β-amyloid (12-28) is a 17-aa peptide fragment, which can produce amyloid aggregates, used in the research of Alzheimer's disease.
CAT No: R1775
CAS No:107015-83-8
Synonyms/Alias:107015-83-8;Amyloid beta-Protein (12-28);MFCD00133075;AKOS024456836;DA-50448;FA110264;PD079193;Amyloid b-Protein (12-28) (H-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-OH);L-Lysine,L-valyl-L-histidyl-L-histidyl-L-glutaminyl-L-lysyl-L-leucyl-L-valyl-L-phenylalanyl-L-phenylalanyl-L-alanyl-L-a-glutamyl-L-a-aspartyl-L-valylglycyl-L-seryl-L-asparaginyl-;
β-amyloid 12-28 is a synthetic peptide fragment corresponding to residues 12 through 28 of the amyloid beta (Aβ) protein, a key molecule implicated in neurodegenerative processes and amyloid plaque formation. As a well-defined segment of the Aβ sequence, this peptide is widely used in biochemical and neurobiological research to study aggregation mechanisms, peptide-protein interactions, and the molecular basis of amyloidogenic disorders. Its defined length and sequence make it a valuable tool for dissecting the structural and functional properties of Aβ peptides in vitro and in cell-based assays, providing critical insights into the pathogenesis of diseases associated with amyloid deposition.
Aggregation studies: β-amyloid 12-28 serves as a model system for investigating the self-assembly and aggregation behavior of amyloidogenic peptides. Researchers utilize this fragment to monitor fibril formation, oligomerization kinetics, and the influence of sequence truncation on aggregation propensity. Its use enables the characterization of intermediate species and the elucidation of structural transitions that underlie amyloid fibril development, which is central to understanding the molecular pathology of Alzheimer's disease and related disorders.
Interaction mapping: The 12-28 fragment is frequently employed in studies aimed at mapping binding interfaces between amyloid beta peptides and cellular proteins, small molecules, or antibodies. By isolating this segment, scientists can pinpoint critical residues involved in protein-protein or protein-ligand interactions, facilitating the identification of potential modulators or inhibitors of amyloid aggregation. Such research is instrumental in advancing knowledge of molecular recognition events that may contribute to amyloid toxicity or clearance.
Structural biology: The peptide is a valuable reagent for high-resolution structural analyses, including nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. Its defined sequence allows for detailed examination of secondary structure formation, beta-sheet propensity, and conformational dynamics. These structural insights are essential for understanding how specific regions of the amyloid beta sequence contribute to the formation of pathogenic aggregates and for guiding the rational design of aggregation inhibitors.
Antibody development: β-amyloid 12-28 is used as an immunogen or as a screening antigen in the development and characterization of amyloid beta-specific antibodies. Its unique sequence enables the production of monoclonal or polyclonal antibodies that recognize specific epitopes within the central region of the Aβ peptide. Such antibodies are critical reagents for immunodetection, quantification, and localization of amyloid species in experimental models, supporting both basic research and the development of analytical assays.
Analytical assay calibration: The peptide fragment is frequently utilized as a reference standard or positive control in various analytical techniques, including enzyme-linked immunosorbent assays (ELISA), mass spectrometry, and Western blotting. Its defined composition and reproducible behavior facilitate the validation and calibration of detection methods aimed at quantifying amyloid beta species in biological samples or experimental preparations. This application enhances the reliability and comparability of results across different research platforms and laboratories.
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