Ultimate 3000

Manufactured by Agilent Technologies

Sourced in United States

The Ultimate 3000 is a high-performance liquid chromatography (HPLC) system designed for a wide range of analytical applications. It features advanced technology for reliable and reproducible results.

Automatically generated - may contain errors

Lab products found in correlation

Eclipse plus c18, by Agilent Technologies (3 mentions) Minidawn treos, by Wyatt Technology (2 mentions) Optilab t rex refractive index detector, by Wyatt Technology (2 mentions) Zorbax extend c18 column, by Agilent Technologies (2 mentions) C18 column, by Agilent Technologies (2 mentions) Sb c18 column, by Agilent Technologies (2 mentions) Nanodrop one, by Thermo Fisher Scientific (2 mentions) Superdex 75 10 300, by GE Healthcare (1 mentions) Superdex 200 10 300, by GE Healthcare (1 mentions) Unity 400, by Agilent Technologies (1 mentions) Kiesel gel 60 rp 18f254s, by Merck Group (1 mentions) Plc 2020, by Gilson (1 mentions) Dionex ultimate 3000, by Thermo Fisher Scientific (1 mentions) Kieselgel 60 f254, by Merck Group (1 mentions) Sephadex lh 20, by Merck Group (1 mentions) 1260 infinity, by Agilent Technologies (1 mentions) Silica gel, by Silicycle (1 mentions) 6540 q tof, by Agilent Technologies (1 mentions) Q exactive, by Thermo Fisher Scientific (1 mentions) Rslcnano3000, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

UltiMate 3000 UHPLC (5 citations) UltiMate 3000 system (3 citations) UltiMate™ 3000 HPLC (2 citations) Ultimate 3000 chromatographic system (2 citations) UltiMate 3000 HPLC system (2 citations) UltiMate 3000 UHPLC system (2 citations) Ultimate 3000 LC (2 citations)

22 protocols using ultimate 3000

HPLC Quantification of Muconic Acid

Check if the same lab product or an alternative is used in the 5 most similar protocols

Both the standard and samples were analyzed and quantified by reverse phase HPLC (Dionex Ultimate 3000) equipped with a ZORBAX SB-C18 column and an Ultimate 3000 photodiode array detector. Solvent A was water with 0.1% formic acid, and solvent B was methanol. The column temperature was set to 28 °C. The HPLC program was set at a flow rate of 1 mL min⁻¹ with gradient concentrations: 5–50% solvent B for 15 min, 50–5% solvent B for 1 min, and 5% solvent B for additional 4 min. Quantification of muconic acid was based on the peak areas at absorbance of 260 nm.

Yang Y., Lin Y., Wang J., Wu Y., Zhang R., Cheng M., Shen X., Wang J., Chen Z., Li C., Yuan Q, & Yan Y. (2018). Sensor-regulator and RNAi based bifunctional dynamic control network for engineered microbial synthesis. Nature Communications, 9, 3043.

+ Open protocol

+ Expand

SEC-MALS Analysis of Protein Complexes

Check if the same lab product or an alternative is used in the 5 most similar protocols

For the SEC-MALS experiment at 25°C, a Superdex200 10/300 or a Superdex75 10/300 (GE Healthcare) column was equilibrated in Tris (20 mM Tris-HCl, pH 7.5, supplemented with 150 mM NaCl and 1 mM DTT; Bik1-CC, Kip2-NMD, and Kip2-NMD-ΔT) or Hepes buffers (20 mM Hepes, pH 7.4, supplemented with 200 mM NaCl and 1 mM DTT; MBP-Kip2-MD, MBP-Kip2-MD-P1, and tubulin) at a flow rate of 0.5 ml/min on an Agilent UltiMate3000 HPLC. 30 μl of the respective single protein or complex was injected onto the column, and the mass was determined using the miniDAWN TREOS and Optilab T-rEX refractive index detectors (Wyatt Technology). For the Bik1-CC, Kip2-NMD, Kip2-NMD-ΔT, MBP-Kip2(71-560)-mCherry, MBP-Kip2(71-560)-P1⁻-mCherry, and tubulin 4–8 mg/ml were applied. In case of the experiments with mixtures of proteins, the individual concentrations of the components were maintained. The Zimm model was chosen for data fitting that was performed in the ASTRA 6 software.

