Beh130

Manufactured by Waters Corporation

Sourced in United States

The BEH130 is a high-performance liquid chromatography (HPLC) column offered by Waters Corporation. It is designed for analytical and preparative separation of a wide range of compounds. The column utilizes BEH (Ethylene Bridged Hybrid) particle technology, providing high efficiency and durability.

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Lab products found in correlation

Prep c18 5 μm, by Waters Corporation (2 mentions) Nanoacquity uplc system, by Waters Corporation (2 mentions) Xevo g2 qtof, by Waters Corporation (1 mentions) Acquity uplc, by Waters Corporation (1 mentions) Ltq orbitrap elite mass spectrometer, by Thermo Fisher Scientific (1 mentions) Symmetry c18 column, by Waters Corporation (1 mentions)

Close spelling variants of this product

BEH130 Prep C18 10-μm column BEH130 C18 column XBridge BEH130 C18 column NanoAquity BEH130 C18 1.7 μm UPLC column Acquity UPLC BEH130 C18 column BEH130 C18 XBridge BEH130 column Acquity M-Class BEH130 C18 XBridge BEH130 Acquity M-Class BEH130 C18 analytical column

8 protocols using beh130

SARS-CoV-2 Spike Protein Peptide Synthesis

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In addition to the longer RBD fragments, JS7 and JS10 (residues 443–505 and 417–505, respectively, of SARS-CoV-2 S protein), for competitive ELISAs, 3 peptides from the JS7 sequence that are most in contact with the ACE2 receptor were synthesized:
SKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGY
Peptide 1: SKVGGNYNYLYRLF (443–457)
Peptide 2: FERDISTEIYQAGST
Peptide 3: EGFNCYFPLQSYGFQPTNGVGY
Purifications (to > 98 % +) were performed on a Waters HPLC preparative workstation with 2545 pump (at 20 mL/min) and using a C18 reverse phase column (Waters BEH 130, 5 μm, 19 × 150) and a gradient from 98 % to 50 % water-acetonitrile with 0.1 % TFA. Peaks were collected based on monitoring at 215 nm using a PDA 2998 detector. Combined product fractions were lyophilized, yielding a white fluffy solid. Peptides were then analyzed for purity by analytical HPLC on a C18 reverse phase column (Waters BEH 130, 5 μm, 4.6 × 150) with a gradient from 98 % to 20 % water-acetonitrile with 0.1 % TFA and by mass spectrometry on Thermo LTQ, Thermo Exactive and ABI 4800 MALDI TOF/TOF mass spectrometers, respectively, in ESI + mode. Additional data on the HPLC conditions and mass spectrometry identification are provided in the supplement.

Schein C.H., Levine C.B., McLellan S.L., Negi S.S., Braun W., Dreskin S.C., Anaya E.S, & Schmidt J. (2021). Synthetic proteins for COVID-19 diagnostics. Peptides, 143, 170583.

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Synthesis of Peptide SEQ ID NO: 6

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Example 1

Synthesis of SEQ ID NO: 6

The solid phase synthesis as described in Methods was carried out on Novabiochem Rink-Amide resin (4-(2′,4′-Dimethoxyphenyl-Fmoc-aminomethyl)-phenoxyacetamido-norleucylaminomethyl resin), 100-200 mesh, loading of 0.23 mmol/g. The Fmoc-synthesis strategy was applied with HBTU/DIPEA-activation. In position 14 Fmoc-Lys(ivDde)-OH and in position 1 BOC-His(Trt)-OH were used in the solid phase synthesis protocol. The ivDde-group was cleaved from the peptide on resin according to literature (S. R. Chhabra et al., Tetrahedron Lett. 1998, 39, 1603-1606). Hereafter Palm-gGlu-gGlu-OSu was coupled to the liberated amino-group employing DIPEA as base. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 1990, 36, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5 μM) using an acetonitrile/water gradient (both buffers with 0.1% TFA). The purified peptide was analysed by LCMS (Method A).

Deconvolution of the mass signals found under the peak with retention time 11.30 min revealed the peptide mass 4782.6 which is in line with the expected value of 4782.6.

