Identification | Back Directory | [Name]
AC-GLN-LYS-LEU-VAL-PHE-PHE-NH2 | [CAS]
189064-06-0 | [Synonyms]
AC-QKLVFF ac-qklvff-nh2 amyloid blocker BETA-AMYLOID LIGAND ACETYL-BETA-AMYLOID (15-20) AC-GLN-LYS-LEU-VAL-PHE-PHE-OH AC-GLN-LYS-LEU-VAL-PHE-PHE-NH2 Acetly-β Amyloid(15-20), Amide Acetyl-Amyloid β-Protein (15-20) Ac-Amyloid β-Protein (15-20) amide AC-AMYLOID BETA-PROTEIN (15-20) AMIDE Acetyl-AMyloid b-Protein (15-20) aMide Acetyl-Amyloid β-Protein (15-20) amide AC-GLN-LYS-LEU-VAL-PHE-PHE-NH2 USP/EP/BP ACETYL-AMYLOID BETA-PROTEIN (15-20) AMIDE acetyl-amyloid B protein fragment 15-20 amide acetyl-amyloid β-protein fragment 15-20 amide AMYLOID BETA-PROTEIN ACETYL-FRAGMENT 15-20 AMIDE Acetyl-Amyloid b-Protein (15-20) amide trifluoroacetate salt Acetyl-Amyloid β-Protein (15-20) amide trifluoroacetate salt Acetyl-Amyloid beta-Protein Fragment 15-20 Amide >=97% (HPLC), powder N2-Acetyl-L-glutaminyl-L-lysyl-L-leucyl-L-valyl-L-phenylalanyl-L-phenylalaninamide L-Phenylalaninamide, N2-acetyl-L-glutaminyl-L-lysyl-L-leucyl-L-valyl-L-phenylalanyl- | [Molecular Formula]
C42H63N9O8 | [MDL Number]
MFCD17215285 | [MOL File]
189064-06-0.mol | [Molecular Weight]
822.01 |
Chemical Properties | Back Directory | [Boiling point ]
1250.0±65.0 °C(Predicted) | [density ]
1.192±0.06 g/cm3(Predicted) | [storage temp. ]
−20°C | [form ]
powder | [pka]
13.33±0.46(Predicted) | [color ]
white | [Sequence]
Ac-Gln-Lys-Leu-Val-Phe-Phe-NH2 |
Hazard Information | Back Directory | [Uses]
Acetly-β Amyloid (15-20), Amide is a peptides fragment. Acetly-β Amyloid (15-20), Amide inhibits the β-sheet formation and stabilizes structure of Aβ (1–40) peptide. Acetly-β Amyloid (15-20), Amide can be used in study Alzheimer’s disease[1]. | [Biological Activity]
Amyloid plaques characteristic of the Alzheimer brain contain fibrils composed of amyloid beta aggregates. Short peptides containing the sequence KLVFF have been shown to bind specifically to the homologous region in Aβ and are used to prevent full length amyloid fibril formation. | [References]
[1] Lin SY, et al. Fourier transform infrared spectroscopy used to evidence the prevention of beta-sheet formation of amyloid beta(1-40) peptide by a short amyloid fragment. Int J Biol Macromol. 2003 Sep;32(3-5):173-7. DOI:10.1016/s0141-8130(03)00051-5 |
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Energy Chemical
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cjbscvictory
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