Neuroscience

beta-Amyloid (1-11) DAEFRHDSGYE

Product number: EP10014_1

€105.00*

Prices excl. VAT plus shipping costs

Available, delivery time: 3 weeks

sterile and endotoxin free

Delivery Format: The product is supplied freeze dried.

Purity: 95% HPLC-MS

Caution: For research use only. Not for use in humans.

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Description

The beta-Amyloid 1-11 peptide with the amino acid sequence DAEFRHDSGYE is a linear peptidic epitope (epitope ID 104443) studied as part of several isoforms of Amyloid-beta precursor protein (APP) from Homo sapiens:

Isoform APP751 (UniProt:P05067-8)
Isoform L-APP752 (UniProt:P05067-9)
Isoform L-APP696 (UniProt:P05067-5) and
Isoform L-APP677 (UniProt:P05067-3).

Anionic interaction of Aß 1-11 with Factor XII is suspected to cause the massive activation of the C4 (Complement 4) system in cerebrospinal fluid of Alzheimer's disease patients.

DAEFRHDSGYE has been studied for immune reactivity and has been tested in T cell assays and B cell assays.

TechData

Sequence:	DAEFRHDSGYE
Gene:	APP
Delivery:	3 weeks
C-Terminus:	OH
N-Terminus:	H
Amount:	1 mg
Counterion:	TFA
Protein:	Amyloid-beta precursor protein
UniProt Id:	P05067
Species:	Human
Application:	ELISPOT, Flow Cytometry, Western Blotting
Indication:	Neuroscience
Purity:	95% HPLC-MS

Documents

Storage and handling of peptides

Probing of membranes with HRP

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[beta]-Amyloid (1-15)

Aβ (1-15) was used in a study investigating the presence of conformational epitope/s (mimotope/s) on fibrillar amyloid β-protein (1-42). The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors.

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[beta]-Amyloid (1-16)

The Cu²⁺ complex of this soluble amyloid β-protein fragment showed significant oxidative activities toward the catechol-like substrate 1,2,3-trihydroxylbenzene (pyrogallol) and plasmid DNA cleavage. The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors. Proteins interactions with reactive oxygen agents may result in covalent modifications of amino acid residues in proteins, formation of protein-protein cross-linkages and oxidation of the protein backbone resulting in protein fragmentation. Oxidation targets for Aß(1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aß in senile plaque of Alzheimer’s disease with Aß (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of Aß and free radical damage.

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[beta]-Amyloid (1-28)

The three-dimensional solution structure of Aß (1-28) reveals the folding of the peptide to form a predominantly a-helical structure with a bend centered at residue 12 and the side chains of histidine-13 and lysine-16 in close proximity, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. Aß (1-28) is highly hydrophilic and shares sequences with bA4, the major component of Aß. Its assembly is fibrillar, i.e., elongated in a single direction. Reports show that synthetic peptides Aß (1-40) and Aß (1-28) have significant effects on normal human plasma cholesterol esterification rate. Both peptides (at concentration of 1 ng/mL) inhibit plasma cholesterol esterification rate by 40-50% compared to the control value.

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[beta]-Amyloid (1-39)

A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-39) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

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[beta]-Amyloid (1-40), rat

A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-40) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

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[beta]-Amyloid (10-35)

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[beta]-Amyloid (22-35)

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beta-Amyloid (11-40)

Amount in mg: 1 mg

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beta-Amyloid (1-11) DAEFRHDSGYE

€105.00*

Description

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