β-amyloid , human

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

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.

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 (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 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(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].

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), 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.

β-Amyloid (42-1), human is the inactive form of amyloid β peptide (1-42), consisting of 42 amino acids. It plays a key role in the pathogenesis of Alzheimer's disease and is commonly used to induce Alzheimer's disease models.

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.

Human Serum Albumin (HSA) is the most abundant protein in human plasma, is produced in the liver and is water soluble, with a molecular weight of 66.5 kDa. HSA inhibits Alzheimer's disease by selectively binding to cross-structured A oligomers. HSA is a key endogenous inhibitor of amyloid-β (Αβ) aggregation. HSA is used as a carrier protein in cell culture for the transport of fatty acids, steroids, and thyroid hormones and to regulate osmolality of the blood, and is also used in drug delivery studies, immunoassays, and cell freezing. cell freezing.

Neuropeptide Y (29-64), amide, human acetate is involved in Alzheimer's disease (AD) and protects rat cortical neurons against β-Amyloid toxicity.

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.

Neuropeptide Y (human) TFA, a compound implicated in Alzheimer's disease (AD), exhibits protective effects against β-Amyloid toxicity in rat cortical neurons.

[D-Arg25]-Neuropeptide Y (human) ([D-Arg25] NPY), a Y1 receptor selective agonist, is involved in Alzheimer's disease (AD) and protects rat cortical neurons from β-Amyloid toxicity [1].

β-Amyloid (1-16) rat is a fragment of the amyloid beta (Abeta) peptide's metal-binding domain, containing three amino acid substitutions compared to its human counterpart, which confer reduced susceptibility to Alzheimer's disease-like neurodegeneration in rats and mice [1].

Amylin, amide, human is a 37-amino acid peptide hormone co-secreted with insulin to regulate postprandial glucose levels, reducing glucagon secretion and delays gastric emptying. DAP Amide's tendency to aggregate into amyloid fibrils is associated with pancreatic β-cell damage in type 2 diabetes.

Neuropeptide Y (29-64), amide, human (TFA) is involved in Alzheimer's disease (AD) and protects rat cortical neurons against β-Amyloid toxicity.It is showed that Neuropeptide Y (29-64), amide, human (TFA) is able to protect cortical neurons from Aβ25-35 t