Chen X., Portran D., Widmer L.A., Stangier M.M., Czub M.P., Liakopoulos D., Stelling J., Steinmetz M.O, & Barral Y. (2023). The motor domain of the kinesin Kip2 promotes microtubule polymerization at microtubule tips. The Journal of Cell Biology, 222(7), e202110126.

+ Open protocol

+ Expand

Identification and Characterization of Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols

Analysis of NMR spectra was carried out through Varian UNITY 400 (Varian, Inc., Palo Alto, CA) FT-NMR spectrometer using the tetramethylsilane as an internal standard. Waters Q-Tof Premier spectrometer (Micromass UK Ltd., Manchester, UK) was used to obtain HR-ESI mass spectra. Sephadex LH-20 (25–100 µm, Sigma-Aldrich, Steinheim, Germany), silica gel (230–400 mesh, SiliCycle Inc., Quebec, Canada), and RP-C18 (Cosmosil 40C₁₈-PREP, Kyoto, Japan) were used for column chromatography. Thin layer chromatography (TLC) was performed on precoated Kiesel-gel 60 F₂₅₄ (0.25 mm, Merck, Darmstadt, Germany) and Kiesel-gel 60 RP-18F_254s (0.25 mm, Merck, Steinheim, Germany). HPLC analysis was conducted on Thermo Dionex Ultimate 3000 equipped with Ultimate 3000 pump, autosampler, column compartment and diode array detector and Agilent Technology model 1260 Infinity equipped with 1260 DAD. Columns used for the analysis were YMC Trait C18 ExRS (5 µm, 4.6 × 250 mm), Phenomenex synergy RP-Polar (5 µm, 4.6 × 250 mm), Thermo acclaim polar advantage (5 µm, 4.6 × 250 mm), and Atlantis T3 (5 µm, 4.6 × 250 mm). Preparative HPLC was carried out with a model Gilson PLC 2020. Preparative columns were Thermo acclaim polar advantage (5 µm, 21.2 × 250 mm), Atlantis (5 µm, 19 × 250 mm), and YMC Trait C18 ExRS (5 µm, 20 × 250 mm).

Pandey J., Hwang B.Y., Lee H.K, & Poudel A. (2022). Pimarane Diterpenoids from Aerial Parts of Lycopus lucidus and Their Antimicrobial Activity. Evidence-based Complementary and Alternative Medicine : eCAM, 2022, 5178880.

+ Open protocol

+ Expand

HPLC Analysis of Retinoic Acid

Check if the same lab product or an alternative is used in the 5 most similar protocols

A total of 31 batches of RA were analyzed by a HPLC system equipped with an evaporative light scattering detector and diode-array detector. Analysis was performed using a Thermo Fisher Ultimate 3000 HPLC system, and an Agilent C18 column (250 mm × 4.6 mm, 5 μm) with a flow rate of 1.0 ml/min (Du et al., 2014 (link); Chen et al., 2015 (link)). The mobile phase consisted of acetonitrile and deionized water (32%:68%). The injection volume was 10 μl, and the column component was set to a temperature of 30°C.

Bi Y., Bao H., Zhang C., Yao R, & Li M. (2020). Quality Control of Radix Astragali (The Root of Astragalus membranaceus var. mongholicus) Along Its Value Chains. Frontiers in Pharmacology, 11, 562376.

