Biodoc it imaging system

Manufactured by Analytik Jena

Sourced in United States, United Kingdom

The BioDoc-It Imaging System is a versatile lab equipment designed for capturing high-quality images of gels, blots, and other samples. The system features a built-in camera and illumination system, allowing for efficient documentation of experimental results.

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BioDoc-It System (7 citations) BioDoc-It (4 citations) UVP BioDoc-It Imaging System (4 citations) BioDoc-Imaging System (2 citations) UVP Biodoc-It 2 imaging system (2 citations)

46 protocols using biodoc it imaging system

Characterization of HuscFvs Targeting HCV NS3/4A

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Spectrometrically standardized soluble HuscFvs in the lysates of transformed HB2151 E. coli clones were tested for binding to the rNS3/4A by indirect ELISA and Western blotting. Original HB2151 E. coli (HB) was used as background binding control in both assays. BSA served as control antigen in the indirect ELISA.
Diversity of the huscfvs sequences of the HB2151 E. coli clones were determined by subjecting the PCR amplified huscfvs to MvaI digestion followed by resolving the cut DNA products in 14% polyacrylamide gel containing 0.5% glycerol. Electrophoresis was carried out in TBE buffer at 20 mA per slab gel. The separated DNA bands were stained by ethidium bromide and the restriction fragment length polymorphism (RFLP) was determined using a Bio Doc-ITTM Imaging System, UVP, USA. CDRs and their respective canonical immunoglobulin framework regions (FRs) of the sequenced huscfvs were predicted using an online Internatioanl ImMunoGeneTics (IMGT^®) Information System.

Jittavisutthikul S., Seesuay W., Thanongsaksrikul J., Thueng-in K., Srimanote P., Werner R.G, & Chaicumpa W. (2016). Human Transbodies to HCV NS3/4A Protease Inhibit Viral Replication and Restore Host Innate Immunity. Frontiers in Immunology, 7, 318.

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ISSR Primer Screening for Genetic Diversity

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Cultivars "Olympic Fire", "Ostbo Red" (maternal parent of "Olympic Fire"), and "Starburst" were used to screen 96 ISSR primers designed by the University of British Columbia (UBC 801-896). Eight primers were selected based on the strong, clear, reproducible, and polymorphic banding patterns they produced. ISSR-PCR amplifications were performed in a total volume of 20 µL consisting of 2 µL (20 ng) template DNA, 2 µL primer, 10 µL master mix (Applied Biosystems, Foster city, CA, USA), and 6 µL double-distilled water. The amplifications were programmed in a Mastercycler nexus gradient (Eppendorf, Hamburg, Germany) under following conditions: an initial denaturation step at 94 • C for 5 min; 40 cycles of 94 • C for 30 s, 52 • C for 50 s, and 72 • C for 120 s; followed by an extension for 7 min at 72 • C. Samples were then cooled to 4 • C and placed in a refrigerator until being loaded into gels. The PCR products were electrophoresed on 1.2% (w/v) agarose gels that, in 0.5 × TBE buffer solution (Fisher Scientific, Fair Lawn, NJ, USA) (80 V for 3.5 h) and stained with 0.5 mg•L -1 ethidium bromide solution (Sigma-Aldrich, St. Louis, MO, USA). 100-bp DNA ladder (Invitrogen, Carlsbad, CA, USA), were loaded onto the outside two lanes of each gel to estimate the size of amplified fragments. Gels were visualized and photographed using a BioDoc-It TM Imaging System (UVP, Upland, CA, USA).

Li H., Chappell M., & Zhang D. (2020). Assessing Genetic Diversity and Population Structure of Kalmia latifolia L. in the Eastern United States: An Essential Step towards Breeding for Adaptability to Southeastern Environmental Conditions. Sustainability, 12(19), 8284-8284.

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Anaerobic and Aerobic Bacterial Growth

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After serial dilution in a maximum-recovery diluent, the bacteria were cultured on MRS agar and LB agar plates in an anaerobic chamber and a regular incubator at 37°C. The growth was monitored after 24~48 h and photographs were taken with the BioDoc-It TM Imaging System (UVP).

Qiu X., Han X., Zhang X., Zhen L., Li Z., Liu M., Ren Y., & Wang S. (2021). Lactobacillus Alleviates Colitis Caused by Chemotherapy Via Biofilm Formation.

