amyloid

Biotin-β-Amyloid (1-42), human TFA, also known as Biotin-Amyloid β-Peptide (1-42) (human) TFA, is a biotin-labeled 42-amino acid peptide implicated in the pathogenesis of Alzheimer's disease.

β-Amyloid (25-35) is a fragment of the Alzheimer’s amyloid beta peptide Aβ(25-35), exhibiting neurotoxic effects and commonly used to establish both cellular and animal models of Alzheimer’s disease.

β-Amyloid (1-42), rat mouse TFA is a 42-amino-acid polypeptide fragment that exhibits neurotoxicity to hippocampal slices and is commonly used to establish Alzheimer's disease models for related research.

Amyloid-β (25-35) (Aβ (25-35)) is an 11-residue fragment of the Aβ protein that retains the physical and biological characteristics of the full length peptide. It forms fibrils that react to thioflavin T and Congo red and are organized in a cross-β arrangement of β-strands similar to Aβ (1-40) and Aβ (1-42) fibrils. Aggregated Aβ (25-35) decreases the viability of rat adrenal PC12 cells. It also decreases the viability of primary rat cortical neurons at concentrations ranging from 1 nM to 30 μM. In vivo, intracerebral injection of Aβ (25-35) (20 nmol) in rats induces lesions of neuronal and tissue loss. Aggregated Aβ (25-35) administered intracerebroventricularly to rats induces learning and memory impairments in the Y-maze, novel object recognition, and contextual fear conditioning tests.

β-Amyloid (1-37) (human) is potentially associated with mental status in Alzheimer's disease.

The amyloid β-protein is a 39- to 43-amino acid polypeptide that is the primary constituent of senile plaques and cerebrovascular deposits in Alzheimer's disease and Down's syndrome. Additionally it acts as an inhibitor of the ubiquitin-dependent protein degradation in vitro.

β-Amyloid (1-40), FAM-labeled, is a β-Amyloid (1-40) peptide tagged with a FAM fluorescent label, exhibiting an excitation wavelength (λ ex) of 492 nm and an emission wavelength (λ em) of 518 nm.

Biotin-β-Amyloid (1-40) is an amyloid-β-(1-40) peptide with an N-terminal biotinylation.

β-Amyloid (1-38), derived from mice and rats, is a chemical compound comprising 38 amino acids, specifically residues 1-38 of the Aβ peptide. Notably, it serves as the primary constituent of amyloid plaques associated with Alzheimer's disease.

β-Amyloid (31-35) (β-Amyloid 31-35) is the shortest sequence of native Amyloid-β peptide.

β-Amyloid (1-40) TFA is a major protein fragment found in the brain plaques of Alzheimer's disease patients and is commonly used to establish Alzheimer's disease models.

β-Amyloid (12-28) (TFA), a peptide fragment of the 42 amino acid protein β-amyloid (β1-42), primarily found in senile plaque cores, exhibits aggregation properties and is significant for Alzheimer's disease research, highlighting its potential utility in understanding the disease's pathology [1].

β-Amyloid (42-1), human TFA is an inactive form of the amyloid β peptide (1-42) composed of 42 amino acids, which plays a key role in the pathogenesis of Alzheimer's disease and is commonly used to establish Alzheimer's disease animal models.

β-Amyloid (1-43)(human) TFA exhibits greater aggregation tendencies and heightened toxicity compared to Aβ1-42. This compound also associates with sAPPα and sAPPβ and has the potential to serve as an additional biomarker for Alzheimer's disease (AD), complementing existing markers [1].

β-Amyloid 22-35 (Amyloid β-Protein 22-35) TFA, a fragment comprising residues 22-35 of the β-amyloid protein, exhibits cytotoxicity towards cultured rat hippocampal neurons in serum-free media. It aggregates and forms typical amyloid fibrils in neutral buffer solution, mirroring those observed with the full-length β-amyloid protein [1].

β-Amyloid (1-40), FAM-labeled TFA, is a FAM fluorescently-labeled β-Amyloid (1-40) peptide (λ ex = 492 nm and λ em = 518 nm) [1].

Biotin-β-Amyloid (17-40) is a biotinylated amyloid-ß-(1-40) peptide labeled at the N-terminal, comprising a 24-residue fragment from the post-translational processing of amyloid precursor protein (APP) [1].

Amyloid 17-42 (Aβ(17-42)), a significant component of diffuse plaques in Alzheimer's disease and cerebellar pre-amyloid in Down's syndrome, results from alpha- and gamma-secretase cleavage of amyloid precursor protein (APP) and can trigger neuronal apoptosis via the Fas-like caspase-8 activation pathway [1].

Amyloid β-Protein (36-42), the 36-42 fragment of β-Amyloid, consists of a polypeptide chain of 36-43 amino acids and is a primary constituent of amyloid plaques in Alzheimer's disease (AD) patients' brains. β-Amyloid oligomers (Aβos) critically contribute to AD progression by causing neuronal harm and cognitive decline [1].

(Met(O)35)-Amyloid β-Protein (1-42) is the oxidized form of Methionine 35 in Aβ42, capable of producing an oligomer size distribution similar to Aβ40. This compound is utilized in Alzheimer's disease (AD) research [1].

(Met(O2)35)-Amyloid β-Protein (1-42) is a peptide [1].

(Nle35)-Amyloid β-Protein (1-42) ammonium is a peptide.

Amyloid β-Protein (33-42) TFA, encompassing residues 33-42 of the β-amyloid protein, mitigates the toxicity induced by Aβ42 [1].

(Gly22)-Amyloid β-Protein (1-42), a peptide fragment of Amyloid β-Protein (Aβ), plays a crucial role in Alzheimer's disease by forming the main component of vascular and parenchymal amyloid deposits. The Glu22 to Gly22 mutation in Aβ is known to enhance aggregation [1] [2].