Kinetex 2.6 μm c18 100 column

Manufactured by Phenomenex

Sourced in United States

The Kinetex 2.6 μm C18 100 Å column is a high-performance liquid chromatography (HPLC) column designed for analytical applications. The column features a core-shell particle technology with a 2.6 μm particle size and a 100 Å pore size. This combination provides efficient separation and high resolution for a wide range of analytes.

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Lab products found in correlation

Standard reagent, by Merck Group (1 mentions) Lc 20ad, by Shimadzu (1 mentions) Api 5500 mass spectrometer, by AB Sciex (1 mentions) Sil 20ac, by Shimadzu (1 mentions) Luna c8, by Phenomenex (1 mentions) Apl1100, by Agilent Technologies (1 mentions) Dionex 500, by Thermo Fisher Scientific (1 mentions) Victor multilabel plate reader, by PerkinElmer (1 mentions) Db 5 analytical column, by Agilent Technologies (1 mentions) Combipal autosampler, by CTC Analytics (1 mentions) Pepsin, by Abcam (1 mentions) Neutrophil elastase, by Abcam (1 mentions) Kinetex 2.6 μm hilic 100 column, by Phenomenex (1 mentions)

Spelling variants of this product

Kinetex C18 column (513 citations) C18 column (366 citations) Kinetex C18 (225 citations) Kinetex column (60 citations) Kinetex C18 100 Å column (14 citations) Kinetex C18 100 Å (9 citations) Kinetex 2.6 μm C18 column (5 citations) Kinetex 2.6 μm (5 citations) Kinetex C18 2.6 μm (2 citations) Kinetex 2.6 μm C18 100 x 3 mm 100Å column (2 citations)

8 protocols using kinetex 2.6 μm c18 100 column

Automated Synthesis of [11C]PiB Radiotracer

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The precursor (6-OH-BTA-0) was obtained from ABX advanced biochemical compounds GmbH (Radeberg, Germany), standard reagents were obtained from Sigma-Aldrich/Merk, sterile solutions were obtained from Herlev University Hospital Pharmacy (Herlev, Denmark), and sterile Millex-GS 0.22 µm filters (SLGSV255F) were obtained from Merck Millipore. 2-butanone was dried over molecular sieves (4 Å), and the sieves were heated to 250 °C for 24 h and cooled to room temperature prior to use. [¹¹C]CH₄ was produced using an IBA Cyclone 18/18 cyclotron (Table 3) by the bombardment of the target gas, 95% N₂ + 5% H₂ (Air Products).
The automated [¹¹C]PiB radiosynthesis and product isolation was performed on a TracerMaker synthesis module (Scansys Laboratorieteknik ApS, Denmark) with a semi-preparative HPLC system with Knauer pumps (AZURA P 2.1S/P 4.1S pumps) and a Kinetex@ 2.6 μm C18 100 Å column (50 × 4.6 mm, Phenomenex). See Table 2 for details on the semi-preparative HPLC eluents and flowrates. See Section S2 (Supplementary Materials) for a detailed description of the radiosynthesis and product isolation process.

Andersen A.B., Lehel S., Grove E.K., Langkjaer N., Fuglø D, & Huynh T.H. (2024). Multicenter Experience with Good Manufacturing Practice Production of [11C]PiB for Amyloid Positron Emission Tomography Imaging. Pharmaceuticals, 17(2), 217.

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Sortase-Mediated Peptide Ligation Assay

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Reactions were generally conducted on 200 μL scale. Stock solutions of peptide substrate, glycine nucleophile, and metal additive were prepared in water and combined with SrtA_staph in appropriate ratios to give the desired final reagent concentrations. Unless indicated otherwise, final reagent concentrations of 100 μM peptide substrate, 100 μM glycine nucleophile, 10 μM SrtA_staph, and 0/200 μM NiSO₄ were employed. All reactions also contained 10% (v/v) 10x sortase reaction buffer (500 mM Tris (pH 7.5), 1500 mM NaCl, 100 mM CaCl₂), as well as residual glycerol (0.2% v/v) from the SrtA_staph stock solution. Reactions were incubated at room temperature and analyzed by LC-ESI-MS and RP-HPLC (Phenomenex Kinetex^® 2.6 μm C18 100 Å column (100 × 2.1 mm), aqueous (95% H₂O, 5% MeCN, 0.1% formic acid) / MeCN (0.1% formic acid) mobile phase at 0.4 mL/min, gradient adjusted for each substrate/nucleophile pair to ensure separation of all reaction components). Estimates of reaction progress were obtained by comparing peak areas for the unreacted substrate peptide, ligation product, and hydrolysis by-product from the 360 nm RP-HPLC chromatograms.