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In Vitro Assay of RET1 Enzyme Activity

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Individual reactions were made up in 0.2 ml PCR tubes (Peqlab 820264-A). RET1 enzyme (see SI text) was added (0.05 μl, 0.2 mg ml⁻¹), UTP (Thermo Scientific R0471 100 mM) was added to a final concentration of 50 μM. RNA substrate (see SI text) was added to a final concentration of 200 nM. Inhibitors were added as required (0.5 μl in DMSO) to a final concentration of 50 μM. When no inhibitor was included 5 % (vol/vol) DMSO was added as control. The volume was made up to 10 μl in buffer D (Tris pH 7.5 10 mM, KCl 200 mM, DTT 1 mM, EDTA 0.5 mM MgCl₂ 3.2 mM) and the reaction was incubated for 20 mins at 27°C, then inactivated at 65°C for 10 mins. RNA loading dye (10 μl, NEB B363A) was added and tubes were heated (5 mins at 70°C), 10 μl was loaded onto 15 % TBE urea pre-cast gel (Invitrogen EC68852) and run in 1 x TBE buffer for 1.5 h at 130 V. Gels were incubated with Sybr Gold nucleic acid stain (Life Technologies S11494) for 20 mins, then imaged on an ultraviolet trans-illuminator (BioDoc-It imaging system, UVP). Experiments were carried out in duplicate for each inhibitor.

Cording A., Gormally M., Bond P.J., Carrington M., Balasubramanian S., Miska E.A, & Thomas B. (2016). Selective inhibitors of trypanosomal uridylyl transferase RET1 establish druggability of RNA post-transcriptional modifications. RNA Biology, 14(5), 611-619.

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Glycoconjugate Labeling and Analysis

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Example 8

Cells were seeded at 3×10⁶/8 ml per 10-cm dish and treated with control and test sugars (200 micromolar Fuc 3 vs. alkynyl derivatized Fuc 1, or 25 micromolar ManNAc 5 vs. alkynyl derivatized ManNAc 2) in growth medium at 37° C. After 3 days, cell extracts were prepared by resuspending the cells in 1 ml of lysis buffer (1% Nonidet P-40/150 mM NaCl/protease inhibitor/100 mM sodium phosphate, pH 7.5). Protein extract (1 mg/ml) was labeled for 1 h at room temperature (conditions as outlined in microscopic analysis; the azido rhodamine probe was a gift from Benjamin F. Cravatt, The Scripps Research Institute). Labeled protein lysate was resolved by SDS/PAGE. For immunoblotting of biotin-labeled glycoconjugates, electrophoresed proteins were transferred onto PVDF membranes, blocked for 20 min with SuperBlock Blocking Buffer, probed for 1 h with anti-biotin MAb (1 microgram/ml), and incubated with peroxidase-conjugated goat anti-mouse IgG (1:7, 500 dilution) for 30 min. Each step was followed by a wash with 0.02% Tween 20/PBS (PBST). Signal was developed with SuperSignal Chemiluminescent Substrate and detected by exposure to x-ray film. For detecting the coumarin-labeled glycoconjugates, gels were examined under 365 nm UV light with a 535+/−50 nm filter. Images were taken by using a BioDoc—It imaging system (UVP). Rhodamine gels were analyzed.

US10317393B2. Alkynyl sugar analogs for labeling and visualization of glycoconjugates in cells (2019-06-11). Academia Sinica [TW]. Inventors: Chi-Huey Wong [US], Tsui-Ling Hsu [TW], Sarah R. Hanson [US], Masaaki Sawa [JP].

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Measuring Plasmid Transformation Efficiency

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Three transformations were carried out as shown in Fig. 2A: the intact target plasmid into cells without the chromosomal gene for CisA, the target plasmid without initiation and termination sequences into cells with the chromosomal gene for CisA, and the intact target plasmid into cells with the chromosomal gene for CisA. Transformant colonies were selected on LB agar plates supplemented with chloramphenicol (15 ng/μl) and inoculated to liquid LB cultures with chloramphenicol. After overnight growth in 37°C shaken at 225 rounds per minute (the same growth conditions from here on unless specified otherwise), 1 ml of culture was purified and eluted to 40 μl of elution buffer, and 5 μl was used for electrophoresis (0.8% agarose gel, 110 V, 40 min; Bio-Rad Mini-Sub Cell GT Systems). An image was taken using UVP BioDoc-It Imaging System and analyzed using ImageJ to calculate fraction of the nicked target plasmid with the following equation: brightness of the band for nicked DNA (brightness of the band for nicked DNA + brightness of the band for supercoiled DNA + brightness of the band for linear DNA).

Yi X., Khey J., Kazlauskas R.J, & Travisano M. (2021). Plasmid hypermutation using a targeted artificial DNA replisome. Science Advances, 7(29), eabg8712.