+ Open protocol

+ Expand

HPLC-MS Analysis of MCLR Biodegradation Products

Check if the same lab product or an alternative is used in the 5 most similar protocols

The MCLR biodegradation products in the crude extract were further separated using a Dionex Ultimate 3000 HPLC system equipped with an Agilent SB-C₁₈ column (9.4 × 250 mm, 5 µm). Firstly, 200 µL of the resuspended sample was injected into the column and eluted by water and acetonitrile (both mobile phases containing 0.1% trifluoroacetic acid). The gradient elution was programmed as follows: 0–5 min, 20% acetonitrile; 35–40 min, 80% acetonitrile; and 40.1–45 min, 20% acetonitrile (35 °C, 2 mL/min). The eluted sample was determined by a UHR-TOF mass spectrometer and the MS parameters were set as in Section 2.3. The separated and purified biodegradation products were collected around specific retention times, evaporated to dryness with N₂, and dissolved in 100 µL acetonitrile.

Ren L., Hu Z., Wang Q., Du Y, & Zong W. (2020). Regulation Efficacy and Mechanism of the Toxicity of Microcystin-LR Targeting Protein Phosphatase 1 via the Biodegradation Pathway. Toxins, 12(12), 790.

+ Open protocol

+ Expand

Peptide Fractionation and Concentration

Check if the same lab product or an alternative is used in the 5 most similar protocols

TMT-labelled tryptic peptides were subjected to HpRP-HPLC fractionation using a Dionex Ultimate 3000 powered by an ICS-3000 SP pump with an Agilent ZORBAX Extend-C18 column (4.6 mm × 250 mm, 5 μm particle size). Mobile phases (H₂0, 0.1% NH_4°H or MeCN, 0.1% NH_4°H) were adjusted to pH 10.5 with the addition of formic acid and peptides were resolved using a linear 40 min 0.1–40 % MeCN gradient over 40 min at a 400 μl/min flow rate and a column temperature of 15°C. Eluting peptides were collected in 15 s fractions. One hundred and twenty fractions covering the peptide-rich region were re-combined to give 10 samples for analysis. To preserve orthogonality, fractions were combined across the gradient, with each of the concatenated samples comprising 12 fractions which were 10 fractions apart. Re-combined fractions were dried down using an Eppendorf Concentrator (Eppendorf, UK) and resuspended in 15 µl MS solvent (3% MeCN, 0.1% TFA)

Greenwood E.J., Matheson N.J., Wals K., van den Boomen D.J., Antrobus R., Williamson J.C, & Lehner P.J. (2016). Temporal proteomic analysis of HIV infection reveals remodelling of the host phosphoproteome by lentiviral Vif variants. eLife, 5, e18296.

+ Open protocol

+ Expand

HPLC Analysis of Bisphenol A (BPA)

Check if the same lab product or an alternative is used in the 5 most similar protocols

The concentration of BPA was analyzed on DIONEX UltiMate 3000 HPLC with a C-18 column (Agilent, 5 μm, 250 × 4.6 mm) and equipped with a UV/vis photodiode array detector, and the BPA was detected using UV absorbance at 278 nm. The mobile phase for the detection of BPA consisted of 80% MeOH and 20% water (0.2% HAc) (v/v) at a constant flow rate of 1.0 mL/min. The column temperature and injection volume were set at 25 °C and 20 μL, respectively.

Qu H., Chen L., Yang F., Zhu J., Qi C, & Peng G. (2023). Synthesis of an Environmentally Friendly Modified Mulberry Branch-Derived Biochar Composite: High Degradation Efficiency of BPA and Mitigation of Toxicity in Silkworm Larvae. International Journal of Molecular Sciences, 24(4), 3609.

+ Open protocol

+ Expand

Microwave-Assisted Peptide Synthesis and Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols

