[beta]-Amyloid (22-35)

Aβ (22-35), EDVGSNKGAIIGLM, forms amyloid fibrils in vitro resembling those of the β-amyloid protein in senile plaques and exhibits a toxicity profile that parallels that of full-length Aβ (1-40) and Aβ (1-42) in hippocampal and cortical neurons in cell culture.

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

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Available, delivery time: 3-4 weeks

sterile and endotoxin free
Delivery Format: The product is supplied freeze dried.
Purity: 95% HPLC-MS

Amount in mg

1 mg

5 mg

Product number: EP10054_1

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[beta]-Amyloid (1-14)

Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimer’s patients, is thought to be the cause of Alzheimer’s Disease (AD). AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60.

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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)

Amyloid β-protein (10-35), YEVHHQKLVFFAEDVGSNKGAIIGLM, was used as a truncated peptide model for the full-length amyloid β-proteins (1-40) and (1-42) in high-resolution structural studies. In contrast to the full-length amyloid β-proteins, amyloid β-protein (10-35) allowed the controlled and reproducible formation of homogeneous fibrils from aqueous solutions of defined pH, ionic strength and soluble peptide concentration necessary for high-resolution structural studies.

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[beta]-Amyloid (12-28)

Aβ (12-28) represents a binding site for apolipoprotein E (apoE). ApoE is a genetically inherited risk factor for Alzheimer’s disease that promotes aggregation of toxic Aβ. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Aß (11-28) and five other fragments enhanced aggregation of full length Aß (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length Aß.

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[beta]-Amyloid (13-27)

This β-Amyloid peptide 13 to 27 amino acid residues was used to study the kinetics of β-amyloid formation.

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[beta]-Amyloid (16-23) ( KLVFFAED )

This octapeptide beta-Amyloid 16 to 23 was used in exploring the design of potential inhibitors of amyloidogenesis. This peptide is capable of forming thin flakes, while the shortest fibril-forming sequence was found to be the decapeptide b-Amyloid 14 to 23.

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[beta]-Amyloid (22-35)

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beta-Amyloid (1-11) ( DAEFRHDSGYE )

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.

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beta-Amyloid (11-22)

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beta-Amyloid (11-40)

Post-mortem Alzheimer’s diseased brain specimens reveals significant levels of Aß (11-40/42) within insoluble amyloid pools. The ß-secretase enzyme or ß-amyloid precursor protein-cleaving enzyme (BACE) generates the N terminus of Aß, ultimately leading to the production of full-length Aß (1-40/42) or truncated Aß (11-40/42). The abundance of Aß (11-40/42) produced by BACE suggests that their roles in AD pathogenesis may be important.

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