aβ42-in-1

Aβ42-IN-1, compound 1v, is a novel, potent and orally active γ-secretase modulator (GSM). Aβ42-IN-1 potently reduced Aβ42 levels with an IC 50 value of 0.091 μM in cultured cells without inhibiting CYP3A4. Aβ42-IN-1 shows a sustained pharmacokinetic profile.

β-Amyloid (1-42), acetate (human) is a peptide consisting of 42 amino acids that is part of β-Amyloid and is commonly used in Alzheimer's disease modeling.

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 (1-42), human, is a 42-amino acid peptide integral to the pathogenesis of Alzheimer disease.

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.

Biotin-amyloid-β (1-42) peptide is an affinity probe that allows amyloid-β (1-42) (Aβ42) to be detected or immobilized through interaction with the biotin ligand. It has been used to identify Aβ42 interaction partners in rat hippocampal synaptosomal membranes.

(Met(O)35)-Amyloid β-Protein (1-42) is the oxidized form of Methionine 35 in Aβ42, capable of producing an oligomer size distribution similar to Aβ40. This compound is utilized in Alzheimer’s disease (AD) research [1].

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly due to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Amyloid β-protein is the principal constituent of amyloid deposits in the vascular system and brain parenchyma in Alzheimer's disease [1] [2].

Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-amino acid protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease.1,2,3Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers.1Aβ42 accumulates in the brain of many transgenic mouse models of Alzheimer's disease and, in many models, the onset of amyloid deposition positively correlates with deficits in spatial learning and memory.4 1.Wolfe, M.S.Therapeutic strategies for Alzheimer's diseaseNat. Rev. Drug Discov.1(11)859-866(2002) 2.Iwatsubo, T., Odaka, A., Suzuki, N., et al.Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)Neuron13(1)45-53(1994) 3.Hardy, J.A., and Higgins, G.A.Alzheimer's disease: The amyloid cascade hypothesisScience256(5054)184-185(1992) 4.Jankowsky, J.L., and Zheng, H.Practical considerations for choosing a mouse model of Alzheimer's diseaseMol. Neurodegener.12(1)89(2017)

Aβ42-IN-1 free base (compound 1v), an orally active γ-secretase modulator with high brain exposure, effectively lowers Aβ42 levels with an IC50 of 0.091 μM, and significantly diminishes brain Aβ42 levels in mice. Given these properties, Aβ42-IN-1 free base represents a potential disease-modifying agent for Alzheimer’s disease [1].

TAMRA-Amyloid-β (1-42) peptide is a fluorescently labeled peptide. Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-residue protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease. Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers. TAMRA-Amyloid-β (1-42) peptide is a labeled form of Aβ42 containing carboxytetramethyl rhodamine (TAMRA), which displays excitation/emission maxima of 543/572 nm, respectively.

(Met(O2)35)-Amyloid β-Protein (1-42) is a peptide [1].

Biotinyl-Ahx-Amyloid β-Protein (1-42) ammonium is an N-terminally biotin-tagged form of Amyloid β-Protein (1-42), the primary component of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), exhibits enhanced fibrillogenic and pathogenic properties [1].

Human beta-amyloid protein 42 (1-7) is a bioactive chemical.

HIV-1 inhibitor-42 (compound 5b) is a potent inhibitor of HIV-1 with an IC50 of 0.06 μM. It inhibits HIV-1 RT RNA-dependent DNA polymerase with an IC50 of 0.518 μM and DNA-dependent DNA polymerase with an IC50 of 0.072 μM.

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].

(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].

Gastric inhibitory peptide (GIP) (1-42), an endogenous incretin hormone comprising 42 amino acids, promotes insulin secretion. Expressed in the intestinal neuroendocrine K cells and submandibular gland, it enters circulation after meals. GIP (1-42) blocks histamine, pentagastrin, and insulin-induced gastric acid and pepsin secretion, enhances glucose-stimulated insulin release, and accelerates gastric emptying in rats.

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.

Piscidin-1 (22-42) (TFA) is a highly potent, multi-functional Antimicrobial Peptide (AMP) produced by Orange-spotted grouper (Epinephelus coioides).

(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 vascular and parenchymal amyloid deposits. The Glu22 to Gly22 mutation in Aβ is known to enhance aggregation [1] [2].

β-Amyloid (42-1), human TFA, a 42-amino acid peptide, represents the inactive form of Amyloid β Peptide (1-42) and is crucial in the development of Alzheimer's disease [1].

'(Lys22)-Amyloid β-Protein (1-42) represents a mutation of the wild-type (WT) Amyloid β-Protein (1-42) peptide [1].'

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

Aβ1-42 aggregation inhibitor 1 effectively inhibits acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) with IC50 values of 2.64 μM and 1.29 μM, respectively. At 25 μM, it also reduces self-mediated Aβ1-42 aggregation by 51.29%, showcasing its potential for Alzheimer's disease research [1].

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.

Piscidin-1 (22-42) is a highly potent, multifunctional Antimicrobial Peptide (AMP) produced by the Orange-spotted grouper (Epinephelus coioides).

Biotinyl-Amyloid β-Protein (1-42) ammonium, a biotinylated form of Amyloid β-Protein (1-42), is used in research on the conversion of Aβ1-42 to Aβ1-40 in the brain [1].

β-Amyloid (1-42), (rat mouse) (TFA), is a 42-amino acid peptide fragment employed in the study of Alzheimer's disease.

