β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows cytotoxic effect on acute hippocampal slices, and used in the research of Alzheimer's disease.
CAT No: R1767
β-Amyloid (1-42), rat TFA is a synthetic peptide corresponding to the 1-42 amino acid sequence of the rat β-amyloid protein, modified as a trifluoroacetate salt. As a key fragment of the amyloid precursor protein (APP), this peptide is central to research on amyloid aggregation and neurodegenerative processes, particularly in rodent models. Its sequence and aggregation properties make it a valuable tool for elucidating the molecular mechanisms of amyloid fibril formation, synaptic dysfunction, and neuronal toxicity. The rat-specific sequence enables comparative studies alongside the human β-amyloid (1-42) peptide, supporting investigations into species-dependent differences in amyloid pathology and offering insights relevant to translational neuroscience.
Aggregation studies: β-Amyloid (1-42), rat TFA is widely utilized in studies of peptide aggregation, where its propensity to form oligomers and fibrils is examined under various biochemical conditions. Researchers employ this peptide to characterize the kinetics and structural transitions involved in amyloidogenesis, using techniques such as thioflavin T fluorescence, atomic force microscopy, and circular dichroism. These investigations provide critical data on the physicochemical factors that drive amyloid formation and are foundational for understanding the aggregation mechanisms underlying neurodegenerative disorders.
Neurotoxicity assays: The rat β-amyloid (1-42) peptide serves as a model agent in in vitro and ex vivo neurotoxicity assays, enabling the assessment of neuronal viability and synaptic integrity in response to amyloid exposure. By exposing primary neuronal cultures or brain slices to defined concentrations of the peptide, researchers can quantify cellular responses, including oxidative stress, apoptosis, and synaptic dysfunction. These assays are essential for dissecting the molecular pathways of amyloid-induced neurotoxicity and for evaluating the efficacy of neuroprotective compounds.
Comparative pathology modeling: Due to its species-specific sequence, the rat β-amyloid (1-42) peptide is instrumental in comparative studies that contrast amyloid aggregation and toxicity between rodent and human forms. Such research is crucial for validating animal models of amyloidosis and for interpreting the translational relevance of preclinical findings. By comparing aggregation kinetics, fibril morphology, and neurotoxic outcomes, investigators gain a deeper understanding of species-dependent differences in amyloid pathobiology.
Screening of aggregation modulators: The peptide is frequently employed in high-throughput screening platforms designed to identify and characterize small molecules, peptides, or antibodies that modulate amyloid aggregation. By monitoring changes in oligomerization or fibril formation in the presence of candidate compounds, researchers can pinpoint agents that alter the aggregation pathway or stabilize non-toxic conformations. These studies are integral to the early-stage discovery and optimization of potential therapeutic leads targeting amyloidogenic processes.
Biophysical and structural analysis: β-Amyloid (1-42), rat TFA facilitates advanced biophysical investigations into the structural properties of amyloid assemblies. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, cryo-electron microscopy, and mass spectrometry are applied to elucidate conformational dynamics, intermolecular interactions, and aggregation intermediates. These analyses provide a molecular-level understanding of amyloid structure and inform the rational design of aggregation inhibitors or diagnostic tools. Through such multifaceted applications, the rat β-amyloid (1-42) peptide remains a cornerstone reagent in amyloid research, supporting both fundamental discovery and translational innovation in the neurosciences.
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