Beta-Amyloid (1-42), HFIP

Name: Beta-Amyloid (1-42), HFIP
SKU: A-1163-1
Price: 200.00 USD
Availability: InStock

Product background: Beta-Amyloid peptides (A-beta), the major constituent of amyloid plaques in the brains of Alzheimer’s patients, is thought to be a primary contributor of Alzheimer’s Disease (AD).

About the product: Expressed recombinantly in E. coli, Beta-Amyloid (1-42) is purified to our highest standards to ensure batch to batch consistency in both purity and quality. This product if treated with HFIP (hexofluoro-isopropanol) and then dried, leaving a clear dry film, rather than a lyophilized powder.

Applications: The HFIP counter ion of our Aβ ensures a highly monomeric starting material that could be suited to aggregation studies, seeding experiments, molecular standards, and more.

Catalog ID: A-1163-1

$200.00

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Product Details
- Size: 0.5 mg
- Physical State: Clear, dry film
- Temperature Storage: -20°C
- Temperature Shipping: Ambient
- Sequence:
  D A E F R H D S G Y E V H H Q K L V F F A E D V G S N K G A I I G L M V G G V V I A
- Source: Recombinant. A DNA sequence encoding the human beta-amyloid (1-42) sequence was expressed in E. coli
- Purity: >97% by Mass Spec.
- Molecular Mass: 4,514 Da theoretical
References

1. Yankner, B., et al., (1990) Science, 250 : 279-282
2. Stine, W., et al., (2003) J. Biol. Chem, 278 : 11612-11622
3. Frank, R., et al., (2003) Neurobiology of Aging, 24 : 521-536
4. Novo, M., Freire, S. & Al-Soufi, W., (2018) Sci Rep 8 : 1783
Publications

Reverse engineering synthetic antiviral amyloids.

Nature Communications; doi.org/10.1038/s41467-020-16721-8.

Michiels, E., Roose, K., Gallardo, R. et al.

Dityrosine cross-link trapping of amyloid-β intermediates reveals that self-assembly is required for Aβ-induced cytotoxicity.

bioRxiv; www.biorxiv.org/content/10.1101/2020.03.25.007690v1.full.

Maina, M., Mengham, K., Burra, G., Al-Hilaly,Y., Serpell, L.

The monomers, oligomers, and fibrils of amyloid-β inhibit the activity of mitoBKCa channels by a membrane-mediated mechanism.

Biochimica et Biophysica Acta (BBA); Biomembranes; doi.org/10.1016/j.bbamem.2020.183337..

Kravenska, Y.,Nieznanska, H., Nieznanski, K., Lukyanetz, E., Szewczyk, A., Koprowski, P.

Small molecule modulation of the p75 neurotrophin receptor inhibits multiple amyloid beta-induced tau pathologies.

Scientific Reports; doi.org/10.1038/s41598-020-77210-y.

Yang, T., Tran, K., Zeng, A., Massa, S., Longo, F.

The monomers, oligomers, and fibrils of amyloid-β inhibit the activity of mitoBKCa channels by a membrane-mediated mechanism.

BBA; doi.org/10.1016/j.bbamem.2020.183337.

Kravenska,Y., Nieznanska,H., Nieznanski,K., Lukyanetz,E., Szewczyk,A., Koprowski,P.,

First amyloid β1‐42 certified reference material for re‐calibrating commercial immunoassays.

Alzheimer’s Association; doi.org/10.1002/alz.12145.

Boulo,S., Kuhlmann,J., Andreasson,U., Venkataraman,I., Herbst,V., Rutz,S., Manuilova,E., Vandijck,M., Dekeyser,F., Bjerke,M., Pannee,J., Charoud-Got,J., Auclair,G., Mazoua,S., Pinski,G., Trapmann,S., Schimmel,H., Emons, H., Quaglia,M., Portelius,E., Korecka, M., Shaw,L., Lame,M., Chambers, E., Vanderstichele,H., Stoops, E., Leinenbach, A., Bittner,T., Jenkins,R., Kostanjevecki,V., Lewczuk,P., Gobom,J., Zetterberg,H., Zegers,I., Blennow,K.

