β amyloid (10 35), amide

β-Amyloid (10-35), amide, is a chemical compound consisting of 26 amino acids, specifically residues 10-35 of the Aβ peptide. It serves as the primary constituent of amyloid plaques found in Alzheimer's disease.

Neurokinin A(4-10) TFA(97559-35-8 free base) is a tachykinin NK2 receptor agonist[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.

Acetyl-β Amyloid (15-20), Amide is a peptide fragment that inhibits β-sheet formation and stabilizes the structure of the Aβ (1–40) peptide, making it a useful tool in Alzheimer’s disease research [1].

β-Amyloid(28-35) human is a neurotoxic β-amyloid peptide fragment that contributes to Alzheimer's disease pathogenesis by interacting with neuronal membranes, modulating its secondary structure and toxicity. It also exhibits anisotropic effects on the acidic phospholipid DPH, thereby increasing the internal fluidity within lipid membrane bilayers [1].

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

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.

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.

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.

[Ala28]-β Amyloid(25-35) (β(25-35)KA), an electrically neutral mutant variant of Aβ(25-35), facilitates the accelerated aggregation of Firefly Luciferase [1].

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

(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].

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 (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.