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Isotemp 3016

Manufactured by Thermo Fisher Scientific
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The Isotemp 3016S is a general-purpose laboratory incubator designed for a variety of applications. It features a stainless steel interior, adjustable temperature range, and digital temperature control.

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Lab products found in correlation

Ptc 423s, by Thermo Fisher Scientific (2 mentions) J 815 cd spectrometer, by Jasco (2 mentions) Quartz cuvette, by PerkinElmer (1 mentions) Sx 19, by Applied Photophysics (1 mentions) Ar1000, by TA Instruments (1 mentions)

Close spelling variants of this product

Isotemp

7 protocols using isotemp 3016

1

Temperature-Dependent Circular Dichroism Analysis

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Wavelength-dependent Circular Dichroism (CD) spectra were collected on a Jasco J-815 CD Spectrometer equipped with a PTC-423S single position Peltier temperature control system and counter-cooled with an Isotemp 3016S (Fisher Scientific) water bath. Samples were loaded in a Hellma 218 quartz cuvette (500 µL, 1 mm path length). A far-UV temperature-dependent wavelength scan from 185–260 nm as a function of temperature was completed for CE1-His6 and E1C-His6 in the absence and presence of GNPs at 0.2 mg/mL in 10 mM sodium phosphate buffer pH 8.0 at scan rate of 50 nm/min for a range of temperatures (25–90°C) with 3 accumulation scans. At least two batches of separately purified proteins were measured. CD data was converted into mean residue molar ellipticity (MRW) via equation [θ]MRW = θ·MW/(10·n·C·l), where θ is in mdeg, MW is molecular weight, n is amino acid number in protein, C is concentration in mg/mL, l is path length in cm [35 (link)]. Fitting and calculation of protein secondary structure was processed with CDSSTR methods [36 (link)–38 (link)]. Parameters for the calculation using CDSSTR program were identical to our previously published work [31 (link)].
Dai M., Frezzo J., Sharma E., Chen R., Singh N., Yuvienco C., Caglar E., Xiao S., Saxena A, & Montclare J. (2016). Engineered Protein Polymer-Gold Nanoparticle Hybrid Materials for Small Molecule Delivery. Journal of nanomedicine & nanotechnology, 7(1), 356.
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2

Intrinsic Tyrosine Fluorescence Quenching Assay for InsP Binding to Arr1

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To assess InsP binding to Arr1, an intrinsic tyrosine fluorescence quenching assay was performed (Arr1 has 14 Tyr residues/monomer), as done previously (Wilson and Copeland, 1997 (link)). 300 nM Arr1 in 500 µL of Heparin Equilibration Buffer was mixed in a quartz cuvette (PerkinElmer, Waltham, MA) with mini stir bar mixing on low and temperature maintained at 20 °C. A PerkinElmer LS55, coupled to an Isotemp 3016S (Fisher Scientific, Pittsburgh, PA) to regulate temperature, was used to measure fluorescence of samples after serial addition of InsP stocks diluted in the same buffer as the Arr1. Device settings for the scans were Ex/Em range of wavelengths of 275/290–350 nm. A slit width of 7 nm was used with a scan rate of 100 nm per min. Every scan was repeated 3 times, and the emission peak at 305 nm was used for the tyrosine emission wavelength. Percent quench values were adjusted for increasing dilution with additional ligand added 5 µL at a time. Curves were fit to the means of the replicates with one site binding accounting for ligand depletion.
Sander C.L., Luu J., Kim K., Furkert D., Jang K., Reichenwallner J., Kang M., Lee H.J., Eger B.T., Choe H.W., Fiedler D., Ernst O.P., Kim Y.J., Palczewski K, & Kiser P.D. (2021). Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure (London, England : 1993), 30(2), 263-277.e5.
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3

Temperature-Dependent Circular Dichroism Analysis

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Wavelength-dependent Circular Dichroism (CD) spectra were collected on a Jasco J-815 CD Spectrometer equipped with a PTC-423S single position Peltier temperature control system and counter-cooled with an Isotemp 3016S (Fisher Scientific) water bath. Samples were loaded in a Hellma 218 quartz cuvette (500 µL, 1 mm path length). A far-UV temperature-dependent wavelength scan from 185–260 nm as a function of temperature was completed for CE1-His6 and E1C-His6 in the absence and presence of GNPs at 0.2 mg/mL in 10 mM sodium phosphate buffer pH 8.0 at scan rate of 50 nm/min for a range of temperatures (25–90°C) with 3 accumulation scans. At least two batches of separately purified proteins were measured. CD data was converted into mean residue molar ellipticity (MRW) via equation [θ]MRW = θ·MW/(10·n·C·l), where θ is in mdeg, MW is molecular weight, n is amino acid number in protein, C is concentration in mg/mL, l is path length in cm [35 (link)]. Fitting and calculation of protein secondary structure was processed with CDSSTR methods [36 (link)–38 (link)]. Parameters for the calculation using CDSSTR program were identical to our previously published work [31 (link)].
Dai M., Frezzo J., Sharma E., Chen R., Singh N., Yuvienco C., Caglar E., Xiao S., Saxena A, & Montclare J. (2016). Engineered Protein Polymer-Gold Nanoparticle Hybrid Materials for Small Molecule Delivery. Journal of nanomedicine & nanotechnology, 7(1), 356.
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4

