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3-[(3-Cholanidopropyl) Dimethylammonio]-1-Propane Sulfonate
$161.00
Sku: CD0110-0025
Synonym(s): CHAPS, 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate
Description
CHAPS is a standard reagent has been found suitable for use as a solubilizing agent in isoelectric focusing applications. It is tested to meet low metal content specifications.
CHAPS is a non-denaturing, zwitterionic sulfobetaine detergent for solubilizing membrane proteins and breaking protein-protein interactions. Commonly used for protein solubilization in isoelectric focusing and two-dimensional electrophoresis, especially for nondenaturing (without urea) IEF.
CHAPS has been shown to give excellent resolution of some subcellular preparations and plant proteins. Concentrations between 1-4% (w/v) are typically used in an IEF gel. A commonly used IEF sample solution consists of 8 M urea, 4% CHAPS, 50-100 mM dithiothreitol (DTT), and 40 mM Tris. Furthermore, its small micellar molecular weight (6,150) and high critical micellar concentration (6 - 10 mM) allow it to be removed from samples by dialysis
Specifications
| Item | Value |
| Chemical Name | 3-[(3-Cholanidopropyl) Dimethylammonio]-1-Propane Sulfonate |
| Appearance | White Powder |
| CAS No. | 75621-03-3 |
| Molecular Formula | C32H58N2SO7 |
| Molecular Weight | 614.88 |
| Grade | Ultra Pure Grade |
| Purity | 98% |
| Nitrogen Content | 4.46~4.65% |
| Aqueous Solution (10% Dissolved in Water at 20℃) | Transparent, Colorless |
| Moisture | 2.0% |
| Thin Layer Chromatography | Single Spot |
| Conductivity | 5μs/cm |
Features
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Ultra‑pure, ≥ 98% grade — High chemical purity ensures minimal contaminants, ideal for rigorous biochemical and proteomic applications.
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Zwitterionic & non‑denaturing — Maintains native protein conformation while solubilizing membrane and other hydrophobic proteins.
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Efficient membrane protein solubilization — Effectively breaks protein–protein interactions and dissolves membrane-bound proteins, facilitating downstream analysis.
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High CMC and small micelle size (~6,150 Da) — Facilitates easy removal by dialysis, enabling further purification or functional assays without detergent interference.
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Compatible with IEF & 2D electrophoresis workflows — Frequently used at 1–4% (w/v) concentrations for non‑denaturing isoelectric focusing, even without urea, improving resolution for subcellular fractions or plant proteins.
Application
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Solubilization of integral membrane proteins while preserving native conformation and activity.
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Disruption of protein–protein interactions in cell lysates or subcellular fractions.
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Sample preparation for isoelectric focusing (IEF) and two-dimensional (2D) gel electrophoresis — especially non-denaturing (no-urea) IEF. Typical usage: 1–4% (w/v) in gel or sample buffer.
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Extraction and purification of membrane receptors and other functional membrane proteins for biochemical assays.
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Use in proteomic workflows, subcellular fractionation, and analysis of plant or animal tissue membrane proteins.
Warning
Toxicity: Harmful (C)
Reconstitution
Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 6 months at 4°C.
Publication
Chen, Y., et al. 1992. Biochemistry 31, 2415.
Ofri, D., et al. 1992. J. Neurochem. 58, 628.
Ransom, R.W., et al. 1992. Biochem. Pharmacol. 43, 1823.
Simonds, W.F., et al. 1992. Proc. Natl. Acad. Sci. USA77, 4623.
Yannariello-Brown, J., and Weigel, P.H. 1992. Biochemistry31, 576.
Hjelmeland, L.M. 1980. Proc. Natl. Acad. Sci. USA77, 6368.
Simonds, W.F., et al. 1980. Proc. Natl. Acad. Sci. USA77, 4623.
Safety Disclaimer
This product is intended for laboratory research use only. Not for drug, human, or veterinary use. Review the Safety Data Sheet (SDS) provided by BioFargo for detailed handling, storage, hazard, and disposal information. Use appropriate personal protective equipment (PPE) including gloves, lab coat, and eye protection when handling. Dispose of waste and residual buffer in accordance with local, state, and federal regulations. Ensure proper ventilation if preparing large volumes or heating solutions.
Documents
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