US09982029B2. Exendin-4 derivatives as selective peptidic dual GLP-1/glucagon receptor agonists (2018-05-29). Sanofi [FR]. Inventors: Martin Bossart [DE], Andreas Evers [DE], Torsten Haack [DE], Katrin Lorenz [DE], Dieter Kadereit [DE], Michael Wagner [DE], Bernd Henkel [DE].

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HPLC-QTOF Analysis of Amino Acids

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For AA analysis, 10 μL of the prepared AA sample was injected onto an HPLC column (1.0 mm i.d. × 10 cm, 1.7 μm C18, BEH130, Waters Corporation, Milford, MA, USA) coupled online to a Q-TOF instrument (ACQUITY UPLC and Xevo G2 QTof, Waters Corporation, Milford, MA, USA), and eluted over 40 min using the following gradient: 0.1% FA/acetonitrile in 0.1% FA gradient at a flow rate of 70 μL/min: 0–5 min, 5% acetonitrile in 0.1% FA; 5–10 min, 5 to 30% acetonitrile in 0.1% FA; 10–25 min, 30 to 40% acetonitrile in 0.1% FA; 25–27 min, 40 to 90% acetonitrile in 0.1% FA; 27–30 min, 90% acetonitrile in 0.1% FA; 30–32 min, 90 to 5% acetonitrile in 0.1% FA; and 32–40 min, 5% acetonitrile in 0.1% FA.

Ku M.C., Fang C.M., Cheng J.T., Liang H.C., Wang T.F., Wu C.H., Chen C.C., Tai J.H, & Chen S.H. (2016). Site-specific covalent modifications of human insulin by catechol estrogens: Reactivity and induced structural and functional changes. Scientific Reports, 6, 28804.

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Denaturing LC/MS Protein Analysis

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Denaturing LC/MS analysis was performed on a Waters Acquity UPLC with TUV detector (at 280 nm) and G2-S Q-ToF mass spectrometer (scan m/z range of 1000–4000). The column used was a 2.1 × 100 mm BEH 130 (Waters, C18, 1.7 μM pore size) with a mobile phase gradient of water/acetonitrile + 0.5% formic acid.

Behrens C.R., Ha E.H., Chinn L.L., Bowers S., Probst G., Fitch-Bruhns M., Monteon J., Valdiosera A., Bermudez A., Liao-Chan S., Wong T., Melnick J., Theunissen J.W., Flory M.R., Houser D., Venstrom K., Levashova Z., Sauer P., Migone T.S., van der Horst E.H., Halcomb R.L, & Jackson D.Y. (2015). Antibody–Drug Conjugates (ADCs) Derived from Interchain Cysteine Cross-Linking Demonstrate Improved Homogeneity and Other Pharmacological Properties over Conventional Heterogeneous ADCs. Molecular pharmaceutics, 12(11), 3986-3998.

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UPLC-SRM Analysis of Prepared Solution

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The prepared solution was analyzed with a nanoAcquity UPLC system (Waters Corporation, Milford, MA) equipped with one analytical capillary column, 100 μm i.d. × 100 mm with a 1.7 μm C18 (stationary phase, BEH130, Waters Corporation, Milford, MA), and an autosampler. Solvents used in the UPLC system consisted of 0.1% formic acid in water (mobile phase A) and 0.1% formic acid in 90% acetonitrile (mobile phase B). Two microliters (2 μL) of the solution for each concentration were loaded into the analytical column, at a flow rate of 300 nL/min. The LC-SRM separation used a binary gradient of 10–15% B in 4.5 min, 15–25% B in 17 min, 25–38.5% B in 11 min, 38.5–95% B in 1 min, and 95% B for 4 min.

Chen T.C., Fillmore T.L., Prost S.A., Moore R.J., Ibrahim Y.M, & Smith R.D. (2015). Orthogonal Injection Ion Funnel Interface Providing Enhanced Performance for Selected Reaction Monitoring-Triple Quadrupole Mass Spectrometry. Analytical chemistry, 87(14), 7326-7331.

