In the fields of molecular biology, biochemistry, and proteomics, understanding protein structure and function is fundamental. A key challenge in this research is managing protein integrity, particularly disulfide bonds which can significantly influence a protein's folding and activity. 2-Mercaptoethanol (BME) emerges as an indispensable tool for researchers due to its potent reducing capabilities, acting to cleave these vital disulfide bonds. As a dedicated supplier of biochemical reagents, we provide researchers with the high-quality 2-Mercaptoethanol they need for accurate analysis.

Disulfide bonds (S-S) are covalent bonds formed between the thiol groups of two cysteine residues within a protein. These bonds are crucial for stabilizing tertiary and quaternary protein structures. However, for certain analytical techniques, such as SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis), it is necessary to break these bonds to ensure proteins migrate according to their subunit molecular weights and to prevent aggregation.

2-Mercaptoethanol achieves this by donating hydrogen atoms, effectively reducing the disulfide bonds into free sulfhydryl groups (-SH). This process helps in denaturing proteins and separating subunits. While other reducing agents exist, 2-Mercaptoethanol is often favored for its effectiveness and is commonly included in sample preparation buffers. Its utility extends to preventing oxidation of free sulfhydryl groups, thus maintaining protein activity in enzymatic reactions and assays.

For research laboratories requiring reliable biochemicals, sourcing pure 2-Mercaptoethanol is essential. We offer 2-Mercaptoethanol that meets high purity standards, ensuring consistent and reproducible results in your experiments. If you are looking to buy 2-Mercaptoethanol for your laboratory needs, whether for protein structure analysis, enzyme stabilization, or other biochemical applications, we are your trusted partner. Contact us today for competitive pricing and detailed technical specifications.