产品介绍：
描述链霉亲和素-生物素相互作用的高强度使得即使是高度稀释的目标也能高效捕获；然而，这使得从亲和树脂中回收蛋白质变得具有挑战性。从固定化亲和素中洗脱生物素化蛋白质的传统方法包括以下几种：（i）通过在可能包含高浓度非共价盐的变性缓冲液中煮沸树脂来变性链霉亲和素；（ii）在蛋白质与树脂结合时进行胰蛋白酶消化；或（iii）用过量自由生物素洗脱蛋白质。这些方案可能会通过释放非特异性结合的蛋白质和/或与标记蛋白质同时释放天然生物素化的蛋白质而共同洗脱污染蛋白。此外，部分方法可能导致与感兴趣的蛋白一起洗脱高水平的树脂基肽段，从而进一步导致样品污染。
DADPS（双烷氧基二苯基硅烷）生物素叠氮探针消除了链霉亲和素-生物素亲和纯化的一个主要限制。这种试剂包含一个生物素基团，通过一个包含可裂解的DADPS连接器的间隔臂与叠氮基团连接。捕获的生物分子可以在温和条件下（5%或10%的甲酸，0.5小时）有效释放，并且在裂解后，标记蛋白上留下的小（143 Da）分子碎片。这些特性使得DADPS探针在生物分子标记和蛋白组学研究中尤其具有吸引力。
英文介绍：
Description
Extraordinary strength of the streptavidin-biotin interaction allows for efficient capturing of even highly dilute targets; however, it makes recovery of proteins from affinity resins challenging. Conventional methods to elute biotinylated proteins from immobilized avidin include the following: (i) denaturation of streptavidin by boiling the resin in a denaturing buffer that may include high concentrations of chaotropic salts, (ii) trypsin digestion of proteins while they are bound to the resin, or (iii) elution of proteins with excess free biotin. These protocols can co-elute contaminant proteins by releasing nonspecifically bound proteins and/or naturally biotinylated proteins concurrently with labeled proteins. In addition, some of these methods can cause elution of high levels of resin-based peptides along with the proteins of interest, resulting in further sample contamination.
DADPS (dialkoxydiphenylsilane) Biotin Azide probes eliminate a major limitation of the streptavidin-biotin affinity purification. This reagent contains a biotin moiety linked to an azide moiety through a spacer arm containing a cleavable DADPS linker. Captured biomolecules can be efficiently released under mild conditions (5% or 10% formic acid, 0.5 h) and the small (143 Da) molecular fragment left on the labeled protein following cleavage. These features make the DADPS probe especially attractive for use in biomolecular labeling and proteomic studies.
反应切割：
产品参数：clickchemistrytools现货DADPS Biotin Azide货号CCT-1330选购指南
精选文献：
1. Wang, C., et al. (2020). Chemoproteomic Profiling of Itaconation by Bioorthogonal Probes in Inflammatory Macrophages. J Am Chem Soc., 142 (25), 10894-10898.
2. Willems, L. I., et al. (2020). Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins. J Am Chem Soc., 142 (37), 15729-15739.
3. Wang, J., et al. (2015). Mapping sites of aspirin-induced acetylations in live cells by quantitative acid-cleavable activity-based protein profiling (QA-ABPP).Sci. Rep.. 5: 7896.
4. Jinxu, G., et al. (2012). Small Molecule Interactome Mapping by Photoaffinity Labeling Reveals Binding Site Hotspots for the NSAIDs. J. Am. Chem. Soc.,. 140: 4259-68.
5. Szychowski, J., et al. (2010). Cleavable Biotin Probes for Labeling of Biomolecules via Azide?Alkyne Cycloaddition. J. Am. Chem. Soc., 132: 18351-60.