Microfluidic Oocyte Manipulation Protocol

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The fluids were driven and controlled using a PHD 2000 dual syringe pump (Harvard Apparatus, Holliston, MA), which supplies the buffers or media at an adjustable rate. Five-ml syringes (Becton Dickenson, Franklin Lakes, NJ) were utilized for each. In these experiments a fast flow rate of 10 μl/min was utilized for flushing the chip, and a slower flow rate of 50 μl/hr for development, live cell imaging and studies with fixed oocytes. The pump was run using the refill mode to pull fluid from the inlet well through the chip. The inlet reservoir is open and allows for easy addition of buffers, dyes, or media using a standard 200μl pipette. A one way check valve (Smart Products Inc., Morgan Hill, CA) was used at the outlet of the chip in order to minimize and eliminate any backflow through the device. For experiments requiring temperature control, a standard temperature control plate (Isotemp 3016S, Fisher Scientific, Pittsburgh, PA) for the microscope stage was utilized at 16°C for sea stars and 37°C for mammalian oocytes. Since the media was equilibrated at the same temperature on the stage, we noticed no bubble formation from temperature differentials and degassing was not required.
Angione S.L., Oulhen N., Brayboy L.M., Tripathi A, & Wessel G.M. (2014). Simple Perfusion Apparatus (SPA) for Manipulation, Tracking and Study of Oocytes and Embryos. Fertility and sterility, 103(1), 281-90.e5.
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5

Stopped-Flow Absorption Spectroscopy of Proteins

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Stopped-flow
data were obtained using an Applied Photophysics SX.19 stopped-flow
absorption spectrophotometer equipped with a Hg/Xe arc lamp and a
PDA1 photodiode array detector in a purge box (Cleatech Isolation
Glove Box 2100) equipped with an oxygen sensor (Neutronics Model 1100).
Stopped-flow experiments were conducted at 4 °C and maintained
using a water/ethanol temperature bath (Fisher Scientific Isotemp
3016) with a cell path length of 1 cm. All solutions were freshly
prepared in an anaerobic glovebox. Both injector ports of the stopped-flow
apparatus were degassed with ∼3.0 mM sodium dithionite for
∼20 min and then washed with the degassed buffer thoroughly.
The protein samples were loaded on the stopped-flow apparatus at concentrations
of ∼50 μM.
Tian S., Jones S.M, & Solomon E.I. (2020). Role of a Tyrosine Radical in Human Ceruloplasmin Catalysis. ACS Central Science, 6(10), 1835-1843.
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6

Stopped-Flow Kinetic Assay for Oxygen Binding

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All stopped flow experiments were conducted at 4 °C. Deoxygenated protein and buffer were prepared. Two injection ports on the stopped flow instrument were degassed with ~3.0 mM sodium dithionite for ~20 min and kept anaerobic with a gaseous nitrogen flow. All protein samples were loaded on the stopped flow at concentrations of 200–250 μM. O2-saturated buffer was prepared by purging buffer (on ice) with O2 gas for 15 min. O2-saturated buffer was added to the protein solution in a 1:1 ratio to obtain a final protein concentration of 100–125 μM. An Applied Photophysics SX20 stopped flow absorption spectrophotometer with a Hg/Xe Arc lamp, PEEK tubing, and a Fisher Scientific Isotemp 3016 water/ethanol bath for controlling temperature was used.
Snyder R.A., Betzu J., Butch S.E., Reig A.J., DeGrado W.F, & Solomon E.I. (2015). Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins. Biochemistry, 54(30), 4637-4651.
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7

Rheological Analysis of Milk Gelation

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The rheometer was used to measure the apparent viscosity of samples and follow the gel formation process. The apparent viscosity of different samples before renneting was measured using a shear rate ramp from 10 to 100 s -1 applied with a controlled stress rheometer (AR 1000, TA Instruments Ltd., New Castle, DE) at 25°C. The sample was loaded on a cone and plate geometry with a set gap of 0.51 mm. The values are reported for viscosity measured at 100 s -1 .
The gel formation process of skim and concentrated milk was followed by oscillatory measurements, using a constant strain of 0.01 and a frequency of 1 Hz. In this case, a concentric cylinder (28 and 30 mm inner and outer cylinders diameter, respectively) and an external water bath (Isotemp 3016, Fisher Scientific) were used to control the temperature at 30°C. Aliquots (20 mL) of sample were transferred to the cylinder within 5 min after the addition of chymosin. The milk gelation point was defined as the point when the elastic modulus (G ) and viscous modulus (G ) cross over (tan δ = 1; Lucey et al., 1998) . This point corresponds to a steep increase in the storage modulus (G ) over time.
Zhao Z, & Corredig M. (2016). Influence of sodium chloride on the colloidal and rennet coagulation properties of concentrated casein micelle suspensions. Journal of dairy science, 99(8).
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