b-amyloid protein precursor 770 135-155

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.

(Gln22,Asn23)-Amyloid β-Protein (1-40) is a peptide employed in the study of Cerebral Amyloid Angiopathy Mutations [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].

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

Amyloid beta-protein(1-40) Arctic variant (Ab40ARC (E22G)), featuring a glycine at position 22 (Gly22), is a peptide utilized in Alzheimer's disease research [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].

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

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

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

(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 both vascular and parenchymal amyloid deposits. The mutation from Glu22 to Gly22 in Aβ is known to enhance aggregation [1] [2].

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

Human vitamin D-binding protein (hDBP) is an abundant, multifunctional, and highly polymorphic serum glycoprotein synthesized by the liver1.

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

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

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

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), demonstrates increased fibrillogenic and pathogenic characteristics [1].

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

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly. This is attributed to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Notably, amyloid β-protein serves as the principal constituent of amyloid deposits found in both 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].

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

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

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

Acetyl-Amyloid β-Protein (1-6) amide, a hexapeptide with a potential copper(II) binding site, is utilized in research focused on Alzheimer's disease and related disorders [1].

Amyloid A proteins (H2N-Ala-Gly-Leu-Pro-Glu-Lys-Tyr-OH) are a family of apolipoproteins associated with high-density lipoprotein in plasma. Different isoforms of SAA are expressed constitutively at different levels or in response to inflammatory stimuli.