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. Source: Recombinant protein corresponding to aa1-311 from renilla reniformis LUC, fused to His-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~38.5kD (335aa), confirmed by MALDI-TOF Biological Activity: Specific activity is >1X10e9 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH 7.5 at 25C. Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSHMTSKVY 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 Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
