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| Name | DTT for Molecular Biology |
| Brand | Thermo Fisher Scientific |
| Product Type | Reagent |
| Application | Reduction and denaturation of disulfide bonds in proteins |
| Formulation | Powder |
| Purity | ≥99% |
| Storage Temperature | -20°C |
| Solubility | Soluble in water |
| Packaging | Bottle |
| Quantity | 5 grams |
| Shelf Life | 2 years |
| CAS Number | 3483-12-3 |
FAQ
What is DTT used for in molecular biology?
DTT, or dithiothreitol, is a reducing agent commonly used in molecular biology to break disulfide bonds in proteins. This helps to maintain proteins in a reduced state, preventing unwanted oxidization and maintaining protein function.
How does DTT work at the molecular level?
DTT functions by donating a pair of electrons to break the disulfide bonds between cysteine residues in proteins. This process reduces the formation of disulfide bridges, which can lead to protein aggregation and loss of protein activity.
What are some common applications of DTT in molecular biology?
DTT is commonly used in a variety of molecular biology techniques, including protein purification, enzyme assays, and protein refolding. It is also used to prevent oxidation in protein samples during storage and transport.
Can DTT be used in conjunction with other reagents or enzymes?
Yes, DTT is often used in combination with other reagents or enzymes to optimize experimental conditions. It can be used alongside protease inhibitors, chaotropic agents, or metal chelators to enhance protein stability and prevent degradation.
Are there any precautions or considerations to keep in mind when using DTT in molecular biology experiments?
It is important to handle DTT with care, as it can be harmful if ingested or inhaled. Additionally, DTT should be stored in a cool, dry place away from light to prevent degradation. It is also recommended to use freshly prepared DTT solutions for optimal results in molecular biology experiments.
DTT, or dithiothreitol, is a reducing agent commonly used in molecular biology to break disulfide bonds in proteins. This helps to maintain proteins in a reduced state, preventing unwanted oxidization and maintaining protein function.
How does DTT work at the molecular level?
DTT functions by donating a pair of electrons to break the disulfide bonds between cysteine residues in proteins. This process reduces the formation of disulfide bridges, which can lead to protein aggregation and loss of protein activity.
What are some common applications of DTT in molecular biology?
DTT is commonly used in a variety of molecular biology techniques, including protein purification, enzyme assays, and protein refolding. It is also used to prevent oxidation in protein samples during storage and transport.
Can DTT be used in conjunction with other reagents or enzymes?
Yes, DTT is often used in combination with other reagents or enzymes to optimize experimental conditions. It can be used alongside protease inhibitors, chaotropic agents, or metal chelators to enhance protein stability and prevent degradation.
Are there any precautions or considerations to keep in mind when using DTT in molecular biology experiments?
It is important to handle DTT with care, as it can be harmful if ingested or inhaled. Additionally, DTT should be stored in a cool, dry place away from light to prevent degradation. It is also recommended to use freshly prepared DTT solutions for optimal results in molecular biology experiments.
