amyloid beta-protein

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 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.

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

[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 precursor protein (96-110), cyclized (human), a segment of the amyloid precursor protein, serves as a research tool in Alzheimer’s disease studies [1].

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

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

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

Beta-Amyloid(1-14),mouse,rat is a 1 to 14 fragment of Amyloid-β peptide. This peptide is amino acids 1 to 14 fragment of Beta-Amyloid 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].

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

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].

(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].

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.

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

[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.

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.

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

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

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).

This synthetic peptide consists of amino acids 1 to 17 of beta amyloid protein. This peptide can be employed in beta amyloid solubility studies.

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.

This synthetic peptide consists of amino acids 1 to 20 of beta amyloid protein.

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.

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.

This synthetic peptide consists of amino acids 22 to 40 of beta amyloid protein. This peptide sequence is often used in beta amyloid structure and aggregation studies.

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