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Description
Luciferase ⅠProduct Specification Species Photinus pyralis Synonyms N. A Amino Acid Sequence N. A Expression System E. coli Molecular Weight 62kDa Purity >95% by SDS PAGE Conjugation Unconjugated Tag His Tag Physical Appearance Liquid Storage Buffer 25 mM Tris acetate (pH7. 8),1 mM EDTA, 1 mM DTT, 50% glycerol, 0. 2 M ammonium sulfate Reconstitution N. A Stability & Storage 12 months from date of receipt, 20 to 70 C as supplied; 6 months, 20 to 70 C under sterile
Product Specification
| Species | Photinus pyralis |
| Synonyms | N.A |
| Amino Acid Sequence | N.A |
| Expression System | E.coli |
| Molecular Weight | 62kDa |
| Purity | >95% by SDS-PAGE |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Liquid |
| Storage Buffer | 25 mM Tris-acetate (pH7.8),1 mM EDTA, 1 mM DTT, 50% glycerol, 0.2 M ammonium sulfate |
| Reconstitution | N.A |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied; 6 months, -20 to -70 °C under sterile conditions after reconstitution; 1 week, 2 to 8 °C under sterile conditions after reconstitution; Please avoid repeated freeze-thaw cycles. |
| Reference |
1.Mcelroy H H S D .THE COLORS OF FIREFLY BIOLUMINESCENCE: ENZYME CONFIGURATION AND SPECIES SPECIFICITY[J].Proceedings of the National Academy of Sciences of the United States of America, 1964, 52(1):75-81. 2.Conti E , Franks N P , Brick P .Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes[J].Structure, 1996, 4(3):287. |
Background
Luciferase is a general term for enzymes that produce biofluorescence in nature. Luciferase can catalyze the oxidation of luciferin to oxyluciferin. In the process of luciferin oxidation, biofluorescence is emitted. The biofluorescence released during the oxidation of luciferin can then be measured by a fluorometer. The Luciferase came from the firefly Photinus pyralis (Ppy) catalyzes a two-step reaction that results in the oxidation of D-luciferin accompanied by emission of yellow−green light with a peak at 560 nm. However, wild-luciferase activity is inhibited by sodium chloride, Therefore, the amino acid mutation we performed improved the inhibition of sodium chloride and was eventually named Luciferase Ⅰ.
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