In the realm of biochemistry, understanding the intricate structures and functions of molecules is key. Among the essential biochemical reagents, Dithiothreitol (DTT), also known by its IUPAC name DL-1,4-Dithio-DL-threitol or as Cleland's reagent, holds a prominent position due to its exceptional reducing capabilities. Its primary function revolves around the efficient reduction of disulfide bonds, which are critical for protein structure and function.

Disulfide bonds, formed by the oxidation of two thiol groups, primarily from cysteine residues, play a vital role in stabilizing the tertiary and quaternary structures of proteins. However, for many experimental procedures, these bonds need to be broken to allow for proper protein unfolding, analysis, or to maintain specific protein activities. This is where DTT excels. It acts as a powerful reducing agent, donating electrons and breaking the S-S covalent bonds to form two free sulfhydryl (-SH) groups. This process is a hallmark of its utility in biochemistry.

The chemical properties of DTT contribute to its effectiveness. It is highly soluble in water, forming clear solutions, and possesses a potent reducing potential of -0.33 V at pH 7. This allows it to readily participate in thiol-disulfide exchange reactions. For researchers seeking to buy DL-Dithiothreitol 3483-12-3, understanding these properties ensures they are acquiring a reagent suitable for tasks like protein denaturation prior to SDS-PAGE, preventing protein aggregation during purification, and as an antioxidant in various assays.

Compared to its predecessor, 2-mercaptoethanol, DTT offers several advantages. It is less volatile, has a lower odor, and generally requires lower working concentrations. Its use in preventing disulfide bonds from forming between cysteine residues is crucial for maintaining the correct conformation of many proteins. The advice on DTT storage and stability is important; while the powder form is relatively stable when stored properly, solutions are less stable and should ideally be prepared fresh for each use.

The applications of DTT extend beyond protein chemistry. It is utilized in the stabilization of enzymes, acting as an antioxidant to protect critical sulfhydryl groups. In molecular biology, it plays a role in nucleic acid extraction by helping to inactivate RNases, thus preserving RNA integrity. The versatility of DTT underscores its importance as a fundamental reagent for biochemical research.

NINGBO INNO PHARMCHEM CO.,LTD. provides high-quality DL-Dithiothreitol, enabling scientists to confidently perform experiments requiring precise disulfide bond reduction and protein stabilization. By utilizing reliable biochemical reagents like DTT, researchers can achieve more accurate and reproducible results in their groundbreaking scientific endeavors.