βamyloid (421), human

Amyloid β Peptide (42-1)(human) acetate is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human) acetate is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

β-Amyloid (1-42), acetate (human) is a peptide consisting of 42 amino acids that is part of β-Amyloid and is commonly used in Alzheimer's disease modeling.

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 (1-42), human, is a 42-amino acid peptide integral to the pathogenesis of Alzheimer disease.

β-Amyloid (42-1), human, is the inactive form of Amyloid β Peptide (1-42), which plays a pivotal role in the pathogenesis of Alzheimer's disease.

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 (42-1), human TFA, a 42-amino acid peptide, represents the inactive form of Amyloid β Peptide (1-42) and is crucial in the development of Alzheimer's disease [1].

β-Amyloid precursor protein (96-110), cyclized (human), a segment of the amyloid precursor protein, serves as a research tool in Alzheimer's disease studies [1].

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(28-35) human is a neurotoxic β-amyloid peptide fragment that contributes to Alzheimer's disease pathogenesis by interacting with neuronal membranes, modulating its secondary structure and toxicity. It also exhibits anisotropic effects on the acidic phospholipid DPH, thereby increasing the internal fluidity within lipid membrane bilayers [1].

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

β-Amyloid(17-28) human is a fragment of the β-amyloid peptide (Abeta) associated with Alzheimer's disease (AD), promoting the aggregation of the full-length β-Amyloid40 into toxic aggregates [1]. This lipid-induced amyloid core segment is implicated in AD pathogenesis.

β-Amyloid (1-42), (rat mouse) (TFA), is a 42-amino acid peptide fragment employed in the study of Alzheimer's disease.