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Sutter p 97 puller

Manufactured by Sutter Instruments
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The Sutter P-97 puller is a laboratory instrument designed for the precise and controlled pulling of glass micropipettes and electrodes. It utilizes a microprocessor-controlled, programmable heating and pulling sequence to produce pipettes of desired geometries. The P-97 puller offers a range of adjustable parameters to accommodate a variety of glass types and sizes.

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Lab products found in correlation

Pclamp 10, by Molecular Devices (4 mentions) Lct 1 mass spectrometer, by Waters Corporation (3 mentions) Soda lime capillary glass, by Thermo Fisher Scientific (3 mentions) Clampex 10, by Molecular Devices (3 mentions) Multiclamp 700b amplifier, by Molecular Devices (3 mentions) R6101, by Dow (2 mentions) Axopatch 200b, by Molecular Devices (2 mentions) E 625 cr controller, by Physik Instrumente (1 mentions) Cyberamp 320, by Molecular Devices (1 mentions) P 621.1cd, by Physik Instrumente (1 mentions) Digidata 1550a, by Molecular Devices (1 mentions) Amicon ultra 0.5 centrifugal filter unit, by Merck Group (1 mentions) Masslynx v4, by Waters Corporation (1 mentions) Digidata 1322a digitizer, by Molecular Devices (1 mentions) Pulse software, by HEKA Elektronik (1 mentions) Epc 10 amplifier, by HEKA Elektronik (1 mentions) Digidata 1440, by Molecular Devices (1 mentions) Rapamycin, by Thermo Fisher Scientific (1 mentions) Axopatch 200b amplifier, by Molecular Devices (1 mentions) Digidata 1322a, by Molecular Devices (1 mentions)

17 protocols using sutter p 97 puller

1

Mass Spectrometry Analysis of IgG Species

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Example 8

Mass Spectrometry was used to identify the different IgG species in the purified IgG mixtures and to establish in what ratios these IgG species are present. Briefly, 2-3 μl at a 1 μM concentration in 150 mM ammonium acetate pH 7.5 of IgG's were loaded into gold-plated borosilicate capillaries made in-house (using a Sutter P-97 puller [Sutter Instruments Co., Novato, Calif., USA] and an Edwards Scancoat six sputter-coater [Edwards Laboratories, Milpitas, Calif., USA]) for analysis on a LCT 1 mass spectrometer (Waters Corp., Milford, Mass., USA), adjusted for optimal performance in high mass detection (Tahallah et al., RCM 2001). A capillary voltage of 1300 V was used and a sampling cone voltage of 200 V; however, these settings were adjusted when a higher resolution of the ‘signal-to-noise’ ratio was required. The source backing pressure was elevated in order to promote collisional cooling to approximately 7.5 mbar. To measure the IgG1's under denaturing conditions the proteins were sprayed at a 1 μM concentration in 5% formic acid.

US10337045B2. Methods and means for the production of Ig-like molecules (2019-07-02). Merus N.V. [NL]. Inventors: Cornelis Adriaan De Kruif [NL], Linda Johanna Aleida Hendriks [NL], Ton Logtenberg [NL].
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2

Patch-Clamp Recordings of DRG Neurons

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Electrophysiological experiments were carried out as described previously.29 (link) Whole-cell patch clamp recordings were carried out at room temperature (22–25°C) using a MultiClamp-700B amplifier (Axon Instruments, CA, USA). The isolated DRG neurons were transferred to a 35 mm culture dish and kept in normal external solution for at least 60 min before electrophysiological recordings. The external solution contained the following (in mM): 150 NaCl, 5 KCl, 2 MgCl2, 2.5 CaCl2, 10 HEPES, 10 d-glucose. Its pH and osmolarity were adjusted to 7.4 with NaOH and 330 mOsm/L with sucrose, respectively. Recording pipettes were pulled using a Sutter P-97 puller (Sutter Instruments, CA, USA) and its resistance was in the range of 3–6MΩ. The micropipette solution contained (in mM): 140 KCl (or CsCl), 2 MgCl2, 11 EGTA, 10 HEPES, 4 ATP, and 0.3 Na2GTP. Its pH and osmolarity were adjusted to 7.2 with KOH and 310 mOsm/L with sucrose, respectively. In the present experiment, DRG neurons with a diameter of 15–35μm were used for electrophysiological recording. After whole-cell configuration established, 70–80% series resistance and membrane capacitance current were compensated. The recording currents were sampled at 10 kHz and filtered at 2 kHz. Data detection and analysis were performed using the pCLAMP 10 software (Axon Instruments, CA, USA).
Jin Y., Wei S., Liu T.T., Qiu C.Y, & Hu W.P. (2021). Acute P38-Mediated Enhancement of P2X3 Receptor Currents by TNF-α in Rat Dorsal Root Ganglion Neurons. Journal of Inflammation Research, 14, 2841-2850.
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3

