![]() ![]() Application Measurement Modes - Quantitative Analysis, Color, PLS, Kinetics, 2-D/3-D analysis.Acquire Modes - Spectral measurement, Time Course measurement, and Photometric measurement. ![]() Compact - The MultiSpec offers the compact design needed for today's laboratories.The simplified optical design results in consistent and stable measurements. Simple - The drive mechanics have been minimized.Including processing time, the full wavelength range spectrum is displayed in approximately 1 second. Fast - High-speed 0.1 second measurement in the time course or monitoring mode, making it ideal for on-line processes or stop-flow kinetic assays.An optional pass/fail indicator makes it ideal for any quality control environment. Time course data can be displayed in 2-dimensional or 3-dimensional plots, allowing the user to quickly determine any change in absorbance over the entire wavelength region. It can perform an array of different quantitative analyses including multiple linear regression, PLS, calibration curves, custom equations, color, kinetics and more. And of course, the software also runs under Windows® 3.1. The MultiSpec-1501 uses powerful PC-based software (Hyper-UV) running under Windows® 95 for control of the instrument. This spectrophotometer brings wavelength scanning into a new era. Just place the sample in the roomy, open sample chamber and click the start button. The MultiSpec-1501, with the newest optical and computer software technology, satisfies the demands of accurate and reproducible results, high-speed productivity and compact size. The energy from the dispersed light is measured almost simultaneously by a highly-sensitive 512 element diode array. The MultiSpec-1501 can acquire spectra over the entire wavelength range in just 100 milliseconds. iLOV, therefore, offers greater utility in FP-tagging of viral gene products and represents a viable alternative where functional protein expression is limited by steric constraints or genome size.In the time it takes you to read this headline, a spectral scan can be performed. When expressed either as a cytosolic protein or as a viral protein fusion, iLOV functioned as a superior reporter to GFP for monitoring local and systemic infections of plant RNA viruses. Moreover, iLOV fluorescence was found to recover spontaneously after photobleaching and displayed an intrinsic photochemistry conferring advantages over GFP-based FPs. One variant in particular, designated iLOV, possessed photophysical properties that made it ideally suited as a reporter of subcellular protein localization in both plant and mammalian cells. Molecular evolution and Tobacco mosaic virus (TMV)-based expression screening produced LOV variants with improved fluorescence and photostability in planta. To overcome this, we have engineered a smaller (≈10 kDa) flavin-based alternative to GFP (≈25 kDa) derived from the light, oxygen or voltage-sensing (LOV) domain of the plant blue light receptor, phototropin. However, FP-tagging of viruses is limited by the constraints of viral genome size resulting in FP loss through recombination events. Fluorescent proteins (FPs) based on green fluorescent protein (GFP) are widely used throughout cell biology to study protein dynamics, and have extensive use as reporters of virus infection and spread. ![]()
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