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Name | 4-Aminoantipyrine |
Type | BioChemica |
CAS Number | 83-07-8 |
Molecular Formula | C11H13N3O |
Molecular Weight | 203.24 g/mol |
Appearance | White to off-white crystalline powder |
Melting Point | 168-171°C |
Solubility | Slightly soluble in water, soluble in ethanol and chloroform |
Storage Conditions | Store in a cool, dry place |
Usage | Used as an analytical reagent in the determination of hydrogen peroxide and phenols |
Handling Precautions | Avoid inhalation, ingestion, and contact with skin and eyes |
Synonyms | Aminophenazone, Aminoantipyrine, Benzohydrazide |
PubChem CID | 6968 |
FAQ
What is 4-Aminoantipyrine BioChemica and its significance in
biochemistry?
4-Aminoantipyrine BioChemica is a chemical compound widely used in biochemical studies. It is known for its role as a chromogenic substrate for peroxidase in enzyme-linked immunosorbent assays (ELISA) as well as in colorimetric determination of hydrogen peroxide. Its ability to form colored complexes makes it a valuable tool in various biochemical assays for detecting enzyme activity and quantifying analytes.
How is 4-Aminoantipyrine BioChemica used in enzyme-linked immunosorbent assays (ELISA)?
In ELISA, 4-Aminoantipyrine BioChemica is utilized as a chromogenic substrate for peroxidase enzymes. When the enzyme of interest is present, it catalyzes the oxidation of a substrate (e.g., hydrogen peroxide) and produces a colored end product. By adding 4-Aminoantipyrine BioChemica to the reaction mixture, the colorimetric change can be observed and quantified, providing a measurable signal that correlates with the presence or concentration of the target analyte.
What are the advantages of using 4-Aminoantipyrine BioChemica in biochemical assays?
One of the key advantages of using 4-Aminoantipyrine BioChemica is its sensitivity and specificity in detecting enzyme activity. The colorimetric reaction facilitated by this compound allows for quantification of enzyme-substrate interactions or detection of analytes with high precision. Additionally, 4-Aminoantipyrine BioChemica has a relatively simple protocol and does not require specialized equipment, making it accessible for researchers in various biochemical studies.
Can 4-Aminoantipyrine BioChemica be used in other applications besides ELISA?
Yes, besides ELISA, 4-Aminoantipyrine BioChemica has been employed in various colorimetric assays for detecting enzyme activity, quantifying analytes, and measuring oxidative stress markers. Its versatile nature makes it suitable for a range of biochemical studies where a colorimetric readout is desired. Researchers have successfully utilized this compound in fields such as clinical diagnostics, environmental monitoring, and drug discovery.
What makes 4-Aminoantipyrine BioChemica a valuable reagent in biochemistry research?
4-Aminoantipyrine BioChemica's unique properties as a chromogenic substrate for peroxidase enzymes and its compatibility with colorimetric detection methods make it a valuable reagent in biochemistry research. Its versatility, sensitivity, and ease of use have positioned it as a preferred choice for researchers looking to study enzyme kinetics, screen potential drug candidates, or monitor biological processes. By harnessing the power of 4-Aminoantipyrine BioChemica, scientists can advance their understanding of biochemical pathways and contribute to important discoveries in the field.
4-Aminoantipyrine BioChemica is a chemical compound widely used in biochemical studies. It is known for its role as a chromogenic substrate for peroxidase in enzyme-linked immunosorbent assays (ELISA) as well as in colorimetric determination of hydrogen peroxide. Its ability to form colored complexes makes it a valuable tool in various biochemical assays for detecting enzyme activity and quantifying analytes.
How is 4-Aminoantipyrine BioChemica used in enzyme-linked immunosorbent assays (ELISA)?
In ELISA, 4-Aminoantipyrine BioChemica is utilized as a chromogenic substrate for peroxidase enzymes. When the enzyme of interest is present, it catalyzes the oxidation of a substrate (e.g., hydrogen peroxide) and produces a colored end product. By adding 4-Aminoantipyrine BioChemica to the reaction mixture, the colorimetric change can be observed and quantified, providing a measurable signal that correlates with the presence or concentration of the target analyte.
What are the advantages of using 4-Aminoantipyrine BioChemica in biochemical assays?
One of the key advantages of using 4-Aminoantipyrine BioChemica is its sensitivity and specificity in detecting enzyme activity. The colorimetric reaction facilitated by this compound allows for quantification of enzyme-substrate interactions or detection of analytes with high precision. Additionally, 4-Aminoantipyrine BioChemica has a relatively simple protocol and does not require specialized equipment, making it accessible for researchers in various biochemical studies.
Can 4-Aminoantipyrine BioChemica be used in other applications besides ELISA?
Yes, besides ELISA, 4-Aminoantipyrine BioChemica has been employed in various colorimetric assays for detecting enzyme activity, quantifying analytes, and measuring oxidative stress markers. Its versatile nature makes it suitable for a range of biochemical studies where a colorimetric readout is desired. Researchers have successfully utilized this compound in fields such as clinical diagnostics, environmental monitoring, and drug discovery.
What makes 4-Aminoantipyrine BioChemica a valuable reagent in biochemistry research?
4-Aminoantipyrine BioChemica's unique properties as a chromogenic substrate for peroxidase enzymes and its compatibility with colorimetric detection methods make it a valuable reagent in biochemistry research. Its versatility, sensitivity, and ease of use have positioned it as a preferred choice for researchers looking to study enzyme kinetics, screen potential drug candidates, or monitor biological processes. By harnessing the power of 4-Aminoantipyrine BioChemica, scientists can advance their understanding of biochemical pathways and contribute to important discoveries in the field.