n111,luciferase,virus,sensitive,gaussia,metridia,renilla,firefly,oplophorus,reporter,nanoglo,nanoluc,response element,nuclear factor, kappaB, minimal promoter
NanoLuc (Nluc) luciferase is a 19.1kDa luminescent reporter enzyme that is about 100-fold brighter than either firefly or Renilla luciferase. Use the pNL3.2.NF-?B-RE[NlucP/NF-?B-RE/Hygro] Vector to measure changes in the levels of NF-kappaB in cells.
NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. The enzyme is about 100-fold brighter than either firefly (Photinus pyralis) or Renilla reniformis luciferase using a novel substrate, furimazine, to produce high intensity, glow-type luminescence. The luminescent reaction is ATP-independent and designed to suppress background luminescence for maximal assay sensitivity. For use as a genetic reporter, multiple forms of NanoLuc luciferase have been configured to meet differing experimental objectives. NanoLuc-PEST (NlucP) present in pNL3.2.NF-?B-RE[NlucP/NF-?B-RE/Hygro] Vector closely couples protein expression to changes in transcriptional activity and increased signal-to background ratios. Use the pNL3.2.NF-?B-RE[NlucP/NF-?B-RE/Hygro] Vector to assess the response to cellular changes in the nuclear factor kappaB. Luminescence is linearly proportional to the amount of NanoLuc protein over a 1,000,000-fold concentration range, with a signal half-life >/=2 hours when detected with Nano-Glo Luciferase Assay Reagent. NanoLuc luciferase possesses a number of physical properties that make it an excellent reporter protein: 1) very small, monomeric enzyme (171 amino acids; 513bp); 2) high thermal stability (Tm = 60