SCP0036
Amyloid β 13-16 human
≥95% (HPLC)
Synonym(s):
HHQK
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1 MG
CZK 2,750.00
5 MG
CZK 9,450.00
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1 MG
CZK 2,750.00
5 MG
CZK 9,450.00
About This Item
Empirical Formula (Hill Notation):
C23H36N10O6
Molecular Weight:
548.60
UNSPSC Code:
12352200
NACRES:
NA.32
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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 Code
11 - Combustible Solids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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
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
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
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