Blp01 488r 25

Manufactured by IDEX Corporation

The BLP01-488R-25 is a laser module that produces a 488 nm wavelength beam with an output power of 25 mW. It is designed for use in various laboratory applications.

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Lab products found in correlation

N storm, by Nikon (1 mentions) Du 897e cs0bv, by Oxford Instruments (1 mentions) Te2000, by Nikon (1 mentions) Apo lwd 25x, by Nikon (1 mentions) Cfi plan fluor 10x, by Nikon (1 mentions) Blp02 561r 25, by IDEX Corporation (1 mentions) Ixon3 897, by Oxford Instruments (1 mentions) Blp01 488r, by IDEX Corporation (1 mentions) Nanomax, by Thorlabs (1 mentions) Avaspec 2048, by Avantes (1 mentions) Ff01 480 40 25, by IDEX Corporation (1 mentions) Ff01 676 37 25, by IDEX Corporation (1 mentions) Di01 r405 488 561 635, by IDEX Corporation (1 mentions) Plan apo, by Nikon (1 mentions) Eclipse te2000 u, by Nikon (1 mentions) L15 buffer, by Thermo Fisher Scientific (1 mentions) Ff01 520 44 25, by IDEX Corporation (1 mentions) Ionomycin, by Merck Group (1 mentions)

8 protocols using blp01 488r 25

Super-Resolution FPALM Imaging Protocol

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FPALM imaging was performed on a super-resolution microscope NIKON N-STORM equipped with a 100X 1.40 NA Nikon objective lend and an Andor Ixon DU-897E-CS0BV running at approximately 30 Hz (30 ms exposure time). The excitation scheme consisted of an activation laser at 405 nm (Coherent CUBE 405–100 mW) and a readout laser at 488 nm (Coherent Sapphire OPSL 488 nm-50 mW). Specific dichroic mirrors (Chroma, T505LP) and band-pass dichroic filters allowed selection of the emitted signal (Semrock BLP01-488R-25).
The molecules position is found, after background subtraction and thresholding, by means of a gaussian fitting procedure. The rendering of the super-resolution image is obtained plotting the position of each single event as a gaussian spot with standard deviation corresponding to the calculated localization precision. Before the rendering of the final image, a filter on brightness and molecule dimension is applied and unsuitable events are rejected [7] (link).

Pennacchietti F., Abbruzzetti S., Losi A., Mandalari C., Bedotti R., Viappiani C., Zanacchi F.C., Diaspro A, & Gärtner W. (2014). The Dark Recovery Rate in the Photocycle of the Bacterial Photoreceptor YtvA Is Affected by the Cellular Environment and by Hydration. PLoS ONE, 9(9), e107489.

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Automated Widefield Epifluorescence Microscopy

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We performed the experiments with an automated widefield epifluorescence microscope (Nikon TE2000). We custom modified the scope to provide two additional modes of imaging: epi-illuminated pattern projection and LED gated transmitted light. We imaged light patterns from a programmable DLP chip (EKB TEchnologies DLP LightCrafter E4500 MKIITM Fiber Couple) onto the sample through a user-modified epi-illumination attachment (Nikon T-FL). The DLP chip was illuminated by a fiber coupled 470 nm LED (ThorLabs M470L3). The epi-illumination attachment had two light-path entry ports, one for the projected pattern light path and the other for a standard widefield epi-fluorescence light path. The two light paths were overlapped with a dichroic mirror (Semrock BLP01-488R-25). The magnification of the epi-illuminating system was designed so that the imaging sensor of the camera (FliR BFLY-U3-23S6M-C) was fully illuminated when the entire DLP chip was on. Experiments were run with Micro-Manager (Edelstein et al., 2010 (link)), running custom scripts to controlled pattern projection and stage movement.

Banks R.A., Galstyan V., Lee H.J., Hirokawa S., Ierokomos A., Ross T.D., Bryant Z., Thomson M, & Phillips R. (2023). Motor processivity and speed determine structure and dynamics of microtubule-motor assemblies. eLife, 12, e79402.

