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 (29-40) is a fragment of Amyloid-β peptide.Alzheimer's beta amyloid peptide (29-40/42) C-terminal fragments have physical and chemical properties related to those of fusion peptides of viral proteins. The fusion of liposomes can be induced by th

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

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].

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].

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].

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

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

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].

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-amyloid peptide.

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 (1-15) (Amyloid β-Protein (1-15)) is a fragment of β-amyloid protein used in the study of Alzheimer's disease.

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

(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].'

(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].

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

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].

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

(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].

(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].

Amyloid β-peptide fragment; minimum section required to bind to brain proteins. Binds with high affinity to α7-nicotinic ACh receptors, and impairs memory retention following central administration in mice in vivo.

β-amyloid (12-28) TFA, a peptide fragment of β-amyloid protein (β1-42), is the major component of senile plaque cores. β-amyloid (12-28) has aggregation properties and the potential for Alzheimer’s disease research.

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.

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].

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

β-Amyloid (1-28) is a β-Amyloid protein fragment involved in metal binding.

β-Amyloid (1-37) (human) Potentially associated with mental status in Alzheimer's disease.

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.

β-Amyloid (35-42) is a peptide derived from the beta-amyloid protein, encompassing amino acids 35 through 42.

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

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

[Asn23] β-Amyloid (1-40), Iowa mutation, is a biologically active peptide associated with autosomal dominant Alzheimer's Disease in multiple families. This specific mutation involves the substitution of Asp 23 with Asn, leading to severe cerebral amyloid beta-protein angiopathy (CAA). Individuals with this mutation exhibit a missense alteration in the APP gene at position 694, which results in the mutated β-amyloid peptide aggregating more quickly and forming toxic fibrils.

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide exhibiting 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 in various kindreds due to its association with severe cerebral amyloid beta-protein angiopathy (CAA). Specifically, the mutation is a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

β-Amyloid (13-27) is a peptide consisting of amino acid of 13 to 27 of beta amyloid protein. This synthetic peptide consists of amino acids 26 to 40 of beta amyloid protein. It can be used to study the kinetics of beta amyloid formation.

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.

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 (1-40) TFA, a principal protein in plaques observed in the brains of Alzheimer's disease patients [1], is pivotal in research focused on this neurodegenerative disorder.

β-Amyloid 22-35 (Amyloid β-Protein 22-35) TFA, a fragment comprising residues 22-35 of the β-amyloid protein, exhibits cytotoxicity towards cultured rat hippocampal neurons in serum-free media. It aggregates and forms typical amyloid fibrils in neutral buffer solution, mirroring those observed with the full-length β-amyloid protein [1].

β-Amyloid (33-40) is a peptide comprising amino acids 33 to 40 of the beta-amyloid protein.

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.

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

β-Amyloid (12-28) (TFA), a peptide fragment of the β-amyloid protein (β1-42)—a 42 amino acid protein primarily found in senile plaque cores—exhibits aggregation properties. This compound holds significance for research into Alzheimer’s disease, highlighting its potential utility in understanding the disease's pathology [1].

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