
Amyloid β-Protein 10-20
CAS No. 152286-31-2
Amyloid β-Protein 10-20( —— )
Catalog No. M30484 CAS No. 152286-31-2
Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.
Purity : >98% (HPLC)






Size | Price / USD | Stock | Quantity |
5MG | 206 | Get Quote |
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10MG | 356 | Get Quote |
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100MG | Get Quote | Get Quote |
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200MG | Get Quote | Get Quote |
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500MG | Get Quote | Get Quote |
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Biological Information
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Product NameAmyloid β-Protein 10-20
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NoteResearch use only, not for human use.
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Brief DescriptionAmyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.
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DescriptionAmyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.(In Vitro):Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide.
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In Vitroβ-Amyloid (10-20) is a fragment of Amyloid-β peptide.
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In Vivo——
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Synonyms——
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PathwayMembrane Transporter/Ion Channel
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TargetBeta Amyloid
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RecptorAmyloid-β
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Research Area——
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Indication——
Chemical Information
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CAS Number152286-31-2
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Formula Weight1446.65
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Molecular FormulaC71H99N17O16
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Purity>98% (HPLC)
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Solubility——
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SMILES——
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Chemical NameSequence:Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe
Shipping & Storage Information
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Storage(-20℃)
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ShippingWith Ice Pack
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Stability≥ 2 years
Reference
Peró-Gascón R, et al. Determination of acidity constants and prediction of electrophoretic separation of amyloid beta peptides. J Chromatogr A. 2017 Jul 28;1508:148-157.
molnova catalog



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