Reed S.A., Brzovic D.A., Takasaki S.S., Boyko K.V, & Antos J.M. (2020). Efficient Sortase-Mediated Ligation using a Common C-terminal Fusion Tag. Bioconjugate chemistry, 31(5), 1463-1473.

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Sortase-Mediated Ligation Optimization

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Select pairings of sortase enzyme (5 μM or 10 μM for the X-NH₂ reactions), substrate (50 μM), and nucleophile (5 mM H₂NOH or X-NH₂) were repeated in the presence or absence of Ca²⁺ under reaction conditions that were otherwise identical to those described above for the fluorescence assay. These reactions were then analyzed using a Dionex UltiMate 3000 HPLC system interfaced with an Advion CMS expression mass spectrometer. Separations were achieved with a Phenomenex Kinetex 2.6 μM C18 100 Å column (100 × 2.1 mm) (aqueous [95% water, 5% MeCN, 0.1% formic acid]/MeCN [0.1% formic acid] mobile phase at 0.3 ml/min, method: hold 10% MeCN for 0.0–0.5 min, linear gradient of 10–90% MeCN for 0.5–7.0 min, hold 90% MeCN for 7.0–8.0 min, linear gradient of 90–10% MeCN for 8.0–8.1 min, re-equilibrate at 10% MeCN for 8.1–13.25 min]).

Piper I.M., Struyvenberg S.A., Valgardson J.D., Johnson D.A., Gao M., Johnston K., Svendsen J.E., Kodama H.M., Hvorecny K.L., Antos J.M, & Amacher J.F. (2021). Sequence variation in the β7–β8 loop of bacterial class A sortase enzymes alters substrate selectivity. The Journal of Biological Chemistry, 297(2), 100981.

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HPLC-MS/MS Analysis of Rat Plasma

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Analysis of rat plasma was performed on a high-performance liquid chromatography−tandem mass spectrometry (HPLC−MS/MS) system consisting of an API 5500 Mass Spectrometer (AB Sciex, Foster City, CA, USA), Shimadzu LC-20AD and Shimadzu SIL-20 A C (Shimadzu, Japan). The MS acquisition was operated in the electrospray (ESI) positive mode. Chromatographic separation was performed on a Kinetex 2.6 μm C18 100 Å column, 50 mm × 3.00 mm (Phenomenex, Torrance, CA, USA) at r.t. using a mobile phase of 5 mmol/L NH₄OAc supplemented with 0.05% (v/v) formic acid (solvent A) and acetonitrile supplemented with 0.1% (v/v) formic acid (solvent B). The gradient was performed with a total flow at 0.7 mL/min as follow: 0–0.40 min 5% (B), 0.40–2.20 min 5%–95% (B), 2.20–2.30 min 95% (B), 2.30–2.31 min 95%–5% (B), 2.31–3.00 min 5% (B). Quantification was achieved by multiple reaction monitoring to identify the analytes (1H) and IS (terfenadine). The retention times of 1H and IS were 1.73 and 2.08 min, respectively. The declustering potential (DP) and collision energy (CE) were optimized as followed: DP: 61V CE: 29V for 1H, DP: 66V CE: 50V for terfenadine. The selected mass transitions were m/z 290.1 → 231.2 for 1H, m/z 472.4 → 436.4 for terfenadine, respectively. AB SCIEX Analyst® software (version 1.6.1) was used for data acquisition and analysis.

Zhang S., Zhao Y., Wang S., Li M., Xu Y., Ran J., Geng X., He J., Meng J., Shao G., Zhou H., Ge Z., Chen G., Li R, & Yang B. (2020). Discovery of novel diarylamides as orally active diuretics targeting urea transporters. Acta Pharmaceutica Sinica. B, 11(1), 181-202.

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LC-MS Analysis of Pharmacokinetic Compounds

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Atenolol, antipyrine, acyclovir, quinidine, and sulfanilic acid in the samples from transport studies with MucilAir were analyzed with a liquid chromatography and mass spectrometry (LC/MS) system (APL1100, Agilent Technology, Santa Clara, CA, USA) equipped with the reverse-phase column Luna C8 (5 μm, 250 × 4.6 mm i.d., Phenomenex Inc., Torrance, CA, USA) for sulfanilic acid and the Kinetex 2.6 μm C18 100 Å column (2.1 × 150 mm i.d., Phenomenex Inc.) for the other compounds. The mobile phases, flow rates, and injection volumes for the determination of the compounds were as follows:

Furubayashi T., Inoue D., Nishiyama N., Tanaka A., Yutani R., Kimura S., Katsumi H., Yamamoto A, & Sakane T. (2020). Comparison of Various Cell Lines and Three-Dimensional Mucociliary Tissue Model Systems to Estimate Drug Permeability Using an In Vitro Transport Study to Predict Nasal Drug Absorption in Rats. Pharmaceutics, 12(1), 79.

