Gaussia(M2)-Luciferase-Streptavidin is a conjugate of one of the brightest luciferases and a protein with the highest known affinity in nature. This fusion protein can be used to detect trace amounts of biotinylated protein, DNA, or other biotinylated bio-molecules.
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Appearance clear liquid as 1 mg/ml in buffer, aliquoted as 50 µg
In experiments we were able to visualize the GLuc luminescence on the surface of Agarose-Biotin beads using a standard light microscope in total darkness. GLuc-SA was engineered by connecting one molecule of GLuc to one Streptavidin subunit. Streptavidin consists of 4 subunits with theoretically 4 biotin binding sites. Purified Streptavidin will have the ability to bind between 3.2 and 3.9 biotin molecules. Due to extensive purification steps, no free Streptavidin is present and cross-linking will be prevented, enabling quantitative read-outs in luminescent assays.
- bioluminescent detection of biotinylated biomolecules (protein, DNA, peptides) in ELISA-style assays
- wide dynamic range
- low background (no interfering BSA/FCS is used in this reagent)
- highly sensitive
- strong biotin binding
- bioluminescent surface labeling generating high signal/noise ratios
- overcoming problems like autofluorescence
- recommended equipment (Olympus LV-200)
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