GSNKGAIIGLM(131602-53-4(free base)) (Amyloid beta-peptide(25-35)) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide.

β-Amyloid (25-35) (Aβ25-35) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide. Which has shown neurotoxic activities in cultured cells.

Amyloid β Peptide (42-1)(human) acetate is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human) acetate is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

β-Amyloid 15-21 acetate (Beta-Amyloid (15-21) acetate) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

[Arg6]-β-Amyloid (1-42), England mutation, is a biologically active peptide associated with autosomal dominant Alzheimer's Disease in various kindreds. The English (H6R) mutation disrupts H6 interactions due to several mutations in the beta-amyloid precursor gene.

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

β-Amyloid (1-40), England mutation, is a biologically active peptide with a histidine (His) to arginine (Arg) substitution at position 6, known to enhance oligomerization kinetics that serve as fibril seeds and increase neurotoxicity in cultured neurons. This alteration is one of several mutations in the beta-amyloid precursor gene implicated in autosomal dominant Alzheimer's Disease across multiple kindreds.

β-Amyloid (1-16) rat is a fragment of the metal-binding domain of the amyloid beta (Abeta) peptide. It contains three amino acid substitutions that distinguish it from its human counterpart, conferring reduced susceptibility to Alzheimer's disease-like neurodegeneration in rats and mice [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

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

β-amyloid (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

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].

[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.

Amyloid (1-42), rat is a polypeptide composed of 42 amino acids. It is toxic to hippocampal slices and can be used in the study of alzheimer's disease.

β-Amyloid (1-42), (rat/mouse) (TFA) is a peptide fragment consisting of 42 amino acids that can be used to study Alzheimer's disease.

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 (42-1), human is the inactive form of Amyloid β Peptide (1-42) which plays a key role in the pathogenesis of Alzheimer disease.

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.

β-Amyloid (1-42), human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

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.

Rat form of the beta-Amyloid (1-40) peptide

Antibodies corresponding to beta-amyloid (4-10) are effective in vivo inhibitors of cytotoxicity, amyloid plaque formation and special memory disturbances in mice. This peptide does not elicit an inflammatory response.

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.

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.

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

This is an N-terminal fragment of beta amyloid. It consists of amino acid residues 1 to 9. Truncated beta amyloid peptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.

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

neuroprotective peptide that binds to amyloid beta (Aβ)

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.

This is a fragment of beta-amyloid peptide. It has amino acids 1 through 34.

β-Amyloid (31-35) (β-Amyloid 31-35) is the shortest sequence of native Amyloid-β peptide.

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