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| Product Name | IPTG BioChemica |
| Supplier | BioChemica |
| Chemical Name | Isopropyl β-D-1-thiogalactopyranoside |
| Purity | ≥99% |
| Form | Powder |
| Appearance | White to off-white crystalline powder |
| Solubility | Soluble in water |
| Storage Condition | Store at -20°C |
| Usage | Inducer of β-galactosidase in molecular biology applications |
| Molecular Weight | 238.3 g/mol |
| Cas Number | 367-93-1 |
FAQ
What is IPTG BioChemica and how is it used in research?
IPTG BioChemica is a chemical compound used in molecular biology research to induce protein expression from recombinant plasmids in bacterial cells. It is a synthetic analog of the natural sugar lactose that binds to the lac repressor protein, allowing the transcription of genes under the control of the lac operon.
What are the advantages of using IPTG BioChemica in protein expression studies?
IPTG BioChemica is preferred for protein expression studies as it is non-metabolizable by most bacteria, ensuring that it remains stable in the growth medium. It also has a high affinity for the lac repressor protein, resulting in efficient induction of gene expression. Additionally, IPTG BioChemica is easy to use and cost-effective, making it a popular choice for researchers.
How is IPTG BioChemica typically added to bacterial cultures for protein expression experiments?
IPTG BioChemica is usually added to bacterial cultures at a final concentration of 0.1-1.0 mM to induce protein expression. This concentration can be optimized based on the specific recombinant plasmid and bacterial strain being used. IPTG BioChemica is typically added to the growth medium at the time of inoculation or during the mid-log phase of bacterial growth.
Are there any potential drawbacks or limitations associated with the use of IPTG BioChemica in protein expression studies?
While IPTG BioChemica is widely used in protein expression studies, there are some limitations to consider. Some bacterial strains may exhibit leaky expression in the presence of IPTG BioChemica, resulting in background protein expression even in the absence of induction. Additionally, high concentrations of IPTG BioChemica can be toxic to bacterial cells, leading to reduced cell viability and protein yield.
What are some alternative methods for inducing protein expression in bacterial cells besides using IPTG BioChemica?
In addition to IPTG BioChemica, other chemical inducers such as arabinose and rhamnose can be used to induce protein expression in bacterial cells. Alternatively, temperature-sensitive promoters or auto-induction media can be employed to regulate gene expression without the need for chemical inducers. Each method has its advantages and limitations, so researchers should choose the most suitable method based on their specific experimental needs.
IPTG BioChemica is a chemical compound used in molecular biology research to induce protein expression from recombinant plasmids in bacterial cells. It is a synthetic analog of the natural sugar lactose that binds to the lac repressor protein, allowing the transcription of genes under the control of the lac operon.
What are the advantages of using IPTG BioChemica in protein expression studies?
IPTG BioChemica is preferred for protein expression studies as it is non-metabolizable by most bacteria, ensuring that it remains stable in the growth medium. It also has a high affinity for the lac repressor protein, resulting in efficient induction of gene expression. Additionally, IPTG BioChemica is easy to use and cost-effective, making it a popular choice for researchers.
How is IPTG BioChemica typically added to bacterial cultures for protein expression experiments?
IPTG BioChemica is usually added to bacterial cultures at a final concentration of 0.1-1.0 mM to induce protein expression. This concentration can be optimized based on the specific recombinant plasmid and bacterial strain being used. IPTG BioChemica is typically added to the growth medium at the time of inoculation or during the mid-log phase of bacterial growth.
Are there any potential drawbacks or limitations associated with the use of IPTG BioChemica in protein expression studies?
While IPTG BioChemica is widely used in protein expression studies, there are some limitations to consider. Some bacterial strains may exhibit leaky expression in the presence of IPTG BioChemica, resulting in background protein expression even in the absence of induction. Additionally, high concentrations of IPTG BioChemica can be toxic to bacterial cells, leading to reduced cell viability and protein yield.
What are some alternative methods for inducing protein expression in bacterial cells besides using IPTG BioChemica?
In addition to IPTG BioChemica, other chemical inducers such as arabinose and rhamnose can be used to induce protein expression in bacterial cells. Alternatively, temperature-sensitive promoters or auto-induction media can be employed to regulate gene expression without the need for chemical inducers. Each method has its advantages and limitations, so researchers should choose the most suitable method based on their specific experimental needs.
