α-Casein (90-95) is a peptide fragment of α-Casein.
CAT No: R1761
CAS No:83471-50-5
Synonyms/Alias:Arg-tyr-leu-gly-tyr-leu;83471-50-5;alpha-Casein (90-95);alpha-Casein(90-95);(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoic acid;-Casein (90-95);DTXSID301003450;HY-P1793;DA-79156;FC108579;CS-0095735;L-Arginyl-L-tyrosyl-L-leucylglycyl-L-tyrosyl-L-leucine;(6S,9S,12S,18S,21S)-1,6-diamino-9,18-bis(4-hydroxybenzyl)-1-imino-12,21-diisobutyl-7,10,13,16,19-pentaoxo-2,8,11,14,17,20-hexaazadocosan-22-oic acid;N-{14,19-Diamino-1,4,7,10,13-pentahydroxy-2,11-bis[(4-hydroxyphenyl)methyl]-19-imino-8-(2-methylpropyl)-3,6,9,12,18-pentaazanonadeca-3,6,9,12-tetraen-1-ylidene}leucine;
α-Casein 90-95 is a synthetic peptide fragment derived from the bovine α-casein protein, encompassing amino acid residues 90 to 95. As a short, well-defined peptide sequence, it serves as a valuable tool in biochemical research focused on protein-protein interactions, structure-function relationships, and the investigation of post-translational modifications. The defined sequence of α-Casein 90-95 allows for precise experimental manipulation, making it highly relevant for studies that require controlled peptide substrates or molecular probes. Its origin from a major milk protein further enhances its utility in exploring casein biology, enzymatic processing, and food-related research contexts.
Peptide substrate studies: Researchers frequently employ α-Casein 90-95 as a model substrate to investigate the activity and specificity of proteolytic enzymes, such as serine and aspartic proteases. The short, defined sequence enables detailed kinetic analyses and mapping of cleavage preferences, providing insight into enzyme-substrate recognition mechanisms. This application is particularly valuable in enzymology, where understanding substrate specificity is essential for characterizing novel proteases or optimizing biocatalytic processes.
Protein interaction assays: The α-Casein 90-95 peptide fragment serves as a useful probe for examining molecular interactions between casein-derived sequences and other proteins, such as receptors, antibodies, or binding partners. By immobilizing or labeling this peptide, researchers can conduct binding studies using techniques like surface plasmon resonance, ELISA, or pull-down assays. These experiments help elucidate the molecular determinants of casein interactions, contributing to a deeper understanding of protein networks in dairy biochemistry and broader protein science.
Antibody epitope mapping: Due to its defined sequence, α-Casein 90-95 is employed in mapping the epitope specificity of antibodies raised against casein or related proteins. Synthetic peptides corresponding to specific regions of α-casein enable researchers to pinpoint the exact amino acid residues recognized by monoclonal or polyclonal antibodies. This approach facilitates the development and validation of immunoassays, supports the generation of highly specific detection reagents, and advances the characterization of immune responses to milk proteins.
Peptide modification research: The sequence of α-Casein 90-95 provides a convenient template for studying post-translational modifications, such as phosphorylation or glycosylation, within a controlled context. Researchers can synthesize modified versions of the peptide to assess the impact of specific chemical changes on peptide structure, stability, and biological recognition. Such studies are instrumental in deciphering the functional consequences of modifications that naturally occur in casein proteins and their relevance to protein folding, aggregation, and function.
Analytical method development: The defined nature of α-Casein 90-95 makes it an excellent standard or reference material for developing and validating analytical techniques, including high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its consistent sequence and physicochemical properties enable accurate calibration, method optimization, and performance benchmarking in peptide analysis workflows. This utility is particularly important for laboratories seeking to ensure reproducibility and sensitivity in the quantification or identification of peptides in complex biological samples.
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