| Identification | Back Directory | [Name]
H-ASP-ALA-GLU-PHE-ARG-HIS-ASP-SER-GLY-TYR-GLU-VAL-HIS-HIS-GLN-LYS-OH | [CAS]
131580-10-4 | [Synonyms]
β-Amyloid 1-16
DAEFRHDSGYEVHHQK
BETA-AMYLOID (1-16)
AMyloid b-Protein (1-16)
AMYLOID BETA-PROTEIN (1-16)
[Gln11] -β- Amyloid (1 - 16)
Amyloidβ-Protein(1-16)/β-Amyloid(1-16),human
Amyloid beta-Protein (1-16) trifluoroacetate salt
H-ASP-ALA-GLU-PHE-ARG-HIS-ASP-SER-GLY-TYR-GLU-VAL-HIS-HIS-GLN-LYS-OH
H-ASP-ALA-GLU-PHE-ARG-HIS-ASP-SER-GLY-TYR-GLU-VAL-HIS-HIS-GLN-LYS-OH USP/EP/BP
L-Lysine, L-α-aspartyl-L-alanyl-L-α-glutamyl-L-phenylalanyl-L-arginyl-L-histidyl-L-α-aspartyl-L-serylglycyl-L-tyrosyl-L-α-glutamyl-L-valyl-L-histidyl-L-histidyl-L-glutaminyl- | [Molecular Formula]
C84H119N27O28 | [MDL Number]
MFCD00214592 | [MOL File]
131580-10-4.mol | [Molecular Weight]
1955.01 |
| Chemical Properties | Back Directory | [density ]
1.57±0.1 g/cm3(Predicted) | [storage temp. ]
-15°C | [solubility ]
Soluble in DMSO | [form ]
Solid | [color ]
White to off-white | [Water Solubility ]
Soluble in water or aqueous buffer | [Sequence]
H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-OH |
| Hazard Information | Back Directory | [Uses]
Aβ(s) peptides, their peptide fragments and mutated fragments are used to study a wide range of metabolic and regulatory functions including activation of kinases, regulation of cholesterol transport, function as a transcription factor, and regulators of inflammation. Aβ(s) peptides and their peptide fragments are also used to study oxidative stress, metal binding and mechanisms of protein cross-linking in the context of diseases such as Alzheimer?s disease and neurodegeneration. | [in vivo]
β-amyloid (1-16) fragment is considered as valid models to examine the contribution of the key histidine residues (His , His in mouse and His , His , His in human fragments) to the Ab–Cu2+ interaction. Oxidation targets for β-Amyloid (1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aβ in senile plaque of Alzheimer’s disease with β-Amyloid (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of -Amyloid and free radical damage[1]. β-amyloid (1-16) is the minimal amino acidic sequence display a Cu coordination mode which involves three Histidines (His6, His13 and His14). β-amyloid (1-16) is supposed to be involved in metal binding[2]. Human β-amyloid interacts with zinc ions through its metal-binding domain 1-16. The C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat β-Amyloid (1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease[3]. | [storage]
Store at -20°C |
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