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High-resolution live cell imaging with SPIM

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Fluorescence-based live imaging was carried out on a MuVI SPIM (Krzic et al., 2012 (link)). Briefly, the optics consisted of two detection and illumination arms. Each detection arm forms a water-dipping epifluorescence microscope, consisting of an objective (Apo LWD 25x, NA 1.1, Nikon Instruments Inc.), a filter wheel (HS-1032, Finger Lakes Instrumentation LLC), with emission filters (BLP01-488R-25, BLP02-561R-25, Semrock Inc.), tube lens (200 mm, Nikon Instruments Inc.), and an sCMOS camera (Zyla 4.2, Andor Technology plc.), with an effective pixel size of 0.26 µm. Each illumination arm consisted of a water-dipping objective (CFI Plan Fluor 10x, NA 0.3), a tube lens (200 mm, both Nikon Instruments Inc.), a scan lens (S4LFT0061/065, Sill optics GmbH and Co. KG), and a galvanometric scanner (6215 hr, Cambridge Technology Inc.), fed by lasers (06-MLD 488 nm, Cobolt AB, and 561LS OBIS 561 nm, Coherent Inc.). Optical sectioning is achieved by translating the sample using a linear piezo stage (P-629.1cd with E-753 controller) sample rotation is performed with a rotational piezo stage (U-628.03 with C-867 controller) and a linear actuator (M-231.17 with C-863 controller, all Physik Instrumente GmbH and Co. KG).

Streichan S.J., Lefebvre M.F., Noll N., Wieschaus E.F, & Shraiman B.I. (2018). Global morphogenetic flow is accurately predicted by the spatial distribution of myosin motors. eLife, 7, e27454.

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Fluorescence Microscope Characterization of Fabricated Structures

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The fabricated structures were imaged and characterized using a custom-built fluorescence microscope, which is shown in Supplementary Fig. S8. The setup contains a 473 nm diode laser (RLTMBL-473-150-10, Roithner Lasertechnik GmbH), a 470 nm LED (Osram), an excitation filter (FF02-470/100, Semrock), two achromatic lenses (f = 200 mm, Thorlabs), a dichroic mirror (FF484-Fdi01, Semrock), objective lens (HCX PL APO, 1.4 NA, 100×, Leica), a manually controlled stage (Nanomax, Thorlabs), an emission filter (BLP01-488R-25, Semrock), a flip mirror, a spectrometer (Avaspec 2048, Avantes) and an EMCCD camera (iXon3 897, Andor). The excitation light was guided towards the objective lens with the help of shortpass dichroic mirror (BLP01-488R, Semrock). The convex lens L1 focused the laser beam into the back aperture of the objective lens, thus illuminating a larger area of the sample. The defocused beam excites the written structure, which, in turn, produces the fluorescence signal. This signal is collected by an objective lens and imaged with a camera. An Avantes spectrometer was added to measure the emission spectrum from the sample. The fluorescence images were false-colored based on their raw values using ImageJ software.

Kunwar P., Hassinen J., Bautista G., Ras R.H, & Toivonen J. (2016). Sub-micron scale patterning of fluorescent silver nanoclusters using low-power laser. Scientific Reports, 6, 23998.

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Imaging Amyloid Aggregation Using TIRF Microscopy

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Imaging experiments were carried out with bespoke TIRF inverted microscope (Eclipse TE2000-U; Nikon) fitted with a Perfect Focus unit. Excitation of ThT and AF647 was achieved with either a 405-nm laser (LBX-405-50-CIR-PP; Oxxius) or 641-nm laser (Cube, 1150205; Coherent), respectively. The beams were aligned parallel to the optical axis and directed into an oil immersion objective lens (1.49 numerical aperture [N.A.], 60×, Plan Apo, TIRF; Nikon) above the critical angle to ensure TIR at the coverslip/sample (glass/water) interface. Fluorescence emission was also collected by the same objective and selected by the presence of a dichroic (Di01-R405/488/561/635; Semrock) and subsequently passed through appropriate emission filters (BLP01-488R-25, FF01-480/40-25, and FF01-676/37-25; Semrock). Image stacks of the AF647 and ThT emission channels were collected by sequential excitation of AF647 followed by ThT. Images were recorded by an electron multiplying charge-coupled device (Evolve delta 512; Photometrics) with an electron multiplication gain of 250 analog-to-digital units per photon running in frame transfer, clear presequence mode. Each pixel on the image was 237 nm. Images from 27 different fields of view were recorded at 50 ms for 200 frames in each emission channel using a custom beanshell script through Micromanager software (v. 1.4).

