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Merck
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Documentos clave

SCP0036

Sigma-Aldrich

Amyloid β 13-16 human

≥95% (HPLC)

Sinónimos:

HHQK

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About This Item

Fórmula empírica (notación de Hill):
C23H36N10O6
Peso molecular:
548.60
UNSPSC Code:
12352200
NACRES:
NA.32

assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥45%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

His-His-Gln-Lys

Application

Amyloid β (Aβ) refers to peptides derived from Amyloid precursor protein that vary in length from 36-43 amino acids. 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. HHQK is a studied as a unique target site for inhibition of amyloid fibril formation and proteoglycan binding.

Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
BD0248

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D Giulian et al.
The Journal of biological chemistry, 273(45), 29719-29726 (1998-10-29)
The beta-amyloid peptide 1-42 (Abeta1-42), a major component of neuritic and core plaques found in Alzheimer's disease, activates microglia to kill neurons. Selective modifications of amino acids near the N terminus of Abeta showed that residues 13-16, the HHQK domain
J McLaurin et al.
European journal of biochemistry, 267(21), 6353-6361 (2000-10-13)
One of the major clinical features of Alzheimer's disease is the presence of extracellular amyloid plaques that are associated with glycosaminoglycan-containing proteoglycans. It has been proposed that proteoglycans and glycosaminoglycans facilitate amyloid fibril formation and/or stabilize these aggregates. Characterization of
Toshio Ariga et al.
Journal of neuroscience research, 88(11), 2303-2315 (2010-07-14)
The extracellular accumulation of amyloid beta proteins (Abetas) in neuritic plaques is one of the hallmarks of Alzheimer's disease (AD). The binding of Abetas to extracellular membranes (ECMs) is a critical step in developing AD. Abetas bind to many biomolecules

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