Uv 2101pc spectrophotometer

Manufactured by Shimadzu

Sourced in Japan, Italy

The UV-2101PC spectrophotometer is a laboratory instrument designed for the measurement of ultraviolet and visible light absorption or transmission spectra. It features a double-beam optical system and a wavelength range of 190 to 1100 nanometers.

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Lab products found in correlation

Silica gel 60 f254, by Merck Group (2 mentions) Zetasizer zs, by Malvern Panalytical (2 mentions) Cary 630 ftir spectrometer, by Agilent Technologies (2 mentions) Escalab 250xi, by Thermo Fisher Scientific (2 mentions) Pw 1710, by Philips (1 mentions) Tripletoft5600, by AB Sciex (1 mentions) Varian cary eclipse, by Agilent Technologies (1 mentions) 1010 microscope, by JEOL (1 mentions) 300 mhz spectrometer, by Bruker (1 mentions) Sfm 300, by Bio-Logic (1 mentions) Dpx300 300 mhz spectrometer, by Bruker (1 mentions) Ultra 55, by Zeiss (1 mentions) 209f1 thermogravimetric analyzer, by Netzsch (1 mentions) F 4500 spectrometer, by Hitachi (1 mentions) Tds 640a oscilloscope, by Tektronix (1 mentions) Lps 220b spectrofluorometer, by Horiba (1 mentions) Avance drx 400 spectrometer, by Bruker (1 mentions) Drx 300 spectrometer, by Bruker (1 mentions)

23 protocols using uv 2101pc spectrophotometer

Characterization of Nanohybrid Materials

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The composition of the nanohybrids was
characterized by Fourier transform infrared spectroscopy (FTIR) (Shimadzu
FTIR-8101 A) in the range of 4000–400 cm^–1. The crystallinity and phases of nanohybrids were examined by an
X-ray diffractometer (Philips PW 1710) equipped with Cu Kα radiation
(λ = 1.54060 Å), a voltage of 40 kV, and a current of 30
mA in the range of 2–80° with 2°/min scanning rate.
The transmission electron microscopy (TEM) micrographs were taken
to investigate the morphology of the nanohybrid (JEM 2100 JEOL) with
an accelerating voltage of 80 kV. An aqueous suspension of samples
was drop-casted onto carbon-coated cobber grids, followed by drying
of the samples on filter paper in ambient conditions. TGA was performed
to test the nanohybrid thermal stability (25–600 °C) in
which the weight residue was reported separately using 7 mg of sample
at a constant heating rate of 10 °C/min and a nitrogen gas flow
of 10 mL/min for each sample in the TG instrument (TGA-50). The UV–visible
absorption spectra were obtained from a Shimadzu UV-2101 PC spectrophotometer.

Salahuddin N.A., Ali M., Al-Lohedan H.A., Issa Z.A., Barakat A, & Ayad M.M. (2021). Aniline-co-o-anthranilic Acid Copolymer-Chitosan/Ag@AgCl Nanohybrid as a Carrier for (E)-N′-(Pyridin-2-ylmethylene) Hydrazinecarbothiohydrazide Release and Antimicrobial Activity. ACS Omega, 6(34), 21939-21951.

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Steady-state ATPase Kinetic Assay

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Steady-state ATPase experiments were carried out in SF50 buffer by using a pyruvate kinase-lactate dehydrogenase (PK-LDH) coupled assay (14 U/mL PK, 20 U/mL LDH, 1 mM ATP, 1 mM phosphoenol pyruvate, 200 μM NADH). Time courses of NADH absorbance (ε₃₄₀ = 6220 M⁻¹cm⁻¹) were followed in a Shimadzu UV-2101PC spectrophotometer.

Harami G.M., Nagy N.T., Martina M., Neuman K.C, & Kovács M. (2015). The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling. Scientific Reports, 5, 11091.

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Characterization of Reagent-Grade Compounds

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We used commercially available reagents without purification. Silica gel 60 F254 (Merck) plates were used for thin layer chromatography. Milli-Q ultrapure water was used for the sensing experiments. ¹H and ¹³C nuclear magnetic resonance (NMR) spectra were recorded on a Bruker 300 MHz spectrometer (Bruker Corporation, Germany). Chemical shifts are reported in ppm with tetramethylsilane as an internal standard. High-resolution mass spectra were recorded in the positive ion mode on a TRIPLETOFT5600 (ABSciex, Canada). UV-vis absorption spectra were recorded on a Shimadzu UV-2101PC spectrophotometer at 293 K (Shimadzu Corporation, Japan). Fluorescence studies were carried out with a Varian Cary Eclipse (Agilent, United States) fluorescent spectrophotometer. Transmission electron microscopy (TEM) images were recorded with a JEOL-1010 microscope (Jeol Ltd., Japan) operated at 100 kV.

Añón E., Costero A.M., Gaviña P., Parra M., El Haskouri J., Amorós P., Martínez-Máñez R, & Sancenón F. (2019). Not always what closes best opens better: mesoporous nanoparticles capped with organic gates. Science and Technology of Advanced Materials, 20(1), 699-709.