Peptide synthesis was performed on Rink amide resin with a microwave assisted peptide synthesizer (CEM DiscoverBio) using standard Fmoc solid phase peptide synthesis and HBTU activation with DIEA (0.5 M) in NMP.³⁸ Coupling reactions were generally performed for 6 min at 75 °C, except for cysteine (C) and arginine (R) which were coupled for 6 min at 50 °C, and 25 min at room temperature then 5 min at 75 °C, respectively. Fmoc protecting groups were deprotected with piperidine (20%) in NMP for 5 min at 75 °C. The peptide was cleaved by treatment with 90:5:2.5:2.5 (TFA:phenol:TIS:water) for 2 hrs at room temperature followed by precipitation in cold diethyl ether. Crude peptide was purified by reverse-phase high performance liquid chromatography (HPLC, Thermo Scientific UltiMate 3000 with Agilent Technologies C18 column, ACN in water with 0.01% TFA) and lyophilized (Supporting Information, Figure S1). Purified product was analyzed via matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) to verify peptide composition (Supporting Information, Figure S2). Peptides were dissolved in PBS and absorbance measurements at 205 nm and 280 nm (Thermo Scientific Nanodrop One) were taken to calculate the stock concentrations.^{39 (link)} MALDI-TOF MS: KCGPQGIAGQCK [M+H] = 1188.513 (expected), 1189 (found); CGRGDSGC [M+H] = 753.242 (expected), 752.9 (found).

Jivan F., Fabela N., Davis Z, & Alge D.L. (2018). Orthogonal click reactions enable the synthesis of ECM-mimetic PEG hydrogels without multi-arm precursors. Journal of materials chemistry. B, 6(30), 4929-4936.

+ Open protocol

+ Expand

Identification of GC Intermediates by UHPLC-QTOF

Check if the same lab product or an alternative is used in the 5 most similar protocols

Identification of GC intermediates was
achieved during PBCD/Fe-ACF treatment using an Agilent 1290
ultrahigh-performance liquid chromatography (UHPLC, Dionex UltiMate
3000, USA) coupled with a QTOF mass spectrometer (Agilent 6540
QTOF, USA). The mass spectrometer scan was performed in negative
ion mode during analysis. Samples were withdrawn at 0, 20, and
60 min. The GC intermediates were screened based on the difference
in concentration from 0 min. Detailed information is displayed in
Text S2 in the SI.

Gao X., Huang K., Zhang A., Wang C., Sun Z, & Liu Y. (2021). Simultaneous degradation of glucocorticoids and sterilization using bubbling corona discharge plasma based systems: A promising terminal water treatment facility for hospital wastewater. Chemical Engineering Journal, 430, 132845.

+ Open protocol

+ Expand

High-Resolution Fractionation and Mass Spectrometry of Tryptic Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols

HpRP-HPLC was performed on tryptic peptides as described previously [28 (link)]. 90% of each tryptic peptide sample was subjected to HpRP-HPLC fractionation using a Dionex Ultimate 3000 powered by an ICS-3000 SP pump with an Agilent ZORBAX Extend-C18 column (4.6 mm x 250 mm, 5 μm particle size). Peptides were resolved using a linear 40 min 0.1%-40% acetonitrile gradient at pH 10.5. Eluting peptides were collected in 15s fractions. For THP-1 experiments, a total of 30 combined fractions were generated then dried using an Eppendorf Concentrator for LC-MSMS using a NanoAcquity uPLC (Waters, MA, USA) coupled to an LTQ-OrbiTrap XL (Thermo, FL, UA). MS data was acquired between 300 and 2000 m/z at 60,000 fwhm with CID spectra acquired in the LTQ with MSMS switching operating in a top 6 DDA fashion. Fractionated HFF experiments were re-combined to give either 40 or 10 fractions. The 40 fraction experiments were acquired using the OrbiTrap XL as above. The 10 fraction experiments were acquired using a Q Exactive (Thermo) coupled to a RSLC nano3000 (Thermo) with MS data acquired between 400 and 1650 m/z at 75,000 fwhm with HCD fragment spectra acquired in a top 10 DDA fashion.

Hsu J.L., van den Boomen D.J., Tomasec P., Weekes M.P., Antrobus R., Stanton R.J., Ruckova E., Sugrue D., Wilkie G.S., Davison A.J., Wilkinson G.W, & Lehner P.J. (2015). Plasma Membrane Profiling Defines an Expanded Class of Cell Surface Proteins Selectively Targeted for Degradation by HCMV US2 in Cooperation with UL141. PLoS Pathogens, 11(4), e1004811.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!