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. MilliporeSigma provides antibodies to identify particular conformational states or protein-protein interactions.
Journal and Article Publications
Alzheimer's Disease Related
| Target | Specificity | Method | Catalog 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
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