75621-03-3
Chemical Structure
CHAPS
- CAS No.: 75621-03-3
- Formula:C32H58N2O7S
- Molecular Weight:614.88
IUPAC Name: 3-(dimethyl(3-((R)-4-((3R,5S,7R,8R,9S,10S,12S,13R,14S,17R)-3,7,12-trihydroxy-10,13-dimethylhexadecahydro-1H-cyclopenta[a]phenanthren-17-yl)pentanamido)propyl)ammonio)propane-1-sulfonate
InChIKey: UMCMPZBLKLEWAF-BCTGSCMUSA-N
SMILES: O[C@@H]1CC[C@]2(C)[C@@]3([H])C[C@H](O)[C@]4(C)[C@@H]([C@H](C)CCC(NCCC[N+](C)(C)CCCS([O-])(=O)=O)=O)CC[C@@]4([H])[C@]3([H])[C@H](O)C[C@@]([H])2C1
Biological Activity: CHAPS is a cholic acid-derived, sulfobetaine-type zwitterionic detergent and micelle-forming agent. CHAPS exhibits properties of weak cationic or nonionic surfactants in different solution systems, undergoes micellization, and forms small, loose hydrophilic aggregates that are temperature-dependent. CHAPS stabilizes mononucleosomes under different ionic strengths, reduces nucleosome sequence specificity, promotes sliding of histone cores along DNA, solubilizes Tamm-Horsfall protein to reduce its interference with urinary exosome isolation, and maintains vesicle structure and the activity of related proteins at the same time. CHAPS is used to recover native folded fusion proteins, enhance the binding capacity of GST fusion proteins, and restore GST enzyme activity. However, CHAPS cannot refold proteins denatured by urea, guanidine hydrochloride or heat, nor can it construct the structure of intrinsically disordered proteins. CHAPS is commonly used in research on the separation and purification of membrane proteins[1][2][3][4].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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CHAPS | 99.91% | CHAPS is a cholic acid-derived, sulfobetaine-type zwitterionic detergent and micelle-forming agent. CHAPS exhibits properties of weak cationic or nonionic surfactants in different solution systems, undergoes micellization, and forms small, loose hydrophilic aggregates that are temperature-dependent. CHAPS stabilizes mononucleosomes under different ionic strengths, reduces nucleosome sequence specificity, promotes sliding of histone cores along DNA, solubilizes Tamm-Horsfall protein to reduce its interference with urinary exosome isolation, and maintains vesicle structure and the activity of related proteins at the same time. CHAPS is used to recover native folded fusion proteins, enhance the binding capacity of GST fusion proteins, and restore GST enzyme activity. However, CHAPS cannot refold proteins denatured by urea, guanidine hydrochloride or heat, nor can it construct the structure of intrinsically disordered proteins. CHAPS is commonly used in research on the separation and purification of membrane proteins. | ||||||||||||||||||||
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CHAPS (Standard) | ≥98% | CHAPS (Standard) is the analytical standard of CHAPS. This product is intended for research and analytical applications. CHAPS, a derivative of Cholic acid, is a zwitterionic detergent for solubilizing membrane proteins. CHAPS is used for stabilization of various protein-DNA complexes and can retain biochemical activity of proteins in solution. | ||||||||||||||||||||
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- [1]. Kroflič A, et al. Thermodynamic characterization of 3-[(3-cholamidopropyl)-dimethylammonium]-1-propanesulfonate (CHAPS) micellization using isothermal titration calorimetry: temperature, salt, and pH dependence. Langmuir. 2012;28(28):10363-10371. [Content Brief]
- [2]. Menshikova I, et al. Nucleosomes structure and dynamics: effect of CHAPS. Int J Biochem Mol Biol. 2011;2(2):129-137. [Content Brief]
- [3]. Musante L, et al. Biochemical and physical characterisation of urinary nanovesicles following CHAPS treatment. PLoS One. 2012;7(7):e37279. [Content Brief]
- [4]. Tao H, et al. Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS. Biotechniques. 2010;48(1):61-64. [Content Brief]
Keywords