Identifying IgG Species by Mass Spectrometry

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Example 8

Mass Spectrometry was used to identify the different IgG species in the purified IgG mixtures and to establish in what ratios these IgG species are present. Briefly, 2-3 μl at a 1 μM concentration in 150 mM ammonium acetate pH 7.5 of IgG's were loaded into gold-plated borosilicate capillaries made in-house (using a Sutter P-97 puller [Sutter Instruments Co., Novato, Calif., USA] and an Edwards Scancoat six sputter-coater [Edwards Laboratories, Milpitas, Calif., USA]) for analysis on a LCT 1 mass spectrometer (Waters Corp., Milford, Mass., USA), adjusted for optimal performance in high mass detection (Tahallah et al., RCM 2001). A capillary voltage of 1300 V was used and a sampling cone voltage of 200 V; however, these settings were adjusted when a higher resolution of the ‘signal-to-noise’ ratio was required. The source backing pressure was elevated in order to promote collisional cooling to approximately 7.5 mbar. To measure the IgG1's under denaturing conditions the proteins were sprayed at a 1 μM concentration in 5% formic acid.

US10329596B2. Methods and means for the production of Ig-like molecules (2019-06-25). Merus N.V. [NL]. Inventors: Cornelis Adriaan De Kruif [NL], Linda Johanna Aleida Hendriks [NL], Ton Logtenberg [NL].
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4

Patch Clamp Electrophysiology Technique

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Patch pipettes were manufactured from soda lime capillary glass (Fisher), using a Sutter P-97 puller (Sutter Instrument). When filled with standard recording solutions, pipettes had a tip resistance of 1–3 MΩ. Recordings were filtered at 5 kHz, sampled at 10 kHz, with manual capacitance compensation and series resistance compensation between 70 and 90%, and stored directly on a computer hard drive using Clampex 10 software (Molecular Devices). Bath solution had the following composition: 135 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, 10 mM HEPES, and was adjusted to pH 7.3 with NaOH. Pipette solution had the following composition: 135 mM KCl, 5 mM K-EGTA, 10 mM HEPES and was adjusted to pH 7.2 using KOH. Chemicals were purchased from Sigma-Aldrich or Fisher.
Baronas V.A., Yang R.Y., Morales L.C., Sipione S, & Kurata H.T. (2018). Slc7a5 regulates Kv1.2 channels and modifies functional outcomes of epilepsy-linked channel mutations. Nature Communications, 9, 4417.
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5

Patch Clamp Electrophysiology Protocol

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Patch pipettes were manufactured from soda lime capillary glass (Fisher), using a Sutter P-97 puller (Sutter Instrument). When filled with standard recording solutions, pipettes had a tip resistance of 1–3 MΩ. Recordings were filtered at 5 kHz, sampled at 10 kHz, with manual capacitance compensation and series resistance compensation between 70–90%, and stored directly on a computer hard drive using Clampex 10 software (Molecular Devices). Bath solution had the following composition: 135 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, 10 mM HEPES, and was adjusted to pH 7.4 with NaOH. Pipette solution had the following composition: 135 mM KCl, 5 mM K-EGTA, 10 mM HEPES and was adjusted to pH 7.2 using KOH. Chemicals were purchased from Sigma-Aldrich or Fisher.
Unless otherwise indicated, recordings in reducing conditions were carried out by incubating cells in the indicated reducing agent (diluted in serum-free DMEM media) for 5–20 min prior to recording. During the recordings, cells were continuously bathed in extracellular solution with the indicated reducing agent. All reducing agents were stored as stock solutions at −20 °C and diluted just prior to experimental use to minimize spontaneous oxidation. For intracellular application of reducing agents, cells were held for five minutes after whole-cell break-in before recording, to allow equilibration with the pipette solution.
Baronas V.A., Yang R.Y, & Kurata H.T. (2017). Extracellular redox sensitivity of Kv1.2 potassium channels. Scientific Reports, 7, 9142.
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6

