Recombinant renilla reniformis Luciferase-eiwit

LUC, also known as luciferase. LUC catalyzes the oxidative decarboxylation of coelenterazine in the presence of dissolvedoxygen to yield oxyluciferin, CO2, and blue light. In vivo, the excited state luciferin-luciferase complex undergoes the process of noradiative energy transfer to an accessory protein, green fluorescent protein, which results in green bioluminescence. In vitro, it emits blue light in the absence of any green fluorescent protein. Recombinant renilla reniformis LUC, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Specific activity is >1x10^9 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH7.5 at 25C.

Luciferase

E.coli

Renilla reniformis

His-Tag

SDS-PAGE, Enzyme Activity

0.5 mg/mL (determined by Bradford assay)

< 1 EU per 1ug of protein (determined by LAL method)

> 95% by SDS-PAGE

Specific activity is >1X10^9 lightunit/mg. One luciferase enzymeunit will produce one Relative Light Unit (RLU) at pH7.5 at 25C.

38.5 kDa (335aa) Confirmed by MALDI-TOF

Luciferase, Luciferase, ATGP3581-10 µg, ATGP3581-20 µg, ATGP3581-50 µg, ATGP3581-100 µg, ATGP3581-250 µg, ATGP3581-500 µg, ATGP3581-1 mg, ATGP3581-10, ATGP3581-20, ATGP3581-50, ATGP3581-100, ATGP3581-250, ATGP3581-500, ATGP3581-1

Lorenz WW., et al. (1991) Proc Natl Acad Sci U S A. 88 (10) :4438-42.

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol

Enzymes & Proteases

AAA29804.1

P27652

Renilla reniformis

MTSKVY DPEQRKRMIT GPQWWARCKQ MNVLDSFINY YDSEKHAENA VIFLHGNAAS SYLWRHVVPH IEPVARCIIP DLIGMGKSGK SGNGSYRLLD HYKYLTAWFE LLNLPKKIIF VGHDWGACLA FHYSYEHQDK IKAIVHAESV VDVIESWDEW PDIEEDIALI KSEEGEKMVL ENNFFVETML PSKIMRKLEP EEFAAYLEPF KEKGEVRRPT LSWPREIPLV KGGKPDVVQI VRNYNAYLRA SDDLPKMFIE SDPGFFSNAI VEGAKKFPNT EFVKVKGLHF SQEDAPDEMG KYIKSFVERV LKNEQ