizes oligomer Tau toxicity. Recombinant protein aggregates ABN454
Neurofibrillary tangles Specifically stains neurofibrillary tangles and degenerating plaque neuritis, not monomers. Highly enriched Paired Helical Filament (PHF) fractions from brain AB1518

Down Syndrome Related

Target
Specificity
Method
Catalog No.
Neurofibrillary tangles Specifically stains neurofibrillary tangles and degenerating plaque neuritis, not monomers. Highly enriched Paired Helical Filament (PHF) fractions from brain AB1518

Parkinson's Disease Related

Target
Specificity
Method
Catalog No.
Aggregated alpha synuclein Aggregated alpha synuclein, not monomers Recombinant protein aggregates MABN389

Prion Protein Related

Target
Specificity
Method
Catalog No.
Scrapie prion This antibody has a conformational epitope at the proposed binding site for the putative prion conversion co-factor protein X Purified Scrapie prions MABN780
Native prion This antibody binds a single linear epitope in the β2-α2 loop region of PrP Purified Scrapie prions MABN772
Scrapie prion This antibody binds within the octarepeat region and near the site of N-terminal truncation of PrP(Sc) by proteinase K Purified Scrapie prions MABN768

Cancer Related

Target
Specificity
Method
Catalog No.
P-glycoprotein This antibody is directed against the extracellular conformational epitope of P-glycoprotein (Pgp) BALB/c 3T3 fibroblasts transfected with human MDR1 cDNA, followed by selection for resistance to vinblastine. MAB4334

Apoptosis Related

Target
Specificity
Method
Catalog No.
Single-stranded DNA This antibody specifically reacts with single-stranded DNA and not recognize DNA in double-stranded conformations Calf thymus single-stranded DNA MAB3299

References:

Brooks, P C, et al. 1994. Science 264: 569-71.
Celej, M. S., et al. 2012. Biochem. J. 443: 719-26.
Cheresh, D. A. 1987. Proc. Natl. Acad. Sci. U.S.A., 84: 6471-5.
Frankfurt, O.S. 1987. Exp. Cell. Res. 170:369-380.
Habicht, G., et al. 2007. Proc. Natl. Acad. Sci. U.S.A. 104(49):19232-19237.
Ihara, Y, et al. 1983. Nature 304: 727-30.
Kayed, R. et al. 2007. Mol Neurodegener. 2:18.
Kovas, G. G. et al. 2012. Acta neuropathol. 124:37-50.
Lasagna-Reeves, C. A. et al. 2012. FASEB J. 26:1946-59.
Mechetner, E. et al. 1998. Clin. Cancer Res. 4: 389-98.
Nussbaum, J. M. et al.2012. Nature 485:651-5 .
Paduch, M. et al. 2013. Methods 60:3-14.
Perchiacca, J. M. et al. 2012. Proc. Natl. Acad. Sci. U.S.A 109:84-89.
Stanker, et al. 2012. Hybridoma 31:314-324.
Upadhaya, et al.2014. Brain 137: 887-903.
Youmans, K. L.et al. 2012. Mol Neurodegener, 7: 8xx