Amyloid-beta impairs insulin signaling by accelerating autophagy-lysosomal degradation of LRP-1 and IR-β in blood-brain barrier endothelial cells in vitro and in 3XTg-AD mice

Molecular and Cellular Neuroscience; https://doi.org/10.1016/j.mcn.2019.103390.

Chaitanya Chakravarthi Gali, Elham Fanaee-Danesh, Martina Zandl-Lang

Misfolded amyloid β-42 induced impairment of the endosomal-lysosomal pathway revealed by real-time optical monitoring

bioRxiv; https://doi.org/10.1101/598540.

Karen E Marshall, Devkee Vadukul, Kevin Staras, Louise C Serpell

Stem cell derived human microglia transplanted in mouse brain to study genetic risk of Alzheimer’s Disease

bioRxiv; http://dx.doi.org/10.1101/562561.

Renzo Mancuso, Johanna Van Den Daele, Nicola Fattorelli, Leen Wolfs, Sriram Balusu, Oliver Burton,..Bart De Strooper

Molecular rotors report on changes in live cell plasma membrane microviscosity upon interaction with beta-amyloid aggregates

Soft Matter; DOI: 10.1039/c8sm01633j.

Markéta Kubánková, Ismael López-Duarte, Darya Kiryushko, Marina K. Kuimova

Ginkgo biloba L. (Ginkgoaceae) Leaf Extract Medications From Different Providers Exhibit Differential Functional Effects on Mouse Frontal Cortex Neuronal Networks.

www.ncbi.nlm.nih.gov; doi: 10.3389/fphar.2018.00848.

Bader, B., Jügelt,K., Schultz,L., Schroeder, O.H.

Inhibition of Poly(ADP-ribose) Polymerase-1 Enhances Gene Expression of Selected Sirtuins and APP Cleaving Enzymes in Amyloid Beta Cytotoxicity.

link.springer.com; https://doi.org/10.1007/s12035-017-0646-8.

Wencel, P.L., Lukiw, W.J., Strosznajder, J.B., Strosznajder, R.P

Counteracting the effects of TNF receptor‐1 has therapeutic potential in Alzheimer’s disease

Wiley Online Library; |https://doi.org/10.15252/emmm.201708300.

Sophie Steeland , Nina Gorlé , Charysse Vandendriessche , Sriram Balusu , Marjana Brkic , Caroline Van Cauwenberghe , Griet Van Imschoot , Elien Van Wonterghem , Riet De Rycke , Anneke Kremer , Saskia Lippens , Edward Stopa , Conrad E Johanson , Claude Libert , Roosmarijn E Vandenbroucke

Inhibition of poly(ADP-ribose) polymerase-1 alters expression of mitochondria-related genes in PC12 cells: relevance to mitochondrial homeostasis in neurodegenerative disorders.

Science Direct; https://doi.org/10.1016/j.bbamcr.2017.11.003.

Czapski,G.A., Cieślik,M., Wencel,P.L., Wójtowicz,S., Strosznajder,R.P., Strosznajder, J.B.

RAD52 is required for RNA-templated recombination repair in post-mitotic neurons.

JBC; doi: 10.1074/jbc.M117.808402.

Welty, S., Teng, Y., Liang,Z., Zhao,W., Sanders,L.H.,…Lan,L

Amelioration of amyloid-β-induced deficits by DcR3 in an Alzheimer’s disease model.

BioMed Central; 10.1186/s13024-017-0173-0.

Yi-Ling Liu, Wei-Ting Chen, Yu-Yi Lin, Po-Hung Lu, Shie-Liang Hsieh and Irene Han-Juo Cheng

Application of quinazoline and pyrido[3,2-d]pyrimidine templates to design multi-targeting agents in Alzheimer’s disease.

RSC Advances; DOI: 10.1039/C7RA02889J.

Tarek Mohamed, Mandeep K. Mann, Praveen P. N. Rao

Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid‐β 1‐42.

FEBS PRESS; https://doi.org/10.1002/1873-3468.12590.

Devkee M. Vadukul , Oyinkansola Gbajumo , Karen E. Marshall , Louise C. Serpell

Synthesis and evaluation of benzothiazole-triazole and benzothiadiazole-triazole scaffolds as potential molecular probes for amyloid-β aggregation.

New Journal of Chemistry; DOI: 10.1039/C6NJ01703G.

