TAPS
[CAS# 29915-38-6]

Identification

• Classification: Chemical reagent >> Organic reagent >> Sulfonic acid / sulfinic acid
• Name: TAPS
• Synonyms: 3-[[2-Hydroxy-1,1-bis(hydroxymethyl)ethyl]amino]-1-propanesulfonic acid; 3-[Tris(hydroxymethyl)methylamino]-1-propanesulfonic acid
• Molecular Formula: C₇H₁₇NO₆S
• Molecular Weight: 243.27
• CAS Registry Number: 29915-38-6
• EC Number: 249-954-1
• SMILES: C(CNC(CO)(CO)CO)CS(=O)(=O)O

Properties

• Melting point: 230-235 °C (dec.)
• Water solubility: Soluble

Safety Data

• Hazard Symbols: GHS07 Warning
• Risk Statements: H302-H315-H319-H335
• Safety Statements: P261-P305+P351+P338

Hazard Classification

Hazard	Class	Category Code	Hazard Statement
Specific target organ toxicity - single exposure	STOT SE	3	H335
Skin irritation	Skin Irrit.	2	H315
Eye irritation	Eye Irrit.	2	H319
Acute toxicity	Acute Tox.	4	H302
Acute toxicity	Acute Tox.	4	H312

Discovery and Applications

TAPS (N-Tris(hydroxymethyl)methyl-3-aminopropanesulfonic acid) is a zwitterionic buffer that was discovered by Norman E. Good and colleagues in the 1960s. The impetus for the development of TAPS and other Good buffers stemmed from the need for stable, non-interfering buffers in biochemical and biological research. Good buffers are designed to maintain a consistent pH during an experiment, even in the presence of biological activity or temperature changes, which is essential for obtaining accurate and reproducible results.

The molecular formula of TAPS is C7H17NO6S and its molecular weight is 243.28 g/mol. It has a sulfonic acid group and three hydroxymethyl groups attached to the nitrogen atom, which give it zwitterionic properties. This structure gives TAPS a high buffering capacity and low ionic strength, making it particularly useful in biological and biochemical applications. TAPS has a pKa of 8.4 at 25°C, making it an excellent buffer for pH values ​​between 7.7 and 9.1.

TAPS is widely used in biochemical and molecular biology laboratories. Its high buffering capacity makes it ideal for maintaining pH stability during enzymatic reactions, electrophoresis, and protein purification. Researchers rely on TAPS to ensure that experimental conditions remain consistent, which is critical to obtaining accurate and reproducible data.

In electrophoresis, TAPS is used as a buffer for the separation of nucleic acids and proteins. Its ability to maintain a stable pH during electrophoresis ensures that the molecules being separated migrate properly, resulting in clear and interpretable results. This application is particularly important in techniques such as SDS-PAGE and agarose gel electrophoresis.

TAPS is also used in cell culture media to maintain the desired pH, ensuring optimal growth conditions for cells. Its non-toxicity and compatibility with a wide range of cell types make it a preferred buffer in a variety of cell culture applications. By providing a stable environment, TAPS helps achieve consistent and reliable results in cell biology research.

In chromatography, TAPS is used as a buffer in the mobile phase to control pH and ionic strength, which are critical parameters for the separation of biomolecules. Its stability and compatibility with different chromatographic media make it suitable for analytical and preparative chromatography, helping to purify and analyze proteins, peptides, and other biomolecules.

TAPS is used in a variety of biochemical assays where maintaining a stable pH is critical for the activity and stability of enzymes and other biomolecules. Its buffering capacity ensures that assay conditions remain optimal, allowing for accurate and reliable measurements of biochemical activity.

TAPS maintains a stable pH over a wide range of conditions, ensuring consistent experimental results. The low ionic strength makes TAPS compatible with a wide range of biological systems and techniques without interfering with the process being studied. TAPS is generally nontoxic to cells and does not interfere with biochemical reactions, making it suitable for sensitive biological applications.

References

2008. Quinone reductase acts as a redox switch of the 20S yeast proteasome. The EMBO Reports, 9(12).
DOI: 10.1038/embor.2008.218

2005. Detection of prion protein using a capillary electrophoresis-based competitive immunoassay with laser-induced fluorescence detection and cyclodextrin-aided separation. ELECTROPHORESIS, 26(9).
DOI: 10.1002/elps.200410202

2021. Molecular Cloning, Purification and Characterization of Mce1R of Mycobacterium tuberculosis. Molecular Biotechnology, 63(4).
DOI: 10.1007/s12033-020-00293-5