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Peptide Separation and Analysis Protocol

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Samples were reconstituted in solvent A (2% ACN/0.1% FA/water) and injected via an auto-sampler for separation by reverse phase chromatography on a NanoAcquity UPLC system (Waters). Peptides were loaded onto the Symmetry C₁₈ column (1.7 mm BEH-130, 0.1 × 100 mm, Waters) with a flow rate of 1 μl/min. A gradient of 2% solvent B to 25% solvent B (solvent A is 0.1% FA/2% ACN/water and solvent B is 0.1% FA/2% water/ACN) was applied over 35 min with a total analysis time of 60 min. Peptides were eluted directly into an Advance CaptiveSpray ionization source (Michrom BioResources/Bruker) with a spray voltage of 1.3 kV and were analyzed using an LTQ Orbitrap Elite mass spectrometer (Thermo Fisher Scientific). Precursor ions were acquired in the FTMS at 60,000 resolution; MS/MS was performed in the LTQ using resonance excitation, with the instrument operated in data-dependent mode, whereby the 15 most abundant ions were selected for fragmentation in each duty cycle.

Calses P.C., Pham V.C., Guarnaccia A.D., Choi M., Verschueren E., Bakker S.T., Pham T.H., Hinkle T., Liu C., Chang M.T., Kljavin N., Bakalarski C., Haley B., Zou J., Yan C., Song X., Lin X., Rowntree R., Ashworth A., Dey A, & Lill J.R. (2023). TEAD Proteins Associate With DNA Repair Proteins to Facilitate Cellular Recovery From DNA Damage. Molecular & Cellular Proteomics : MCP, 22(2), 100496.

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Synthesis of Bioactive Peptide SEQ ID NO: 17

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Example 3

Synthesis of SEQ ID NO: 17

The solid phase synthesis was carried out on Rink-resin with a loading of 0.38 mmol/g, 75-150 μm from the company Agilent Technologies. The Fmoc-synthesis strategy was applied with HBTU/DIPEA-activation. In position 1 Boc-Tyr(tBu)-OH and in position 14 Fmoc-Lys(ivDde)-OH was used in the solid phase synthesis protocol. The ivDde-group was cleaved from the peptide on resin according to literature (S. R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603). Hereafter Fmoc-γ-amino butyric acid was coupled to the liberated amino-group employing the coupling reagents HBTU/DIPEA followed by Fmoc-deprotection with 20% piperidine in DMF. Finally stearic acid was coupled using HBTU/DIPEA. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 36, 1990, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5 μM) using an acetonitrile/water gradient (both buffers with 0.05% TFA). The purified peptide was analysed by LCMS (Method C). Deconvolution of the mass signals found under the peak with retention time 29.59 min revealed the peptide mass 4561.4 which is in line with the expected value of 4561.26.

US10253079B2. Functionalized Exendin-4 derivatives (2019-04-09). SANOFI [FR]. Inventors: Torsten Haack [DE], Michael Wagner [DE], Bernd Henkel [DE], Siegfried Stengelin [DE], Andreas Evers [DE], Martin Lorenz [DE], Katrin Lorenz [DE].

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Synthesis of Peptide SEQ ID NO: 18

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Example 4

Synthesis of SEQ ID NO: 18

The solid phase synthesis was carried out on Rink-resin with a loading of 0.38 mmol/g, 75-150 μm from the company Agilent Technologies. The Fmoc-synthesis strategy was applied with HBTU/DIPEA-activation. In position 1 Boc-Tyr(tBu)-OH and in position 14 Fmoc-Lys(ivDde)-OH was used in the solid phase synthesis protocol. The ivDde-group was cleaved from the peptide on resin according to literature (S. R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603). Hereafter Fmoc-β-Ala-OH was coupled to the liberated amino-group employing the coupling reagents HBTU/DIPEA followed by Fmoc-deprotection with 20% piperidine in DMF. Again Fmoc-β-Ala-OH was coupled followed by Fmoc-deprotection and the final coupling of stearic acid using HBTU/DIPEA. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 36, 1990, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5 μM) using an acetonitrile/water gradient (both buffers with 0.05% TFA). The purified peptide was analysed by LCMS (Method C). Deconvolution of the mass signals found under the peak with retention time 28.97 min revealed the peptide mass 4618.6 which is in line with the expected value of 4618.32.

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