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Evaluate Bacterial Motility and Inhibition

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Cultured S. Typhimurium was suspended in Tris-Maleate buffer (50 mM, pH 6.4) at 1e7 CFU/ml. The semi-solid agar plates were composed of Tris-Maleate buffer (50 mM, pH 6.4), 0.2% w/v casamino acids (BD bacto-tryptone 211705), and 0.3% w/v agar (BD bacto-agar 244520), and prepared the day prior to the experiment. To the center each plate, an aliquot (20μl) was added of either HD6, mouse IgG1 antibody, or Tris-Maleate buffer (50 mM, pH 6.4, as vehicle control). Next, the center of each plate was inoculated with an aliquot (3 μl) of the S. Typhimurium suspension. Plates were then incubated at 37°C for 6.5 hours. After incubation, the plates were photographed using a gel imager (UVP, Upland, CA, BioDoc-It Imaging system). The bacterial motility/swimming parameters were assessed for each plate using ImageJ. Thus, for each image, a circular mask of swimming bacteria was generated using the “Threshold” and “Find Edges” tools. From this mask, the diameter of the circle of swimming bacteria was then measured.

Akahoshi D.T., Natwick D.E., Yuan W., Lu W., Collins S.R, & Bevins C.L. (2023). Flagella-driven motility is a target of human Paneth cell defensin activity. PLOS Pathogens, 19(2), e1011200.

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RAPD Analysis of In Vitro Regenerated Plants

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Twelve in vitro regenerated plants were PCR analysed using RAPD primers to check the extent of genetic similarity. Genomic DNA was isolated from leaves using the cetyltrimethylammonium bromide (CTAB) method [20 (link)]. The DNA concentration was estimated using Multiskan GO (Thermo Scientific). DNA samples were diluted, and the concentration was adjusted up to 50 ng µl⁻¹. A 25 µl reaction mix was prepared for each DNA sample using 10 × PCR buffer, MgCl₂ (25 mM), dNTPs (10 mM), primers (10 mM), Taq polymerase (BR Biochem) (0.25 unit/rxn.), autoclaved ddH₂O and DNA (1 µl of 50 ng µl⁻¹) as a template. PCR tubes were arranged in My Cycler (Bio-Rad). Reaction conditions were set as denaturation at 94 °C for 5 min (for the 1st cycle), [94 °C for 1 min, annealing at 37 °C for 1 min, extension at 72 °C for 3 min] for 30 cycles, final extension at 72 °C for 10 min and hold at 4 °C for infinite. Gel electrophoresis was performed for the PCR products, and gel pictures were captured using a BioDoc-It™ Imaging System (UVP). Total bands were scored by counting manually.

Goyal S., Chatterjee V., Kulkarni V.M, & Bhat V. (2023). Plant regeneration through somatic embryogenesis in cell suspensions of Cenchrus ciliaris L.. Plant Methods, 19, 110.

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Sperm Genomic DNA Isolation Protocol

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DNA /RNA Shield (#R110 0; Zy mo) and Quick gDNA Genomic Lysis Buffer (included in kit), were used for sperm lysis instead of Buffer RLT. Samples in the Genomic Lysis Buf fer were loaded onto the columns, while samples in DNA /RNA Shield were combined with 3 volumes of Genomic Lysis Buffer before being loaded onto spin columns. Samples were centrifuged at 10,000 × g for 1 min to bind. Wash and elution steps followed the manufacturer’s protocol for a final elution volume of 100 µL.
DNA yields and quality were determined using the Nanodrop 2000 Spectrophotometer (#E112352; Thermo Scientific, Somerset, NJ). A total of 350 ng of genomic DNA (gDNA) was resolved on a 0.7% agarose gel at 100 V for 45 min, stained with 0.5 µg/mL ethidium bromide solution, and visualized on a BioDoc-It Imaging System (#97-0172-01; UVP, Upland, CA). Given that haploid cells are expected to contain 3 pg DNA per cell, DNA yields were calculated as the observed yield/expected yield based on cell count. The full protocol for DNA isolation is provided in the Supplementary Material.

Wu H., de Gannes M.K., Luchetti G, & Pilsner J.R. (2015). Rapid method for the isolation of mammalian sperm DNA. BioTechniques, 58(6), 293-300.

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EMSA for MSMEG_0307 DNA Binding

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The DNA fragments (∼300bp) containing the binding sequence motifs were amplified using PCR and primers (Table S1) and further purified. The reactions had a final volume of 10 μl and contained 100 ng of DNA, 1× EMSA buffer (20 mM Tris.HCl pH8, 75 mM NaCl, 10 mM MgCl₂) and increasing concentrations of recombinant His-tagged MSMEG_0307 protein (0.01 μg to 1 μg). The reactions were incubated at room temperature for 30 min and then were loaded onto a 5% (v/v) native polyacrylamide gel. Following electrophoresis the gels were stained with ethidium bromide and the bands were visualised using BioDoc-It™ imaging system (UVP, Cambridge, UK).

Evangelopoulos D., Gupta A., Lack N.A., Maitra A., ten Bokum A.M., Kendall S., Sim E, & Bhakta S. (2014). Characterisation of a putative AraC transcriptional regulator from Mycobacterium smegmatis. Tuberculosis (Edinburgh, Scotland), 94(6), 664-671.

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