货号 | 13173-10mg |
描述 | Redox-sensitive cysteine residues in proteins may function as sensors of reactive oxygen species (ROS) and also serve as molecular switches, activating or deactivating proteins, following a change in oxidation state. Modification of protein function through the reversible oxidation of cysteine is emerging as a biologically relevant signal transduction mechanism. Sulfenic acid is the initial oxidation product of cysteine by relatively mild oxidizing agents such as hydrogen peroxide. Sulfenic acid can be reduced back to the free thiol or be further oxidized to sulfinic and sulfonic acids.1 DAz-1 is a cell-permeable chemical probe that reacts specifically with sulfenic acid-modified proteins.2,3 The azido group of DAz-1 provides a method for selective conjugation to phosphine- or alkynyl- derivatized reagents, such as biotin or various fluorophores, for subsequent analysis of the labeled proteins. DAz-1 is a less sensitive a probe for sulfenic acid detection compared to its analog DAz-2 (Item No. 13382).4 |
别名 | Click Tag™ DAz-1; |
供应商 | Cayman |
应用文献 | |
1.Reddie, K.G. and Carroll, K.S. Expanding the functional diversity of proteins through cysteine oxidation. Current Opinion in Chemical Biology 12(6), 746-754 (2008). 2.Seo, Y.H. and Carroll, K.S. Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins. Bioorganic & Medicinal Chemistry Letters 19, 356-359 (2009). 3.Reddie, K.G.,Seo, Y.H.,Muse, W.B., III, et al. A chemical approach for detecting sulfenic acid-modified proteins in living cells. Molecular BioSystems 4, 521-531 (2008). 4.Leonard, S.E.,Reddie, K.G. and Carroll, K.S. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4(9), 783-799 (2009). | |
运输条件 | Room temperature in continental US; may vary elsewhere |
存放说明 | -20 |
纯度 | ≥98% |
计算分子量 | 238.2 |
分子式 | C10H14N4O3 |
CAS号 | 1112977-84-0 |
稳定性 | ≥ 2 years |
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