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Analytical Methods for Environmental Contaminants

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BAM and
metolachlor concentrations
were measured using a Prominence HPLC system (Schimadzu Corp., Japan)
with a 75 × 4.6 mm² Kinetex 2.6 μm C18 100 Å
column (Phenomenex Inc., Golden, CO). Benzene, toluene, and ethylbenzene
concentrations were measured on a Trace DSQ GC-MS system (Thermo Electron,
Germany) equipped with a Combi PAL autosampler (CTC Analytics, Switzerland)
with a DB-5 analytical column (30 m, 0.25 mm i.d., 0.5 μm film,
Agilent Technologies, Germany). Chloride (Cl^–) concentrations
in the diffusion-cell experiments were analyzed by ion chromatography
(Dionex 500, Dionex, Sunnyvale, CA). Concentrations of the conservative
tracer uranine in the tank experiment were measured on VICTOR Multilabel
Plate Reader (PerkinElmer, U.S.A.). A detailed description of the
methods is provided in the SI.

Sun F., Peters J., Thullner M., Cirpka O.A, & Elsner M. (2021). Magnitude of Diffusion- and Transverse Dispersion-Induced Isotope Fractionation of Organic Compounds in Aqueous Systems. Environmental Science & Technology, 55(8), 4772-4782.

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Enzymatic Peptide Degradation Analysis

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The enzymes (pepsin, Ph.Eur. grade, Carl Roth GmbH, and neutrophil elastase, 20–22 U/mg, Abcam, respectively) were diluted to 5.5 µg/mL in TFA 10 mM (pepsin) or Tris buffer 0.1 M + NaCl 0.5 M pH 7.8 (neutrophil elastase) and pre-incubated for 15 min at 37 °C. Peptides were added at 100 µM and incubated at 37 °C. A sample of 40 µL was taken after 60 min of incubation and the reaction was stopped by adding 5 µL sodium carbonate solution (1 M, pepsin) and 5 µL TFA (neutrophil elastase), respectively. After 10 min, 60 µL acetonitrile/water 50:50 containing 1% TFA were added, and the resulting solution was analyzed by LC-MS (conditions: Phenomenex Kinetex 2.6 μm C18 100 Å column, 50 × 2.1 mm, flow rate 0.55 mL/min, gradient of acetonitrile in H₂O (both containing 0.1% TFA, 20–60% over 20 min)).

Weißenborn L., Richel E., Hüseman H., Welzer J., Beck S., Schäfer S., Sticht H., Überla K, & Eichler J. (2022). Smaller, Stronger, More Stable: Peptide Variants of a SARS-CoV-2 Neutralizing Miniprotein. International Journal of Molecular Sciences, 23(11), 6309.

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HILIC and C18 Columns for Lipid Analysis

Cited 1 time

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For separation
and quantification
of the lysophospholipids, a Phenomenex Kinetex 2.6 μm HILIC
100 Å column of 30 × 2.1 mm size was used. The binary gradient
consisted of (A) ACN/water (95/5, v/v, pH = 8.0) containing 25 mM
AcNH₄ and (B) ACN/water (50/50, v/v, pH = 7.5) containing
25 mM AcNH₄. Gradient elution was carried out for 1.6 min
at a flow rate of 0.8 mL/min. Gradient conditions were as follows:
0% B for 0.8 min; 0–100% B for 0.4 min; 100% B for 0.3 min;
and 100% B for 0.1 min.^{10 (link)} For separation
and quantification of free FAs, a Phenomenex Kinetex 2.6 μm
C18 100 Å column of 30 × 2.1 mm size was used. A mobile
phase of ACN/water (80/20, v/v, pH = 8.9) containing 10 mM NH₄HCO₃ was used in an isocratic elution. A 10 μL
aliquot of each sample was injected into the column. The column temperature
was kept at 40 °C. All samples were maintained at 4 °C throughout
the analysis.

Mouchlis V.D., Armando A, & Dennis E.A. (2019). Substrate-Specific Inhibition Constants for Phospholipase A2 Acting on Unique Phospholipid Substrates in Mixed Micelles and Membranes Using Lipidomics. Journal of Medicinal Chemistry, 62(4), 1999-2007.

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