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Fluorescent Dyes  >  Fluorescent Biopolymers  >>  Beta-Amyloid (1-42), HiLyteᵀᴹ Fluor 488-labeled, Human

Product Name Beta - Amyloid (1 - 42), HiLyteᵀᴹ Fluor 488 - labeled, Human
Size 0.1 mg
Catalog # AS-60479-01
US$ $249
Purity % Peak Area By HPLC ≥ 95%

This is a fluorescent (HiLyte™ Fluor 488)-labeled ß-Amyloid peptide, Abs/Em=503/528 nm. Hilyte 488™ Fluor labeled Aß (1-42) has a brighter intensity than FAM-labeled Aß (1-42).

Solvent Information

Fgure 1. Absoprtion and emission spectra of HiLyte™ Fluor 488 labeled β-Amyloid (1-42).

Figure 2. Staining pattern of HiLyte™ Fluor 488 labeled Aβ (1-42) peptide on an AD (A) and a normal brain (B). Images courtesy of Dr. Jian-Ping Guo in Dr. Patrick L. McGeer’s lab, University of British Columbia, Vancouver, Canada.

Images Beta-Amyloid (1-42), HiLyteᵀᴹ  Fluor 488-labeled, Human
Detailed Information Datasheet
Material Safety Data Sheets (MSDS)
Storage -20°C
Molecular Weight 4870.5
(One-Letter Code)
(Three-Letter Code)
Hilyte™ Fluor488 - Asp - Ala - Glu - Phe - Arg - His - Asp - Ser - Gly - Tyr - Glu - Val - His - His - Gln - Lys - Leu - Val - Phe - Phe - Ala - Glu - Asp - Val - Gly - Ser - Asn - Lys - Gly - Ala - Ile - Ile - Gly - Leu - Met - Val - Gly - Gly - Val - Val - Ile - Ala - OH
Product Citations Xiang, X. et al. (2016). TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance. EMBO Mol Med 8:992-1004. https://doi.org/10.15252/emmm.201606370

Minogue, A. et al. (2015). Bone marrow-derived macrophages from AβPP/PS1 mice are sensitized to the effects of inflammatory stimuli. J Alz Dis 44, 949. doi: 10.3233/JAD-142076.

Esbjörner, EK. et al. (2014). Direct observations of Amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ (1–40) and Aβ (1–42) aggregation. Chemistry Biol 21, 732. doi:10.1016/j.chembiol.2014.03.014.

Mittag, JJ. et al. (2014). Simultaneous measurement of a range of particle sizes during Aβ < sub> 1–42 fibrillogenesis quantified using fluorescence correlation spectroscopy. Biochem Biophys Res Commun 448, 195. doi: 10.1016/j.bbrc.2014.04.088.

Li, W. et al. (2013). Autophagy is involved in oligodendroglial precursor-mediated clearance of amyloid peptide. Mol Neurodegener 8, 27.

Zhu, L. et al. (2013). Reduction of synaptojanin 1 accelerates Aβ clearance and attenuates cognitive deterioration in an Alzheimer mouse model. J Biol Chem 288, 32050. doi: 10.1074/jbc.M113.504365.

Le Droumaguet, B. et al. (2011). Selegiline-functionalized, PEGylated poly(alkyl cyanoacrylate) nanoparticles: Investigation of interaction with amyloid-β peptide and surface reorganization. Int J Pharm doi:10.1016/j.ijpharm.2011.01.015.

Chakrabarty, P. et al. (2010). Massive gliosis induced by interleukin-6 suppresses Aβ deposition in vivo: evidence against inflammation as a driving force for amyloid deposition. FASEB J 24, 548. doi: 10.1096/fj.09-141754.

Halle, A. et al. (2008). The NALP3 inflammasome is involved in the innate immune response to amyloid-β. Nature Immunol 9, 857. doi: 10.1038/ni.1636.

Hickman, S. et all (2008). Microglial dysfunction and defective β-amyloid clearance pathways in aging Alzheimer's Disease mice. J. Neurosci. 28, 8354. doi: 10.1523/JNEUROSCI.0616-08.2008.

Nazer, B. et al. (2008). LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-β peptide in a blood–brain barrier in vitro model. Neurobiol Dis 30, 94. doi: 10.1016/j.nbd.2007.12.005.

Vestergaard, M. et al. (2008). Detection of Alzheimer’s amyloid beta aggregation by capturing molecular trails of individual assemblies. Biochem. Biophys. Res. Comm. 377, 725. doi: 10.1016/j.bbrc.2008.10.072.

Widenbrant, MJO. et al. (2006). Lipid-Induced β-Amyloid Peptide Assemblage Fragmentati. Biophys. J. 91, 4071. doi: 10.1529/biophysj.106.085944.
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