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Stopped-flow and Quenched-flow Kinetic Assays

Cited 1 time

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Unless otherwise stated, all measurements were carried out in SF50 buffer at 25°C. Stopped-flow experiments were carried out in KinTek SF-2004 and BioLogic SFM 300 apparatuses. Quenched-flow experiments were performed in a KinTek RQF-3 instrument. Post-mixing concentrations are stated in all experiments. In experiments requiring nucleotide-free RecQ, nucleotide contamination was removed by pre-incubation with 0.02-U/ml apyrase for 15 min at 25°C. P_i liberation from ATP was followed using a fluorescently labeled P_i binding protein (MDCC-PBP) (12 (link)). MDCC-PBP calibration was performed as described earlier (13 (link),14 (link)). mdATP and mdADP were excited at 280 nm and fluorescence emission was detected through a 420-nm long-pass filter utilizing FRET (Förster Resonance Energy Transfer) from aromatic residues of RecQ.
Steady-state ATPase measurements were carried out in SF50 buffer plus 50-μg/ml bovine serum albumin using a pyruvate kinase-lactate dehydrogenase (PK-LDH) linked assay (14-U/ml PK, 20-U/ml LDH, 1-mM ATP, 1-mM phosphoenol pyruvate, 200-μM NADH (nicotinamide adenine dinucleotide, reduced form)). Time courses of NADH absorbance (ϵ_{340 nm} = 6220 M⁻¹cm⁻¹) were followed in a Shimadzu UV-2101PC spectrophotometer.

Sarlós K., Gyimesi M., Kele Z, & Kovács M. (2014). Mechanism of RecQ helicase mechanoenzymatic coupling reveals that the DNA interactions of the ADP-bound enzyme control translocation run terminations. Nucleic Acids Research, 43(2), 1090-1097.

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Steady-State ATPase Activity Measurement

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Steady-state ATPase activities were measured by using a pyruvate kinase-lactate dehydrogenase (PK-LDH) coupled assay (14 U/ml PK, 20 U/ml LDH, 1 mM ATP, 1 mM phosphoenol pyruvate, 200 μM NADH). Time courses of NADH absorbance (ε₃₄₀ = 6220 M⁻¹ cm⁻¹) were followed in a Shimadzu UV-2101PC spectrophotometer.

Mills M., Harami G.M., Seol Y., Gyimesi M., Martina M., Kovács Z.J., Kovács M, & Neuman K.C. (2017). RecQ helicase triggers a binding mode change in the SSB–DNA complex to efficiently initiate DNA unwinding. Nucleic Acids Research, 45(20), 11878-11890.

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Analytical Characterization of Samples

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All reagents were commercially available and used without purification. Silica gel 60 F₂₅₄ (Merck, 64293 Darmstadt, Germany) plates were used for test strips. UV/Vis absorption spectra were recorded in a 1 cm pathlength quartz cuvette with a UV-2101PC spectrophotometer (Shimadzu, 47269 Duisburg, Germany).

Martínez-Aquino C., Costero A.M., Gil S, & Gaviña P. (2018). A New Environmentally-Friendly Colorimetric Probe for Formaldehyde Gas Detection under Real Conditions. Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, 23(10), 2646.

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Synthesis and Characterization of Gold Nanoparticles

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Chloroauric acid (HAuCl₄·3H₂O), sodium citrate dihydrate, α-lipoic acid, 3,5-dihydroxybenzyl alcohol, diisopropyl azodicarboxylate (DIAD), and triphenylphosphine (TPP) were commercially available and were used without purification. Anhydrous tetrahydrofuran (THF) was freshly distilled from sodium/benzophenone under argon. All the aqueous solutions were prepared with Milli-Q water (18.2 MΩ cm⁻¹). A Bruker DPX300 300 MHz spectrometer (Billerica, MA, USA) was used to obtain the ¹H-NMR spectrum, using tetramethylsilane as internal standard. UV-vis absorption spectra were performed on a Shimadzu UV-2101PC spectrophotometer (Kyoto, Japan). Fourier-transform infrared spectra (FT-IR) were recorded with an Agilent Cary 630 FT-IR spectrometer (Santa Clara, CA, USA). Transmission electron microscopy images were obtained with a JEOL JEM-1010 transmission electron microscope (Tokyo, Japan,) operating at 100 kV. A Malvern Instruments Zetasizer ZS was used for dynamic light scattering (DLS) measurements (Worcestershire, UK, 3 times in 10–25 cycles).

Martínez-Aquino C., Costero A.M., Gil S, & Gaviña P. (2019). Resorcinol Functionalized Gold Nanoparticles for Formaldehyde Colorimetric Detection. Nanomaterials, 9(2), 302.

