Recombinant Renilla reniformis Luciferase His (N-Term) Protein

SDS-Page: Recombinant Firefly Luciferase Protein [NBP2-59648] - 15% SDS-PAGE (3ug)

• Reactivity: Rr
• Applications: PAGE, Enzyme Activity
• Concentration: 0.5 mg/ml

Recombinant Renilla reniformis Luciferase His (N-Term) Protein Summary

• Description: A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1-311 of Renilla reniformis Luciferase
  

  Source: E.coli

  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

• Details of Functionality: Specific activity is >1x10^9 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH7.5 at 25C.
• Source: E. coli
• Protein/Peptide Type: Recombinant Protein
• Purity: >95%, by SDS-PAGE

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
  • SDS-Page
• Theoretical MW: 38.5 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 10% glycerol
• Preservative: No Preservative
• Concentration: 0.5 mg/ml
• Purity: >95%, by SDS-PAGE

Alternate Names for Recombinant Renilla reniformis Luciferase His (N-Term) Protein

• Coelenterazine h 2-monooxygenase
• ec 1.13.12.7
• firefly luciferase
• Fluc
• LuC
• Luciferase
• luciferin 4 monooxygenase
• Luciferin 4-monooxygenase
• Renilla reniformis Luciferase
• Renilla-luciferin 2-monooxygenase
• Renilla-type luciferase

Background

Luciferase is a generic term for a group of oxidative enzymes used in bioluminescence. Firefly (Photinus pyralis) and bacterial luciferase enzymes are commonly used in assay systems such as cell viability assays, reporter gene assays, and for in vivo imaging. Bacterial luciferases are flavoenzymes composed of two subunits each encoded by the luxA and luxB genes, while the firefly luciferase is a single polypeptide specified by the luc gene (1). Firefly luciferase (theoretical molecular weight: 61 kDa) oxidizes the substrate luciferin to oxyluciferin in a bioluminescent reaction requiring Mg2+ and ATP (2,3). This reaction produces a flash of yellow-green light with an emission peak around 560nm that can be detected by a luminometer (3). Firefly luciferase has become one of the more widely used reporter proteins and is an excellent tool for the study of gene expression, given that the amount of light emitted is directly proportional to luciferase activity (4).

The luciferase assay is fast and sensitive, differentiating itself from the CAT (chloramphenicol acetyltransferase) assay because it does not require a radioactive substrate.

References

1. Eun, H. (1996). Marker/Reporter enzymes. Enzymology Primer for Recombinant DNA Technology, 567-645. doi:10.1016/b978-012243740-3/50011-9

2. McNabb, D. S., Reed, R., & Marciniak, R. A. (2005). Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae. Eukaryotic Cell, 4(9), 1539-1549. doi:10.1128/ec.4.9.1539-1549.2005

3. Fraga, H. (2008). Firefly luminescence: A historical perspective and recent developments. Photochemical & Photobiological Sciences, 7(2), 146-158. doi:10.1039/b719181b

4. Younes, A., Lukyanenko, Y. O., Lyashkov, A. E., Lakatta, E. G., & Sollott, S. J. (2011). A bioluminescence method for direct measurement of phosphodiesterase activity. Analytical Biochemistry, 417(1), 36-40. doi:10.1016/j.ab.2011.05.036

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.