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Pathways Recommended:	Neuronal Signaling Cell Cycle/DNA Damage

Results for "

neuronal synaptic damage

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Akt (1) Amyloid-β (4) Drug Derivative (1) Epigenetic Reader Domain (1) ERK (1) iGluR (1) Indoleamine 2,3-Dioxygenase (IDO) (1) Interleukin Related (1) Isotope-Labeled Compounds (1) nAChR (1) NF-κB (1) PI3K (1) Tau Protein (1) TNF Receptor (1)
By Research Areas:	Neurological Disease (7)

Inhibitors & Agonists

Peptides

Isotope-Labeled Compounds

Targets Recommended: Synaptic Vesicle Proteins

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-P1363

β-Amyloid (1-42), human TFA Maximum Cited Publications 24 Publications Verification Amyloid β-peptide (1-42) (human) TFA	Amyloid-β	Neurological Disease
β-Amyloid (1-42) (Amyloid β-peptide (1-42), human TFA, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human TFA remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human TFA, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363A

β-Amyloid (1-42), human Maximum Cited Publications 24 Publications Verification Amyloid β-peptide (1-42) (human)	Amyloid-β	Neurological Disease
β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363B

β-Amyloid (1-42), human, HFIP-treated Maximum Cited Publications 24 Publications Verification	Amyloid-β	Neurological Disease
β-Amyloid (1-42), human, HFIP-treated, a 42-amino acid peptide that has been treated with HFIP from β-Amyloid (1-42), human (HY-P1363A), is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human, HFIP-treated remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, HFIP-treated, after being dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4°C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37°C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363S1

β-Amyloid (1-42), human, Ala(13C3,15N) TFA	Isotope-Labeled Compounds Amyloid-β	Neurological Disease
β-Amyloid (1-42), human, Ala( ¹³C₃, ¹⁵N) TFA is the ¹³C and ¹⁵N-labeled β-Amyloid (1-42), human (HY-P1363A). β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-184078

8-F-2-(Me-Pip-Me)-Tryptanthrin	Drug Derivative Indoleamine 2,3-Dioxygenase (IDO) Tau Protein iGluR	Neurological Disease
8-F-2-(Me-Pip-Me)-Tryptanthrin is a tryptanthrin derivative with blood-brain barrier penetration. 8-F-2-(Me-Pip-Me)-Tryptanthrin protects neurons from Aβ-induced apoptosis, inhibits Aβ-induced Tau protein hyperphosphorylation and neuronal synaptic damage, and improves learning and memory abilities in Alzheimer's disease mice. 8-F-2-(Me-Pip-Me)-Tryptanthrin can be used for the research of nervous system diseases, including diseases related to abnormal Tau protein phosphorylation and abnormal PSD-95 function .

HY-181672

PI3K/AKT/ERK/CREB activator 1	PI3K Akt ERK Epigenetic Reader Domain	Neurological Disease
PI3K/AKT/ERK/CREB activator 1 is an orally active PI3K/AKT/ERK/CREB pathway activator. PI3K/AKT/ERK/CREB activator 1 maintains neuronal survival and function, promotes neuronal proliferation, restores the viability of damaged neurons, and facilitates synapse formation. PI3K/AKT/ERK/CREB activator 1 alleviates neuroinflammation by reducing the levels of pro-inflammatory cytokines, preserves synaptic ultrastructure and restores spatial memory in Alzheimer's disease models. PI3K/AKT/ERK/CREB activator 1 can be used in research related to Alzheimer's disease .

HY-182707

JWX-A0108	nAChR Interleukin Related TNF Receptor NF-κB	Neurological Disease
JWX-A0108 is a selective human α7 nAChR positive allosteric modulator with an EC₅₀ of 4.35 μM. JWX-A0108 potentiates α7 nAChR currents only in the presence of acetylcholine, with no direct activating effect or alteration of desensitization. JWX-A0108 enhances hippocampal GABAergic synaptic transmission by increasing spontaneous inhibitory postsynaptic currents. JWX-A0108 reduces the brain expression levels of IL-1β, TNF-α, and IL-6 by blocking the NF-κB signaling pathway, and reduces microglial activation by downregulating Iba1. JWX-A0108 effectively improves cognitive deficits, neuroinflammation, and hippocampal neuronal damage in mouse models of schizophrenia and Alzheimer's disease. JWX-A0108 can be used for research related to schizophrenia and Alzheimer's disease .

Cat. No.	Product Name	Target	Research Area

HY-P1363

β-Amyloid (1-42), human TFA Maximum Cited Publications 24 Publications Verification Amyloid β-peptide (1-42) (human) TFA	Amyloid-β	Neurological Disease
β-Amyloid (1-42) (Amyloid β-peptide (1-42), human TFA, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human TFA remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human TFA, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363A

β-Amyloid (1-42), human Maximum Cited Publications 24 Publications Verification Amyloid β-peptide (1-42) (human)	Amyloid-β	Neurological Disease
β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363B

β-Amyloid (1-42), human, HFIP-treated Maximum Cited Publications 24 Publications Verification	Amyloid-β	Neurological Disease
β-Amyloid (1-42), human, HFIP-treated, a 42-amino acid peptide that has been treated with HFIP from β-Amyloid (1-42), human (HY-P1363A), is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human, HFIP-treated remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, HFIP-treated, after being dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4°C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37°C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

HY-P1363S1

β-Amyloid (1-42), human, Ala(13C3,15N) TFA	Isotope-Labeled Compounds Amyloid-β	Neurological Disease
β-Amyloid (1-42), human, Ala( ¹³C₃, ¹⁵N) TFA is the ¹³C and ¹⁵N-labeled β-Amyloid (1-42), human (HY-P1363A). β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

Cat. No.	Product Name	Chemical Structure

HY-P1363S1

β-Amyloid (1-42), human, Ala(13C3,15N) TFA
β-Amyloid (1-42), human, Ala( ¹³C₃, ¹⁵N) TFA is the ¹³C and ¹⁵N-labeled β-Amyloid (1-42), human (HY-P1363A). β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, *can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic* toxicity and neurotoxicity*; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage* process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

β-Amyloid (1-42), human, Ala(13C3,15N) TFA

β-Amyloid (1-42), human, Ala( ¹³C₃, ¹⁵N) TFA is the ¹³C and ¹⁵N-labeled β-Amyloid (1-42), human (HY-P1363A). β-Amyloid (1-42) (Amyloid β-peptide (1-42)), human, a 42-amino acid peptide that has not been treated with HFIP, is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, after being monomericized by HFIP and dissolved in DMSO to form the stock solution, on the one hand, can form soluble oligomers (AβOs) when incubated at 4 °C, which have synaptic toxicity and neurotoxicity; on the other hand, it can be incubated at 37 °C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death .

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