Christine Dyrager, Rafael Pinto Vieira, Sofie Nyström, K. Peter R. Nilsson, Tim Storr

FcγRIIb-SHIP2 axis links Aβ to tau pathology by disrupting phosphoinositide metabolism in Alzheimer’s disease model

eLife 2016;5:e18691; http://dx.doi.org/10.7554/eLife.18691.

Tae-In Kam, Hyejin Park, Youngdae Gwon, Sungmin Song, Seo-Hyun Kim, Seo Won Moon, Dong-Gyu Jo, Yong-Keun Jung

The Alzheimer’s-related amyloid beta peptide is internalised by R28 neuroretinal cells and disrupts the microtubule associated protein 2 (MAP-2)

Science Direct; http://dx.doi.org/10.1016/j.exer.2016.10.013.

George Taylor-Walkera, Savannah A. Lynna, Eloise Keelinga, Rosie Mundaya, David A. Johnstonb, Anton Pageb, Jennifer A. Scotta, Srini Goverdhana, Andrew J. Loterya, c, J. Arjuna Ratnayakaa,

Effect of IVIG Formulation on IgG Binding to Self- and Exo- Antigens In Vitro and In Vivo

PLOS ONE; http://dx.doi.org/10.1371/journal.pone.0161826.

Susann Cattepoel ,Annette Gaida,Alain Kropf, Marc W. Nolte,Reinhard Bolli,Sylvia M. Miescher

Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased Aβ generation in Alzheimer’s disease.

Acta Neuropathologica; doi: 10.1007/s00401-016-1558-9.

Katherine R. Sadleir, Patty C. Kandalepas, Virginie Buggia-Prévot, Daniel A. Nicholson, opal Thinakaran, Robert Vassar

Technical performance of a novel, fully automated electrochemiluminescence immunoassay for the quantitation of β-amyloid (1–42) in human cerebrospinal fluid.

Alzheimer’s & Dementia; doi: 10.1016/j.jalz.2015.09.009..

Tobias Bittner, Henrik Zetterberg, Charlotte E.Teunissen, Richard E.Ostlund Jr, Christina Rabe, Kaj Blennow

Inhibition of Aβ42 oligomerization in yeast by a PICALM ortholog and certain FDA approved drugs

Microbial Cell; doi: 10.15698/mic2016.02.476.

Sei-Kyoung Park, Kiira Ratia, Mariam Ba, Maria Valencik, and Susan W. Liebman

Lysosomal Enzyme Glucocerebrosidase Protects against A[Beta]1-42 Oligomer-Induced Neurotoxicity: e0143854.

Plos One; doi:10.1371/journal.pone.0143854.

Choi, Seulah; Kim, Donghoon; Kam, Tae-In; Yun, Seungpil; Kim, Sangjune

Protective properties of lysozyme on β-amyloid pathology: implications for Alzheimer disease.

Science Direct; doi:10.1016/j.nbd.2015.08.024.

Linda Helmfors, Andrea Bomanb, Livia Civitelli, Sangeeta Nath, Linnea Sandin, Camilla Janefjord, Heather McCann, Henrik Zetterberg, Kaj Blennow, Glenda Halliday, Ann-Christin Brorsson, Katarina Kågedal

The Transient Receptor Potential Melastatin 2 (TRPM2) Channel Contributes to β-Amyloid Oligomer-Related Neurotoxicity and Memory Impairment.

The Journal of Neuroscience; doi: 10.1523/JNEUROSCI.4081-14.2015.

Valeriy G. Ostapchenko, Megan Chen, Monica S. Guzman, Yu-Feng Xie, Natalie Lavine, Jue Fan, Flavio H. Beraldo, Amanda C. Martyn, Jillian C. Belrose, Yasuo Mori, John F. MacDonald, Vania F. Prado, Marco A.M. Prado, and Michael F. Jackson

Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation.

Science Direct; doi:10.1016/j.febslet.2015.09.027.

Thomas L. Williamsa, Brigita Urbanc, Karen E. Marshall, Devkee M. Vadukul, A. Toby A. Jenkins, Louise C. Serpell

Analyzing and Modeling the Kinetics of Amyloid Beta Pores Associated with Alzheimer’s Disease Pathology.

PLOS One; DOI: 10.1371/journal.pone.0137357.

