General description

Sodium dodecyl sulfate (SDS), also known as sodium lauryl sulfate, is a versatile anionic surfactant with a broad range of applications in molecular biology, biochemistry, and various industries. Its amphiphilic nature, characterized by a hydrophobic hydrocarbon tail and a hydrophilic sulfate head group, makes it an effective detergent capable of solubilizing and denaturing proteins, lipids, and other hydrophobic molecules.

In protein biochemistry, SDS plays a pivotal role in protein extraction and SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis). Its ability to denature proteins by disrupting their secondary and tertiary structures allows for their uniform migration during gel electrophoresis, enabling the separation and analysis of proteins based on their molecular weight. This technique has become an indispensable tool for identifying and characterizing proteins in biological samples.

Beyond its role in protein analysis, SDS also finds utility in nucleic acid extraction and various hybridization techniques. Its detergent properties aid in the lysis of cells and the release of nucleic acids, facilitating their subsequent purification and analysis. Additionally, SDS is employed in hybridization techniques to promote the annealing of complementary nucleic acid strands, enabling the detection and analysis of specific DNA or RNA sequences.

Application

Sodium dodecyl sulfate has been used:

as an ionic surfactant in polystyrene (PS) particle suspension for surfactant-based experiments
in phosphate-buffered saline as a component of lysis buffer to homogenize myometrium and leiomyoma tissue
as a component of lysis buffer to dissolve formazans
as a component of high-salt nuclear extraction buffer

Anionic detergent

Biochem/physiol Actions

Sodium dodecyl sulfate (SDS) serves as an important detergent in the structural biology field and protein folding/unfolding studies. The sulfate groups and alkyl chains of SDS can strongly bind to the positively charged and the hydrophobic residues of proteins. SDS induces the formation of α-helices in a protein structure. At high concentrations, SDS stimulates cooperative unfolding in various proteins such as bovine serum albumin (BSA), hen egg-white lysozyme, -lactalbumin, and -lactoglobulin structures.

Features and Benefits

Suitable for molecular biology and biochemical research
BioUltra grade for your sensitive applications
Free from DNase, RNase, NICKase and protease
Tested for trace levels of Anions and Cations
Tested to confirm low levels of heavy metal contamination, ensuring suitability for various applications