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide with 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 and associated with severe cerebral amyloid beta-protein angiopathy (CAA) due to a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

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

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

ChE Aβ1-42-IN-1 (compound 28) is a potent aggregation inhibitor of ChE and Aβ1-42 with excellent BBB permeability, exhibiting IC50 values of 0.062 μM for AChE, 0.767 μM for BuChE, and 1.227 μM for Aβ1-42 aggregation. ChE Aβ1-42-IN-1 is a potent multi-targeted anti-Alzheimer's disease agent [1].

Gastric inhibitory peptide 1 (GIP-1) (3-42), a fragment of the incretin hormone GIP and antagonist to the GIP receptor, is generated through the action of serum dipeptidyl peptidase 4 (DDP-4). When administered at 25 nmol/kg to an ob/ob mouse diabetes model, GIP-1 (3-42) elevates plasma glucose levels and lowers plasma insulin levels, demonstrating its effect on reducing insulin secretion from BRIN-BD11 pancreatic cells at a concentration of 100 nM.

YS-49 (monohydrate) is an activator of PI3K/Akt (a downstream target of RhoA).

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

Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42), a peptide fragment derived from amyloid β-protein (Aβ), is crucial in Alzheimer's disease research [1].

Compound 16 (hAChE/Aβ1-42-IN-1) is a potent inhibitor targeting both hAChE and Aβ1-42 aggregation, demonstrating considerable safety in hepG2 cell lines and excellent brain-blood barrier (BBB) penetration with a broad safety margin. This compound shows promise for Alzheimer's disease (AD) research [1].

Hematoxylin (Natural Black 1) is a dye obtained from the heartwood of logwood (Haematoxylon campechianum Linn., Leguminosae) used as a stain in microscopy and in the manufacture of ink.

Aβ-IN-1 is a novel, potent and orally active γ-secretase modulator (GSM). Aβ-IN-1 potently reduced Aβ42 levels with an IC 50 value of 0.091 μM in cultured cells without inhibiting CYP3A4. Aβ-IN-1 shows a sustained pharmacokinetic profile.

Aβ42-IN-2, a γ-secretase modulator with an IC50 of 6.5 nM for Αβ42, can be used for Alzheimer's disease research [1].

1. Licochalcone B (LCB) inhibits the proliferation of human malignant bladder cancer cell lines (T24 and EJ) in vitro and antitumor activity in vivo in MB49 (murine bladder cancer cell line) tumor model. 2. LCB and Licochalcone D(LCD) significantly reduce

Aftin-4, an amyloid forty-two inducer, activates γ-secretase, promoting the generation of amyloid-β-1-42 (Aβ1-42) from amyloid-β protein precursor. Aftin-4(Aftin4) increased Aβ-1-42, but not Aβ-1-40 in mouse hipppocampus, accompanied by learning deficits and mitochondrial ultrastructural changes similar to those found in the brains of patients with AD. Aftin-4(Aftin4) can thus be used to induce a rapid, acute Alzheimer's disease-like toxicity in the rodent brain.

3,5-Bis(4-nitrophenoxy)benzoic acid (Compound W) is a γ-secretase inhibitor that reduces the levels of released Aβ42 and notch-1 Aβ-like peptide 25 (Nβ25).

Sulindac EP Impurity C-d3 is a deuterated compound of Sulindac EP Impurity C. Sulindac EP Impurity C has a CAS number of 32004-67-4. (E/Z)-Sulindac sulfide is a potent γ-secretase modulator (GSM) that selectively reduces Aβ42 production in favor of shorter Aβ species. (E/Z)-Sulindac sulfide can be used for researching Alzheimer’s disease [1].

γ-Secretase modulator 12 (Compound 1a) is a selective compound that effectively reduces amyloid-β42 (Aβ42) levels with an IC50 of 0.39 μM, specifically designed for Alzheimer's disease research. Notably, γ-Secretase modulator 12 exhibits a favorable brain plasma ratio (Kp, brain = 0.72) in mice [1].

BACE1-IN-13 (Compound 36), an orally active inhibitor of BACE1, exhibits high potency with an IC50 of 2.9 nM and demonstrates greater efficacy in hAβ42 cells (IC50 = 1.3 nM). It is considered safe for the cardiovascular system and induces a sustained reduction of Aβ42 in both mouse and dog animal models [1].

Remternetug is a humanized IgG1-kappa monoclonal antibody that targets the N3pGlu peptide of the amyloid beta A4 precursor protein (APP) Aβ42. It specifically binds to the pyroglutamate-modified form of Aβ, which is implicated in the aggregation of amyloid plaques [1].

Amyloid-β (1-8, A2V) is a truncated form of amyloid-β (Aβ) that contains a valine to alanine substitution at position 2 of the Aβ numbering convention (Aβ A2V), which corresponds to position 673 of the amyloid precursor protein (APP) numbering convention (APP A673V). An Aβ (1-40) (Aβ40) A2V peptide increases the production of Aβ and the rate and amount of amyloid fibril formation in vitro, effects that can be reduced by coincubation with wild-type Aβ40. Aβ40 and Aβ42 levels are increased in CHO cells expressing the Aβ A2V mutation and in fibroblasts derived from patients with the Aβ A2V mutation. As a homozygous mutation, Aβ A2V is correlated with Alzheimer's disease with distinctive pathological features, but disease does not develop in patients with a heterozygous Aβ A2V mutation.