Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) is a cornerstone technique for separating proteins based on their molecular weight. However, the effectiveness of SDS-PAGE relies heavily on the complete denaturation of proteins, a process that requires breaking both non-covalent interactions and disulfide bonds. This is where DL-Dithiothreitol (DTT), also known as Cleland's reagent, becomes an indispensable component. As a leading manufacturer of high-purity biochemicals, we understand the critical role DTT plays in achieving reliable protein analysis.

Disulfide bonds, formed between cysteine residues within or between protein chains, contribute significantly to a protein's three-dimensional structure. If these bonds remain intact during SDS-PAGE sample preparation, proteins may not fully unfold, leading to aberrant migration patterns and inaccurate molecular weight estimations. DTT acts as a powerful reducing agent, efficiently cleaving these disulfide linkages, thereby ensuring that proteins are linearized and coated uniformly with SDS. This allows for precise separation solely by size.

When researchers decide to buy DTT for SDS-PAGE, selecting a product with high purity is paramount. Impurities in DTT can interfere with the reduction process or introduce unwanted artifacts into the gel. Our DL-Dithiothreitol is manufactured to strict quality standards, boasting a purity of ≥98%, making it an ideal choice for researchers demanding accuracy and reproducibility. We are a trusted DTT supplier in China, committed to providing biochemicals that meet the highest performance benchmarks.

The concentration of DTT used in SDS-PAGE sample buffers typically ranges from 50 mM to 100 mM. While effective, it's important to note that DTT can be oxidized over time, especially when stored as a solution. Therefore, preparing fresh DTT solutions or storing them properly under inert conditions is recommended. If you are looking to purchase Cleland's reagent, considering our reliable supply and consistent quality will ensure your SDS-PAGE experiments are consistently successful. We offer competitive DTT prices, making high-quality protein denaturation accessible for all laboratories.

In conclusion, DL-Dithiothreitol is a critical reagent for achieving proper protein denaturation in SDS-PAGE. Its ability to efficiently reduce disulfide bonds ensures accurate protein separation. By choosing high-purity DTT from a reputable DTT manufacturer, researchers can guarantee the integrity and reliability of their results. If your laboratory requires this essential biochemical, we are your trusted partner for quality and supply.