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Assaying Steady-State Metabolic Fluxes

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The steady-state fluxes were measured in standard buffer at 37°C by coupling the reaction with an excess of the auxiliary enzymes TPI and GDH. The final concentrations in the cuvette were 2 mM NADH, 2 mM MgATP, 10 mM Glc, 20 mM PC, 3 U/ml CK, 3.5 U/ml TPI and 0.5 U/ml GDH. NADH consumption was monitored at 385 nm (ε^{385 nm}_NADH = 0.75 mM⁻¹ cm⁻¹), as described by Puigjaner et al.[25] (link), using a Shimadzu UV-2101PC Spectrophotometer with 1-cm light path cells. These assay conditions are not quite representative for mouse muscle in vivo, but in view of the considerable amount of consensus building required to achieve proper in vivo standard conditions [27] (link), we here reverted to conditions that are not far off from the in vivo state and that our previous work [15] (link), [25] (link) has shown to work well.
Extracts were pre-incubated with Cd(NO₃)₂ (0–7 µM) and Hg(NO₃)₂ (0–10 µM) in standard buffer at 37°C for 60 min. The reaction was then started by adding 100 µl of the reaction mixture to 900 µl of the pre-incubated extract.

Ramírez-Bajo M.J., de Atauri P., Ortega F., Westerhoff H.V., Gelpí J.L., Centelles J.J, & Cascante M. (2014). Effects of Cadmium and Mercury on the Upper Part of Skeletal Muscle Glycolysis in Mice. PLoS ONE, 9(1), e80018.

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Recombinant VWF A1 and A1A2A3 Domains

Cited 2 times

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Wild type VWF A1 (Q₁₂₃₈-P₁₄₇₁) and its mutants
G1324S and P1337L were expressed in E. coli M15 cells as fusion constructs
containing an N-terminal His₆ tag. Inclusion body preparation,
refolding and purification of the proteins were performed as previously
described [12 (link), 55 (link)]. RCAM A1 was prepared in 2 M GdnHCl by reduction
of the single disulfide bond connecting N- and C-termini of A1 with 6 mM DTT,
followed by blocking with 12 mM iodoacetamide as previously described [27 (link), 30 (link)]. A2 and A3 domains were expressed and purified from E. coli M15
cells as fusion constructs containing an N-terminal His₆ tag. A2 was
purified in the presences of CaCl₂. Wild type A1A2A3 tridomains
(amino acids Q1238 - G1874) and the mutants P1337L, V1314D and F1369I in A1A2A3
were expressed in HEK293 cells as fusion proteins containing a C-terminal
His₆ tag and purified via Ni²⁺ affinity chromatography
as described previously [34 (link), 35 (link)]. The purity of the A1 and of A1A2A3
domains was confirmed via Analytical Gel filtration and/or RP-HPLC as recently
described [55 (link)]. A1 and A1A2A3
concentrations were measured on a Shimadzu UV2101PC spectrophotometer using
extinction coefficients of 15350 L/mol/cm for the A1 domain and 74497 L/mol/cm
for A1A2A3.

Tischer A., Brehm M.A., Machha V.R., Moon-Tasson L., Benson L.M., Nelton K.J., Leger R.R., Obser T., Martinez-Vargas M., Whitten S.T., Chen D., Pruthi R.K., Bergen HR I.I.I., Cruz M.A., Schneppenheim R, & Auton M. (2019). Evidence for the Misfolding of the A1 Domain within Multimeric von Willebrand Factor in Type 2 von Willebrand Disease.. Journal of molecular biology, 432(2), 305-323.

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Protein Concentration and CD Spectroscopy

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All protein concentrations were determined on a UV2101PC spectrophotometer (Shimadzu, Kyoto, Japan) after centrifugation of the solutions at 60,000 × g at 4°C for 10 or 20 minutes to remove potential protein aggregates. The extinction coefficients used for C4 and C1-CTCK were 11,260 and 41,515 L mol
⁻¹cm
⁻¹and were calculated from the number of tryptophan and tyrosine residues.
CD spectra were recorded at 25°C on an Aviv Biomedical Model 420SF CD spectrophotometer. Spectra in the far-ultraviolet (far-UV) range (200–260 nm) were recorded using a 1 mm quartz cell with an integration time of 60 seconds and band- and step-widths of 1 nm. Near-UV CD spectra were recorded using either a 10 cm cylindrical quartz cell (for both C1CTCK proteins) or a 0.2 or 1 cm quartz cell (both for wtVWF and p.Pro2555Arg C4, respectively). The integration time was 60 or 120 seconds and band- and step-widths were 1 nm. All spectra were corrected for the signal of the corresponding buffer and converted to mean ellipticity per amino acid residue.

Huck V., Chen P.C., Xu E.R., Tischer A., Klemm U., Aponte-Santamaría C., Mess C., Obser T., Kutzki F., König G., Denis C.V., Gräter F., Wilmanns M., Auton M., Schneider S.W., Schneppenheim R., Hennig J, & Brehm M.A. (2020). Gain-of-Function Variant p.Pro2555Arg of von Willebrand Factor Increases Aggregate Size through Altering Stem Dynamics. Thrombosis and Haemostasis, 122(2), 226-239.

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