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Description
Luciferase ⅡProduct Specification Species Photinus pyralis Amino Acid Sequence N. A Expression System E. coli Molecular Weight 61. 7kDa Purity >95% by SDS PAGE Conjugation Unconjugated Tag His Tag Physical Appearance Liquid Storage Buffer 20 mM Tris (pH7. 4), 1 mM EDTA, 1 mM DTT, 50% glycerol Reconstitution 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
Product Specification
| Species | Photinus pyralis |
| Amino Acid Sequence | N.A |
| Expression System | E.coli |
| Molecular Weight | 61.7kDa |
| Purity | >95% by SDS-PAGE |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Liquid |
| Storage Buffer | 20 mM Tris (pH7.4), 1 mM EDTA, 1 mM DTT, 50% glycerol |
| Reconstitution | |
| 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. In our work, 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, some biological applications are limited by the low stability of the luciferase, so we combined amino acid mutations to enhance the enzyme’s thermostability and was eventually named Luciferase Ⅱ.
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