2-Nitrophenyl β-D-galactopyranoside (ONPG)
99%, non-animal origin
- Product Code: 58060
Alias:
2-nitrophenyl-β-D-galactopyranoside (ONPG); o-nitrophenyl-β-D-galactopyranoside
CAS:
369-07-3
| Molecular Weight: | 301.25 g./mol | Molecular Formula: | C₁₂H₁₅O₈N |
|---|---|---|---|
| EC Number: | 206-716-1 | MDL Number: | MFCD00063255 |
| Melting Point: | 186-193 °C (dec.) | Boiling Point: | |
| Density: | Storage Condition: | 2~8°C |
Product Description:
Used primarily as a substrate in biochemistry and molecular biology to detect the presence of β-galactosidase enzyme activity. When the enzyme cleaves the glycosidic bond, it releases o-nitrophenol, which turns yellow and can be measured spectrophotometrically at 420 nm. This makes it a valuable tool in assays for gene expression studies, particularly in lacZ reporter systems. It is also employed in microbiology to identify and differentiate bacterial species based on their ability to produce β-galactosidase. Additionally, it aids in studying enzyme kinetics and inhibition mechanisms.
Product Specification:
| Test | Specification |
|---|---|
| PURITY | 98.5 |
| APPEARANCE | WHITE TO PALE YELLOW SOLID |
| MELTING POINT | 185-195 |
Sizes / Availability / Pricing:
| Size (g) | Availability | Price | Quantity |
|---|---|---|---|
| 1.000 | 10-20 days | ฿970.00 |
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| 5.000 | 10-20 days | ฿2,850.00 |
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| 25.000 | 10-20 days | ฿8,700.00 |
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| 100.000 | 10-20 days | ฿31,200.00 |
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2-Nitrophenyl β-D-galactopyranoside (ONPG)
Used primarily as a substrate in biochemistry and molecular biology to detect the presence of β-galactosidase enzyme activity. When the enzyme cleaves the glycosidic bond, it releases o-nitrophenol, which turns yellow and can be measured spectrophotometrically at 420 nm. This makes it a valuable tool in assays for gene expression studies, particularly in lacZ reporter systems. It is also employed in microbiology to identify and differentiate bacterial species based on their ability to produce β-galactosidase. Additionally, it aids in studying enzyme kinetics and inhibition mechanisms.
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