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Fluorescent Dyes  >  Fluorescent Biopolymers  >>  Beta-Amyloid (1-42), HiLyte™ Fluor 488-labeled, Human
Product Name Beta - Amyloid (1 - 42), HiLyte™ Fluor 488 - labeled, Human
HiLyte™ Fluor 488 - DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Size 0.1 mg
Catalog # AS-60479-01
US$ $237
Purity % Peak Area By HPLC ≥ 95%
Description

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).

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), HiLyte™ Fluor 488-labeled, Human
Detailed Information Datasheet
Material Safety Data Sheets (MSDS)
Brochure
Storage -20°C
Molecular Weight 4870.5
Sequence
(One-Letter Code)		 HiLyte™ Fluor 488-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Sequence
(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 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.
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.
Halle, A. et al. (2008). The NALP3 inflammasome is involved in the innate immune response to amyloid-bold beta. Nature Immunol 9, 857.
Hickman, S. et all (2008). Microglial dysfunction and defective β-amyloid clearance pathways in aging Alzheimer's Disease mice. J. Neurosci. 28, 8354.
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. Neurobio. Dis. 30, 94.
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.
Widenbrant, M. J. O. et al. (2006). Lipid-Induced β-Amyloid Peptide Assemblage Fragmentati. Biophys. J. 91, 4071.
     
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