β amyloid (25 35)

β-Amyloid (25-35) is a fragment of the Alzheimer’s amyloid beta peptide Aβ(25-35), exhibiting neurotoxic effects and commonly used to establish both cellular and animal models of Alzheimer’s 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.

[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 (35-25) is the reverse sequence of β-Amyloid (25-35).

β-Amyloid (25-35) acetate is the Aβ(25-35) fragment of amyloid beta peptide, exhibiting neurotoxicity and commonly employed in constructing Alzheimer's disease cell and animal models.

Dactylorhin B is an active compound isolated from Coeloglossum Viride. Dactylorhin B reduces the toxic effects of β -amyloid fragments (25-35) on neuron cells and isolated rat brain mitochondria, which play an important role in neurodegenerative diseases.

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

FITC-β-Amyloid (25-35) is a FITC-labeled β-Amyloid (25-35) . FITC is a green fluorescent probe used for labeling biomolecules, while β-Amyloid (25-35) is a neurotoxic amyloid beta peptide fragment associated with Alzheimer's disease.