β-amyloid (tfa)

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.

β-Amyloid (1-40) TFA is a major protein fragment found in the brain plaques of Alzheimer's disease patients and is commonly used to establish Alzheimer's disease models.

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

β-Amyloid (42-1), human TFA is an inactive form of the amyloid β peptide (1-42) composed of 42 amino acids, which plays a key role in the pathogenesis of Alzheimer's disease and is commonly used to establish Alzheimer's disease animal models.

β-Amyloid (1-43)(human) TFA exhibits greater aggregation tendencies and heightened toxicity compared to Aβ1-42. This compound also associates with sAPPα and sAPPβ and has the potential to serve as an additional biomarker for Alzheimer's disease (AD), complementing existing markers [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 (1-40), FAM-labeled TFA, is a FAM fluorescently-labeled β-Amyloid (1-40) peptide (λ ex = 492 nm and λ em = 518 nm) [1].

Amyloid β-Protein (33-42) TFA, encompassing residues 33-42 of the β-amyloid protein, mitigates the toxicity induced by Aβ42 [1].

Biotin-β-Amyloid (1-42), human TFA, also known as Biotin-Amyloid β-Peptide (1-42) (human) TFA, is a biotin-labeled 42-amino acid peptide implicated in the pathogenesis of Alzheimer's disease.

β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows the effects of cytotoxicity on acute hippocampal slices, and has been used in studies of alzheimer's disease.

Amyloid β-Protein (3-42) TFA is a precursor of the Pyr peptide. The core of amyloid plaques in Alzheimer's disease is composed of pyroglutamate-modified Aβ (pEAβ) (3-42). Interestingly, pEAβ (3-42) accelerates the aggregation of Aβ(1-42), whereas Aβ(1-42) significantly slows both the primary and secondary nucleation of pEAβ(3-42).

(Pyr3)-Amyloid β-Protein (3-42) TFA is a principal amyloid β-peptide structure found in the brains of patients with Alzheimer's disease and Down syndrome. It is believed to accumulate in the brain and initiate the formation of insoluble amyloid β-peptide deposits.

β Amyloid (1-42) (scrambled) TFA serves as a negative control for β-Amyloid (1-42), human TFA.

β-Amyloid (1-38) (Aβ (1-38)) TFA is a peptide of β-amyloid (Aβ). This compound can disrupt the conversion of Aβ (1-42) into β-sheet-rich aggregates. Moreover, β-Amyloid (1-38) TFA counteracts the negative effects of Aβ (1-42) on long-term potentiation in acute hippocampal slices and membrane conductance in primary neurons, while also mitigating the Aβ (1-42) phenotype in Caenorhabditis elegans.

(Gln22)β-Amyloid (1-40) (human) TFA is a peptide containing amyloid β-protein (Aβ), utilized in Alzheimer's disease research.

β-Amyloid Protein Precursor 770 (135-155) TFA is a polypeptide fragment of a subtype of the β-amyloid precursor protein (APP 770). APP 770 is known for producing Aβ40/42.

β-Amyloid(1-42), human, Ala-13C3,15N trifluoroacetic acid is a β-Amyloid (1-42), human marked with 13C and 15N. This unprocessed HFIP peptide comprises 42 amino acids and is a brain-permeable amyloid fragment, useful for researching Alzheimer's and Down syndrome. In monomer form, β-Amyloid (1-42), human provides antioxidant and neuroprotective effects. Upon HFIP monomerization and DMSO solvent preparation, it forms soluble oligomers (AβOs) at 4°C, which exhibit synaptotoxicity and neurotoxicity, while at 37°C it forms insoluble fibrils with lower neurotoxicity, involved in oxidative damage. Aβ42 oligomers interact with neuronal surface receptors such as PrPc, mGluR5, and NMDA receptor, activating signaling pathways that induce oxidative stress, calcium imbalance, synaptotoxicity, leading to neuronal dysfunction and death.

β-Amyloid (1-40), HFIP-treated, refers to the β-Amyloid (1-40) peptide that has been processed with HFIP. This peptide is a key protein fragment found in the brain plaques of individuals with Alzheimer's disease.

β-Amyloid (1-42), rat/mouse TFA is a 42-amino-acid polypeptide fragment that exhibits neurotoxicity to hippocampal slices and is commonly used to establish Alzheimer's disease models for related research.

Neuropeptide Y (human) TFA, a compound implicated in Alzheimer's disease (AD), exhibits protective effects against β-Amyloid toxicity in rat cortical neurons.

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

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.

CS-6253TFA is the TFA salt form of CS-6253. This compound serves as an activator for the ATP Binding Cassette 1 (ABCA1). It effectively modulates the amyloid-beta Aβ42/40 ratio and influences the metabolism of lipoproteins in plasma. Additionally, CS-6253TFA facilitates the production of cholesterol-rich high-density lipoprotein (HDL) particles and induces the release of microparticles.

Neuropeptide Y (29-64), amide, human (TFA) is involved in Alzheimer's disease (AD) and protects rat cortical neurons against β-Amyloid toxicity.It is showed that Neuropeptide Y (29-64), amide, human (TFA) is able to protect cortical neurons from Aβ25-35 t