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Fluorescent Dyes > Fluorescent Biopolymers >> Beta-Amyloid (1-40)

Product Name	Beta - Amyloid (1 - 40)
Size	1 mg
Catalog #	24236
US$	$220
Purity	% Peak Area By HPLC ≥ 95%
Description	Aß (1-40) together with Aß (1-42) are two major C-terminal variants of the Aß protein constituting the majority of Aßs. These undergo post-secretory aggregation and deposition in the Alzheimer’s disease brain. Electron microscopy of b-amyloid (1-40) stained with Thioflavin T (data generated by an AnaSpec scientist).
Detailed Information	Datasheet Material Safety Data Sheets (MSDS) Brochure
Storage	-20°C
References	Ref: Masters, CL. et al. Proc. Natl. Acad. Sci. USA 82, 4245 (1985); Yankner, BA. Neuron 16, 921 (1996); Geula, C. et al. Nat. Med. 4, 827 (1998); Shin, R. et al. J. Neurosci.17, 8187 (1997).
Molecular Weight	4329.9
Sequence (One-Letter Code)	DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV
Sequence (Three-Letter Code)	H - 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 - OH
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A screening UHPLC–MS/MS method for the analysis of amyloid peptides in cerebrospinal fluid of preclinical species. Bioanalysis 3, 45. Li, W. et al. (2011). Regulation of matrix metalloproteinase 2 by oligomeric amyloid β protein. Brain Res 10.1016/j.brainres.2011.02.078. Libeu, CP. et al. (2011). Structural and functional alterations in amyloid-β precursor protein induced by amyloid-β peptides. J Alzheimer's Dis 25, 547. Soto-Ortega, D. et al. (2011). Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center. Bioorg Med Chem 19, 25996. Vivekanandan, S. et al. (2011). A partially folded structure of amyloid-beta(1-40) in an aqueous environment. Biochem Biophys Res Commun 10.1016/j.bbrc.2011.06.133. Hoi, C. et al. (2010). Neuroprotective effect of honokiol and magnolol, compounds from Magnolia officinalis, on beta-amyloid-induced toxicity in PC12 cells. Phytother Res10.1002/ptr.3178. Keshet, B. et al. (2010). Can size alone explain some of the differences in toxicity between -amyloid oligomers and fibrils? Biotech Bioengineer 106, 333. Ravindran, C. et al. (2010). CpG-ODNs induces up-regulated expression of chemokine CCL9 in mouse macrophages and microglia. Cell Immunol 260, 113. Reza, M. et al. (2010). Microchip electrophoresis profiling of Aβ peptides in the cerebrospinal fluid of patients with Alzheimer’s disease. Anal Chem 82, 7611. Vargas, T. et al. (2010). Gelsolin restures Aβ-induced alterations in choroid plexus epithelium. J Biomed Biotech 10.1155/2010/805405. Daivs, TJ. et al. (2009). Comparative study of inhibition at multiple stages of amyloid-β self-assembly provides mechanisitic insight. Mol Pharmacol 76, 405. Lin, MS. et al. (2009). Dynamic fluorescence imaging analysis to investigate the cholesterol recruitment in lipid monolayer during the interaction between β-amyloid (1–40) and lipid monolayers. Colloids Surf B 74, 59. Liu, L. et al. (2009). Differential modification of Cys10 alters transthyretin's effect on beta-amyloid aggregation and toxicity. PEDS 10.1093/protein/gzp025. Muresan, V. et al. (2009). The cleavage products of amyloid-β precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites. J Neuro Sci 29, 3565. Andras, IE. et al. (2008). Simvastatin protects against amyloid β and HIV-1 tat-induced promoter activities of inflammatory genes in brain endothelial cells. Mol Pharmacol 73, 1424. Ho, C. et al. (2008). Bio-assay guided isolation and identification of anti-Alzheimer active compounds from the root of Angelica sinensis. Food Chem 114, 246. Kukar, TL. et al. (2008). Substrate-targeting γ-secretase modulators. Nature 453, 925. Minicozzi, V. et al. (2008). Identifying the minimal copper- and zinc-binding site sequence in amyloid-β peptides. J Biol Chem 283, 10784. Shimojo, M. et al. (2008). Enzymatic characteristics of I213T mutant presenilin-1/ γ-secretase in cell modles and knock-in mouse brains. J Biol Chem 283, 16488. Cho, S. et al. (2007). Activation of 5-HT4 receptors inhibits secretion of β peptides and increase neuronal survival. Exp Neurol 203, 274. Gonzales-Velasquez, FJ. et al. (2008). Soluble aggregates of the amyloid-β protein activate endothelial monolayers for adhesion and subsequent transmigration of monocyte cells. J Neurochem 104, 500. Lee, S. et al. (2007). Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway. Protein Sci 16, 723. Guo, JP. et al. (2006). Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease. PNAS 103, 1953. Jacobsen, JS. et al. (2006). Early-onset behavioral and synaptic deficits in a mouse model of Alzheimer's disease. PNAS 103, 5161. Carrotta, R. et al. (2005). Protofibril formation of amyloid &$946;-protein at low pH via a non-cooperative elongation mechanism. J Biol Chem 280, 30001. Edwin, J. et al. (2005). Elucidating the kinetics of β-amyloid fibril formation. New Polymeric Mater 10.1021/bk-2005-0916.ch009. Inaba, S. et al. (2005). Specific binding of amyloid-β-protein to IMR-32 neuroblastoma cell membrane. J Pept Res 65, 485. Osada, Y. et al. (2004). CLAC binds to amyloid β peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrils. J Biol Chem 280, 8596. Sun, Z. et al. (2005) Cholesterol depletion inhibits the degradation of amyloid β-peptide in rat pheochromocytoma (PC12) cells. Neurosci Lett 391, 71. Kim, JR. et al. (2003). Targeted control of kinetics of β-amyloid self-association by surface tension-modifying peptides. J Biol Chem 278, 40730. Ege, C. et al. (2004). Insertion of Alzheimer's Aβ40 peptide into lipid monolayers. Biophys J 87, 1732. Boros, S. et al. (2004). Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β. FEBS Lett 576, 57. Cottingham, MG. et al. (2004). Rapid method for measurement of surface tension in multiwell plates. Lab Invest 84, 523. Watanabe, N. et al. (2004). Glypican-1 as an Aβ binding HSPG in the human brain: Its localization in DIG domains and possible roles in the pathogenesis of Alzheimer’s disease. FASEB J 10.1096/fj.03-1040fje. Kim, JR. et al. (2003). Targeted control of kinetics of β-amyloid self-association by surface tension-modifying peptides. J Biol Chem 278, 40730. Zou, P. et al. (2003). Humanin peptides block calcium influx of rat hippocampal neurons by altering fibrogenesis of Aβ1–40. Pept 24, 679. Ji, SR. et al. (2001). Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation. J Biol Chem 277, 6273. Nakagami, Y. et al. (2002). A novel compound RS-0466 reverse β-amyloid-induced cytotoxcity through the Akt signaling pathway in vitro. Eur J Pharmacol 457, 11. Kajkowski, EM. et al. (2001). β-amyloid peptide-induced apoptosis regulated by a novel protein containing a G protein activation module. J Biol Chem 276, 18748. Klegeris, A. et al. (2001). Inflammatory cytokine levels are influenced by interactions between THP-1 monocytic, U-373 MG astrocytic, and SH-SY5Y neuronal cell lines of human origin. Neurosci Lett 313, 41. Lowe, T. et al. (2001). Structure−function relationships for inhibitors of β-amyloid toxicity containing the recognition sequence KLVFF. Biochem 40, 7882. Pallitto, MM. et al. (2001). A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state. Biophys J 81, 1805. Liang, JJN. (2000). Interaction bewteen β-amyloid and lens αB-crystallin. FEBS Lett 484, 98. Satoh, K. et al. (2000). Expression of prostaglandin E synthase mRNA is induced in beta-amyloid treated rat astrocytes. Neurosci Lett 283, 221. Stege, GJJ. et al. (1999). The molecular chaperone αB-crystallin enhanes amyloid β neurotoxicity. Biochem Biophy Res Commun 262, 152. Bradt, BM. et al. (1998). Complement-dependent proinflammatory properites of the Alzheimer's disease β-peptide. J Exp Med 188, 431.

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