Rabbit Monoclonal LUCI antibody - conjugated to Alexa Fluor® 594.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Upon binding the substrate, the enzyme catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO(2) molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
Coelenterazine h 2-monooxygenase, Renilla-luciferin 2-monooxygenase, Renilla-type luciferase
Rabbit Monoclonal LUCI antibody - conjugated to Alexa Fluor® 594.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
Renilla Luciferase also known as RLuc is an enzyme that catalyzes the oxidation of its substrate coelenterazine producing bioluminescence. With a molecular mass of approximately 36 kDa RLuc facilitates this reaction by oxygenation resulting in the emission of blue light. Renilla Luciferase is typically isolated from the sea pansy Renilla reniformis and has been widely used as a reporter gene in molecular biology for monitoring gene expression and cellular events due to its efficient light production.
Renilla Luciferase operates as part of the bioluminescent system found in certain marine organisms. In its native environment it interacts with other proteins like Green Fluorescent Protein (GFP) to which it transfers energy converting blue light to green fluorescence. This process of bioluminescence serves various ecological functions including predator avoidance and communication between organisms. These interactions highlight the importance of Renilla Luciferase in understanding biological luminescence systems.
Researchers use Renilla Luciferase extensively in signaling and metabolic pathway analyses. It plays an important role in the study of G-protein coupled receptor (GPCR) pathways where it can help to analyze receptor activation and downstream communication. In these pathways it often pairs with other luminescent or fluorescent markers like Firefly Luciferase or GFP enabling simultaneous dual-reporter assays to provide more comprehensive data on cellular responses.
Renilla Luciferase aids in the study of cancer and infectious diseases. Its role in reporter assays facilitates the investigation of gene expression changes and the screening of potential therapeutic compounds. For example in cancer research it is frequently paired with p53 proteins for studying apoptosis and cell cycle regulation. Similarly in infectious disease studies Renilla Luciferase reporters can track viral infections and the efficacy of antiviral drugs. These applications highlight its value in advancing biomedical research and drug development.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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