Ghanim Ullah, Angelo Demuro, Ian Parker, John E. Pearson

Effect of methionine-35 oxidation on the aggregation of amyloid-β peptide.

ScienceDirect; doi:10.1016/j.bbrep.2015.07.017.

Merlin Friedemann, Eneken Helk, Ann Tiiman, Kairit Zovo, Peep Palumaa, Vello Tõugu

The Molecular Mechanism of Amyloid β42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins.

PLOS One; DOI: 10.1371/journal.pone.0137193.

Magdalena Cieślik, Grzegorz A. Czapski, Joanna B. Strosznajder

Time dynamics of photothermal vs optoacoustic response in mid IR nanoscale biospectroscopy.

Cornell University Library; http://arxiv.org/abs/1509.00726v1.

Peter D. Tovee, Claire Tinker-Mill, Kevin Kjoller, David Allsop, Peter Weightman, Mark Surman, Michele R. F. Siggel-King, Andy Wolski, Oleg V. Kolosov

Development of Immunoassays for the Quantitative Assessment of Amyloid-β in the Presence of Therapeutic Antibody: Application to Pre-Clinical Studies.

ISO Press; DOI: 10.3233/JAD-142988.

Bogstedt, Anna Groves, Maria Tan, Keith Narwal, Rajesh McFarlane, Mary Höglund, Kina

Development of Immunoassays for the Quantitative Assessment of Amyloid-β in the Presence of Therapeutic Antibody: Application to Pre-Clinical Studies.

IOS Press; DOI: 10.3233/JAD-142988.

Bogstedt, Anna; Groves, Maria; Tan, Keith; Narwal, Rajesh; McFarlane, Mary; Höglund, Kina

NLRP3 Inflammasome Is Expressed and Functional in Mouse Brain Microglia but Not in Astrocytes.

PLOS ONE; DOI: 10.1371/journal.pone.0130624.

Audrey Gustin, Mélanie Kirchmeyer, Eric Koncina, Paul Felten, Sophie Losciuto, Tony Heurtaux, Aubry Tardivel, Paul Heuschling, Catherine Dostert

Reciprocal modulation of Aβ42 aggregation by copper and homocysteine.

Front Aging Neurosci.; https://doi.org/10.3389/fnagi.2014.00237.

Salla Keskitalo, Melinda Farkas, Michael Hanenberg, Anita Szodorai, Luka Kulic, Alexander Semmler, Michael Weller, Roger M. Nitsch, Michael Linnebank

Suppression of Alzheimer-Associated Inflammation by Microglial Prostaglandin-E2 EP4 Receptor Signaling

The Journal of Neuroscience; doi: 10.1523/JNEUROSCI.0410-14.2014.

Nathaniel S. Woodling, Qian Wang, Prachi G. Priyam, Paul Larkin, Ju Shi, Jenny U. Johansson, Irene Zagol-Ikapitte, Olivier Boutaud, and Katrin I. Andreasson

Microglial derived tumor necrosis factor-α drives Alzheimer’s disease-related neuronal cell cycle events

Neurobiol Dis.; doi: 10.1016/j.nbd.2013.10.007.

Kiran Bhaskar, Nicole Maphis, Guixiang Xu, Nicholas H. Varvel, Olga N.Kokiko-Cochran, Jason P.Weick, Susan M. Staugaitis, Astrid Cardona, Richard M.Ransohoff, Karl Herrup, Bruce T. Lamb

Ultrasonic force microscopy for nanomechanical characterization of early and late-stage amyloid-β peptide aggregation

Scientific Reports; doi:10.1038/srep04004.

Claire Tinker-Mill, Jennifer Mayes, David Allsop, & Oleg V. Kolosov

Development and assessment of sensitive immuno‐PCR assays for the quantification of cerebrospinal fluid three‐ and four‐repeat tau isoforms in tauopathies.

Journal of Neurochemistry; https://doi.org/10.1111/j.1471-4159.2012.07911.x.

Connie Luk, Yaroslau Compta, Nadia Magdalinou, Maria José Martí, Geshanthi Hondhamuni, Henrik Zetterberg, Kaj Blennow, Radu Constantinescu, Yolande Pijnenburg

Beta-Amyloid (1-42), HFIP

Product Details

References

Publications

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