Patch-Clamp Recording of Mechanically-Induced Currents

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Patch-clamp recordings were performed using HEKA EPC-10 and Patchmaster v2 × 71 software as previously described [37 (link), 39 (link), 40 (link)]. Mechanically induced currents were recorded in small diameter (< 20 μm) and large diameter (> 30 μm) sensory neurons with glass pipettes (3–5 MΩ resistance) fabricated from borosilicate glass capillaries using a Sutter P-97 puller (Sutter Instruments, Novato, CA, USA). The external solution contained (in mmol/L): 127 NaCl, 3 KCl, 1 MgCl2, 10 HEPES, 2.5 CaCl2 and 10 glucose (pH adjusted to 7.3 with NaOH). The internal solution contained (in mmol/L): 133 CsCl, 10 HEPES, 5 EGTA, 1 CaCl2, 1 MgCl2, 4 MgATP and 0.4 Na2GTP (pH adjusted to 7.3 with CsOH). The membrane holding potential was − 80 mV. Mechanical stimulation was applied to neurons or cells using a fire-polished glass pipette (tip diameter 3–5 μm) positioned at an angle of 60°, and the probe displacement was advanced in increments of 1 μm.
Xie M.X., Lai R.C., Xiao Y.B., Zhang X., Cao X.Y., Tian X.Y., Chen A.N., Chen Z.Y., Cao Y., Li X, & Zhang X.L. (2024). Endophilin A2 controls touch and mechanical allodynia via kinesin-mediated Piezo2 trafficking. Military Medical Research, 11, 17.
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7

Alexa Fluor 594 Dye Injection Protocol

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Dye injections were performed as described previously (Meyer et al., 2014 (link)). Briefly, borosilicate glass electrodes were pulled with a Sutter P-97 puller (Sutter, Novato, CA, USA). Electrode tips were filled with 5 mM Alexa Fluor 594 diluted in 0.2 M KCl. Electrodes were then backfilled with 0.2 M KCl. Electrodes typically had resistances between 100 and 200 MΩ. AII amacrine cells were targeted for injection under epifluorescence in the DAPI-stained retina. The dye was iontophoresed with −0.5 nA square pulses of 500 ms at 1 Hz for 5–10 min. The dye was allowed to diffuse for at least 30 min prior to fixation.
Tetenborg S., Yadav S.C., Hormuzdi S.G., Monyer H., Janssen-Bienhold U, & Dedek K. (2017). Differential Distribution of Retinal Ca2+/Calmodulin-Dependent Kinase II (CaMKII) Isoforms Indicates CaMKII-β and -δ as Specific Elements of Electrical Synapses Made of Connexin36 (Cx36). Frontiers in Molecular Neuroscience, 10, 425.
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8