Aprile F.A., Sormanni P., Podpolny M., Chhangur S., Needham L.M., Ruggeri F.S., Perni M., Limbocker R., Heller G.T., Sneideris T., Scheidt T., Mannini B., Habchi J., Lee S.F., Salinas P.C., Knowles T.P., Dobson C.M, & Vendruscolo M. (2020). Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. Proceedings of the National Academy of Sciences of the United States of America, 117(24), 13509-13518.

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Multispectral Calcium Imaging of Cortex

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A multispectral imaging system based on the design of Bouchard et al. and Sun et al. was used to perform calcium sensitive dye imaging [15 (link), 21 (link)]. Briefly, a high-power light emitting diode (LED) centered at 488 nm with a 460 ± 30 nm bandpass filter (Thorlabs, MCLED, Newark NJ, Semrock, FF01-460/60-20, Rochester NY) was focused onto the cortex with a bi-convex lens (Thorlabs, BK7, focal length = 10.0 mm). Images of the cortex were acquired using a 480×640 pixel Pike fire-wire camera (AVT, Newburyport MA) using a Zoom 7000 macro lens (Navitar, Rochester NY). A 500 nm longpass filter (BLP01-488R-25, Semrock) was placed between the lens and camera to reject the excitation light. The camera and LED were controlled by the SPLASSH software package [21 (link)].
For each experiment, one imaging run was composed of multiple (5 – 10) imaging trials, where a stimulus was presented once in each trial. Each imaging trial consisted of 30 seconds of imaging at 30 fps, with 6–10 seconds of baseline acquired before stimulation and images were binned 2×2. Image acquisition was synchronized with the start of INS (or electrical) stimulation, and LED illumination was driven from the camera’s ‘expose’ output signal to minimize photobleaching and exposure of the camera during read-out.

Cayce J.M., Bouchard M.B., Chernov M.M., Chen B.R., Grosberg L.E., Jansen E.D., Hillman E.M, & Mahadevan-Jansen A. (2014). Calcium imaging of infrared-stimulated activity in rodent brain. Cell calcium, 55(4), 183-190.

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Kinetics of Amyloid-beta Fibrillization

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Time-resolved ThT fluorescence data were acquired with the same stopped flow spectrometer used for the light scattering experiments. Fluorescence excitation light at 450 nm was provided by the same arc lamp and monochromator. Fluorescence emission was detected by the PMT after passing through a 488 nm long pass filter (Semrock, part number: BLP01-488R-25). After rapid mixing by the stopped flow instrument, solutions contained 25 µM ThT, 175 mM sodium phosphate, and 20% glycerol at pH 7.4, with Aβ40 concentrations from 29 μM to 1.5 mM.

Jeon J., Yau W.M, & Tycko R. (2023). Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering. Nature Communications, 14, 2964.

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Quantitative Vesicle Permeabilization Assay

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A quantitative vesicle assay was used to measure the ability of αS oligomers to permeabilize membranes as described previously (Flagmeier et al., 2017 (link)). αS was aggregated as described earlier, and aliquots were removed and diluted so that the final concentration of αS added to the vesicles was 50 nM. The diluted samples were preincubated for 5 min at RT in the presence or absence of α₂M, BSA, or CLU (concentrations are indicated in the legend for Figure 3) before being added to the solution above POPC lipid vesicles containing Cal-520 (100 μM; Stratech Scientific) tethered to the surface using biotin/neutravidin linkage. A change in the fluorescence as a result of Ca²⁺ (present at 1.3 mM in L-15 buffer; Thermo Fisher Scientific) entering the vesicles was quantified by means of TIRF microscopy using a 488 nm laser for excitation (Toptica Photonics) and emission filters BLP01-488R-25 and FF01-520/44-25 (Semrock). The fluorescence intensity of each vesicle was then normalized to the maximum possible fluorescence intensity of the vesicle measured following incubation with ionomycin (1.4 μM; Sigma). For each sample, the acquisition of 9 fields of view (3 × 3 grid) was automated to prevent user bias.

Whiten D.R., Cox D., Horrocks M.H., Taylor C.G., De S., Flagmeier P., Tosatto L., Kumita J.R., Ecroyd H., Dobson C.M., Klenerman D, & Wilson M.R. (2018). Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers. Cell Reports, 23(12), 3492-3500.

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