amyloid precursor protein

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)

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

BACE-IN-1 acetate (BACE-IN-1 acetate (350228-37-4,Free base)) has been used as β-site amyloid precursor protein (APP) cleaving enzyme-1 (BACE1) inhibitor in BACE1 inhibitor assay. β-Site amyloid precursor protein (APP) cleaving enzyme-1 (BACE1), an aspartic protease belongs to the protease family of enzymes comprises of six luminal cysteine residues. These residues help in the formation of three intermolecular disulfide bonds and N-linked glycosylation sites.

Fmoc-Ala-Glu-Asn-Lys-NH2 is a peptide inhibitor that selectively targets asparagine endopeptidase (AEP) and inhibits the cleavage of amyloid precursor protein (APP). AEP, a pH-controlled cysteine proteinase, plays a crucial role in the proteolytic processing of APP, and its activity is enhanced during the aging process [1].

Biotin-β-Amyloid (17-40) is a biotinylated amyloid-ß-(1-40) peptide labeled at the N-terminal, comprising a 24-residue fragment from the post-translational processing of amyloid precursor protein (APP) [1].

Amyloid 17-42 (Aβ(17-42)), a significant component of diffuse plaques in Alzheimer's disease and cerebellar pre-amyloid in Down's syndrome, results from alpha- and gamma-secretase cleavage of amyloid precursor protein (APP) and can trigger neuronal apoptosis via the Fas-like/caspase-8 activation pathway [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].

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide with increased aggregation propensity and fibril toxicity. This mutation involves the substitution of Aspartic acid (Asp) at position 23 with Asparagine (Asn), contributing to autosomal dominant Alzheimer's Disease and associated with severe cerebral amyloid beta-protein angiopathy (CAA) due to a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

M-2420 is a fluorogenic substrate specifically designed for the β-secretase site associated with the Swedish mutation of the amyloid precursor protein (APP).

Amyloid β1-40 is one of the fragments generated after cleavage of the amyloid peptide precursor protein by β and γ secretases.

β-Amyloid/A4 Protein Precursor (319-335) (APP (319-335)) is a polypeptide fragment derived from the β-Amyloid/A4 Protein Precursor (APP). It is capable of identifying an APP-related, heparinase-resistant site that promotes neurocellular activity.