Whole-Cell Voltage-Clamp and Mechanical Stimulation

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Standard whole-cell voltage clamp and mechanical stimulation by a piezoelectric-driven glass probe were used as described previously (11 (link), 21 (link)). Electrodes (Kimble KG12 glass) were pulled by Sutter P97 puller (Sutter Instruments), coated with R6101 (Dow Corning), and fire-polished to 2–5 MΩ. Stimulation and data acquisition were done with an Axopatch 200B patch-clamp amplifier, CyberAmp 320 signal conditioner, Digidata 1550A, and pClamp 10.5 software (Molecular Devices). Whole-cell voltage-clamp signals were sampled at 20 kHz and filtered at 4 kHz. Series resistance was compensated in all whole-cell recordings. Cells held at −120 mV, and voltage-dependent currents were recorded from −80 through +15 mV in 5-mV steps for 50 ms to measure steady-state activation, then stepped to 0 mV for 50 ms to measure steady-state inactivation. The start-to-start time was 250 ms per sweep and 6 s per run for up to 10 runs. Mechanical stimulation was applied as stated in results via fire-polished glass microelectrodes driven by a piezotransducer P-621.1CD attached to an E-625.CR controller (Physik Instrumente). Displacement ladders were 50-ms steps of 0.3-µm increments at a 0.6-µm/ms upstroke/downstroke rate.
Alcaino C., Knutson K.R., Treichel A.J., Yildiz G., Strege P.R., Linden D.R., Li J.H., Leiter A.B., Szurszewski J.H., Farrugia G, & Beyder A. (2018). A population of gut epithelial enterochromaffin cells is mechanosensitive and requires Piezo2 to convert force into serotonin release. Proceedings of the National Academy of Sciences of the United States of America, 115(32), E7632-E7641.
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9

Mass Spectrometry Analysis of IgG Mixtures

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Example 8

Mass Spectrometry was used to identify the different IgG species in the purified IgG mixtures and to establish in what ratios these IgG species are present. Briefly, 2-3 μl at a 1 μM concentration in 150 mM ammonium acetate pH 7.5 of IgG's were loaded into gold-plated borosilicate capillaries made in-house (using a Sutter P-97 puller [Sutter Instruments Co., Novato, Calif., USA] and an Edwards Scancoat six sputter-coater [Edwards Laboratories, Milpitas, Calif., USA]) for analysis on a LCT 1 mass spectrometer (Waters Corp., Milford, Mass., USA), adjusted for optimal performance in high mass detection (Tahallah et al., RCM 2001). A capillary voltage of 1300 V was used and a sampling cone voltage of 200 V; however, these settings were adjusted when a higher resolution of the ‘signal-to-noise’ ratio was required. The source backing pressure was elevated in order to promote collisional cooling to approximately 7.5 mbar. To measure the IgG1's under denaturing conditions the proteins were sprayed at a 1 μM concentration in 5% formic acid.

US10752929B2. Methods and means for the production of ig-like molecules (2020-08-25). Merus N.V. [NL]. Inventors: Cornelis Adriaan De Kruif [NL], Linda Johanna Aleida Hendriks [NL], Ton Logtenberg [NL].
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10

Mass Spectrometry Analysis of TH-14-3-3γ Complexes

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Purified samples (14-3-3γ, nonphosphorylated TH, TH-pSer19, and TH-pSer19pSer40) were exchanged into 150 mM ammonium acetate, pH 7.5 or pH 6.1, using 10-kDa molecular weight cut-off spin-filter columns (Amicon Ultra-0.5 Centrifugal Filter Unit, Millipore, Billerica, MA). 2 μl of each sample were sprayed at a concentration of 5 μM on an electrospray ionization TOF mass spectrometer (LCT, Waters, Manchester, UK). In particular, for the analysis of the complexes, TH (nonphosphorylated TH, TH-pS19, or TH-pS19pS40) and 14-3-3γ samples were prepared at both 1:0.5 and 1:3 molar subunit mixing ratios. Gold-coated borosilicate capillaries, made in-house for nano-electrospray (using a Sutter P-97 puller (Sutter Instruments Co., Novato, CA) and an Edwards Scancoat Six sputter-coater (Edwards Laboratories, Milpitas, CA)), were used to directly infuse the samples into the instrument. Source backing pressure was increased to 6.5 mbar. Mass calibration was performed using 25 mg/ml CsI. MassLynx V4.1 (Waters) was used for data analysis and therefore for experimental mass determination.
Kleppe R., Rosati S., Jorge-Finnigan A., Alvira S., Ghorbani S., Haavik J., Valpuesta J.M., Heck A.J, & Martinez A. (2014). Phosphorylation Dependence and Stoichiometry of the Complex Formed by Tyrosine Hydroxylase and 14-3-3γ. Molecular & Cellular Proteomics : MCP, 13(8), 2017-2030.
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