amyloid β-protein

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].

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly due to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Amyloid β-protein is the principal constituent of amyloid deposits in the vascular system and brain parenchyma in Alzheimer's disease [1] [2].

(D-Asp1)-Amyloid β-Protein (1-42), a peptide fragment of amyloid β-protein (Aβ), serves as the primary constituent of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42), a peptide fragment derived from amyloid β-protein (Aβ), is crucial in Alzheimer's disease research [1].

Biotinyl-Amyloid β-Protein (1-42) ammonium, a biotinylated form of Amyloid β-Protein (1-42), is used in research on the conversion of Aβ1-42 to Aβ1-40 in the brain [1].

FITC-β-Ala-Amyloid β-Protein (1-42) ammonium, a fluorescein isothiocyanate (FITC)-tagged monomer peptide of Aβ1-42, is instrumental in Alzheimer's disease pathogenesis [1].

Biotinyl-Ahx-Amyloid β-Protein (1-42) ammonium is an N-terminally biotin-tagged form of Amyloid β-Protein (1-42), the primary component of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

'(Asp37)-Amyloid β-Protein (1-42) [1]' refers to the G37D mutant variant of the wild-type Amyloid-beta (1-42) peptide.

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), exhibits enhanced fibrillogenic and pathogenic properties [1].

'(Lys22)-Amyloid β-Protein (1-42) represents a mutation of the wild-type (WT) Amyloid β-Protein (1-42) peptide [1].'

Acetyl-Amyloid β-Protein (1-6) amide, a hexapeptide potentially binding copper(II), is used in Alzheimer's disease research and related disorders [1].

Amyloid β-Protein (3-42), the precursor of Pyr peptide, serves as the foundation of the amyloid template block in Alzheimer's disease when modified to pyroglutamate Aβ (pEAβ) (3-42). This modified form, pEAβ(3-42), hastens the aggregation of Aβ(1-42) although Aβ(1-42) markedly decelerates both the primary and secondary nucleation of pEAβ(3-42) [1].

(Pyr11)-Amyloid β-Protein (11-40) (Aβ11pE-40), a peptide, is utilized in Alzheimer's disease research [1].

(Gln22,Asn23)-Amyloid β-Protein (1-40) is a peptide used to study Cerebral Amyloid Angiopathy Mutations [1].

Amyloid β-Protein 10-20 acetate (Amyloid β-Protein 10-20 acetate (152286-31-2 free base)) 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) responsible for binding to microglial cells.

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].

Beta-Amyloid Protein Precursor 770 (135-155)Aβ Protein Precursor 770 (135-155)

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.

BACE-IN-1 is amyloid precursor protein beta-secretase inhibitor