User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi]

User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi]: CLIP-Tag Substrate for Advanced Click Chemistry

User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi] is a cutting-edge CLIP-tag substrate designed for sophisticated click chemistry applications. Engineered to interact specifically with benzylcytosine derivatives, this modified SNAP-tag offers unparalleled flexibility in protein labeling and tracking. Its unique methylcyclopropene moiety acts as a dienophile in inverse electron-demand Diels-Alder (iEDDA) reactions, enabling stable conjugation and molecular labeling without the need for catalysts. This versatile substrate is a game-changer in bioorthogonal chemistry, making it an ideal choice for researchers seeking innovative solutions in live-cell imaging and other biological studies.

Product Specifications and Benefits

User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi] boasts a molecular formula of C18H20N4O3 and a molecular weight of 340.383. With a purity of >= 95% (HPLC), this high-quality substrate ensures reliable and consistent results. Its solubility in DMSO and DMF further enhances its usability. Key benefits of User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi] include its compatibility with both SNAP-tag and CLIP-tag systems, enabling dual-labeling experiments, and its suitability for a wide range of biological applications, such as live-cell imaging and molecular labeling.

Practical Applications and Target Audience

User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi] is a powerful tool for researchers in various fields, including molecular biology, biochemistry, and biotechnology. Its ability to facilitate stable conjugation and molecular labeling without catalysts makes it highly advantageous for live-cell imaging, drug discovery, and protein engineering. Ideal for those seeking advanced click chemistry solutions, User-friendly Bc-cp Holiday Cheer Edition [X2tISqzi] is perfect for researchers and scientists looking to push the boundaries of their research and explore new possibilities in protein labeling and tracking.