CHAPS hydrate 

CHAPS hydrate is a cholic acid-derived, sulfobetaine-type zwitterionic detergent and micelle-forming agent. CHAPS hydrate 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 hydrate 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 hydrate is used to recover native folded fusion proteins, enhance the binding capacity of GST fusion proteins, and restore GST enzyme activity. However, CHAPS hydrate cannot refold proteins denatured by urea, guanidine hydrochloride or heat, nor can it construct the structure of intrinsically disordered proteins. CHAPS hydrate is commonly used in research on the separation and purification of membrane proteins^[1][2][3][4].

CHAPS hydrate forms low aggregation number (5.4-6.7) micelles with cmc values dependent on solvent and temperature (U-shaped cmc vs temperature curve with minimum at ~295 K) and ΔH_m⁰ transitioning from endothermic to exothermic with increasing temperature in aqueous solutions, NaCl solutions, and buffer solutions^[1].
CHAPS hydrate (16-4.8 mM; 1-120 h) stabilizes reconstituted mononucleosomes (assembled with human histones H2A, H2B, H3, H4 on 601 sequence DNA) at 0.4 nM concentration at 0°C without altering their structure, with 16 μM preventing dissociation for 1 hour, 1.6 mM maintaining over 50% intact nucleosomes for 120 hours, and 4.8 mM maintaining over 70% intact nucleosomes for 120 hours^[2].
CHAPS hydrate (1% (w/v); overnight at 4°C) treatment of pooled urine-derived exosomal pellets (P18, P200) preserves vesicle morphology, exosomal marker distribution, and nephrilysin activity while removing interfering proteins like THP and albumin^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

632.89

C₃₂H₆₀N₂O₈S

331717-45-4

Solid

White to off-white

O[C@H]1[C@@]2([H])[C@@]3([H])[C@@]([C@@](CC3)([H])[C@H](C)CCC(NCCC[N+](C)(C)CCCS(=O)([O-])=O)=O)([C@H](C[C@]2([H])[C@@]4([C@](C[C@@H](CC4)O)([H])C1)C)O)C.O

Room temperature in continental US; may vary elsewhere.

4°C, sealed storage, away from moisture and light

*In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light)

* Please refer to the solubility information to select the appropriate solvent. Once prepared, please aliquot and store the solution to prevent product inactivation from repeated freeze-thaw cycles.
Storage method and period of stock solution: -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light). When stored at -80°C, please use it within 6 months. When stored at -20°C, please use it within 1 month.

• [1]. Kroflic 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 Jul 17;28(28):10363-71.  [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]