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.
Amyloid precursor c-terminal peptide has the amino acid sequence Gly-Tyr-Glu-Asn-Pro-Thr-Tyr-Lys-Phe-Phe-Glu-Gln-Met-Gln-Asn. APP is best known as the precursor molecule whose proteolysis generates beta-amyloid (Aβ), a 37 to 49 amino acid peptide whose am
Amyloid (1-42), rat is a polypeptide composed of 42 amino acids. It is toxic to hippocampal slices and can be used in the study of alzheimer's disease.
[Arg6]-β-Amyloid (1-40), England mutation 是具有生物活性的肽,与多种家族性常染色体显性阿尔茨海默病相关。特别地,这种英国突变,即位于第6位的His被Arg所替换,已报告可提高寡聚体形成动力学,加速初级纤维的种子化过程。此类寡聚体对神经元培养细胞展现出较高毒性。
β-Amyloid (1-16) is an amyloidogenic protein fragment with a sequence derived from β-amyloid. It exhibits the ability to bind to metal ions, indicating its involvement in metal-binding processes. β-Amyloid, a peptide, is responsible for the formation of amyloid plaques in the brains of individuals affected by Alzheimer's disease (AD).
β-Amyloid (29-40), a fragment of the Amyloid-β peptide, possesses physical and chemical properties similar to those of viral protein fusion peptides. The C-terminal fragments (29-40 42) of Alzheimer's beta amyloidpeptide can induce the fusion of liposomes.
β-Amyloid (22-35) is a 14-aa peptide, shows aggregates and induces neurotoxicity in the hippocampal cells. Beta amyloid (22-35) is a synthetic truncated fragment of beta-amyloidpeptide.
Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) re
Exendin (5-39) is a powerful antagonist of the glucagon-like peptide 1 (GLP-1) receptor with the ability to ameliorate memory impairment in rats treated with β-amyloid protein.
β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows the effects of cytotoxicity on acute hippocampal slices, and has been used in studies of alzheimer's disease.
β-Amyloid (1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. β-Amyloid (1-14),mouse,rat is produced through the proteolytic processing of a transmembrane protein, amyloid precursor protein (APP), by β- and γ-secretases. β-Amyloid (1-14),mouse,rat accumulation in the brain is proposed to be an early toxic event in the pathogenesis of Alzheimer’s disease, which is the most common form of dementia associated with plaques and tangles in the brain[1]. [1]. Chen GF, et al. Amyloid beta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin. 2017 Sep;38(9):1205-1235.
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 (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.
β-Amyloid (11-22) is a peptide fragment of β-Amyloid. Beta-amyloidpeptide (Abeta), the primary component of amyloid plaques in the brains of Alzheimer’s patients, is believed to be the cause of Alzheimer’s Disease (AD), the most common neurodegenerative disorder.