Xbridge beh130 prep c18

Manufactured by Waters Corporation

Sourced in United States

The XBridge BEH130 Prep C18 is a reversed-phase high-performance liquid chromatography (HPLC) column designed for preparative-scale separations. It features a 130 Angstrom pore size and a 5 micron particle size. This column is intended for use in the purification of chemical compounds and other preparative applications.

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Lab products found in correlation

Rp hplc, by Waters Corporation (1 mentions) 4800 maldi tof tof analyzer, by Thermo Fisher Scientific (1 mentions) Reversed phase high performance liquid chromatography rp hplc, by Shimadzu (1 mentions) Doxorubicin dox, by LC Laboratories (1 mentions) Xbridge beh c18 column, by Waters Corporation (1 mentions) Ltq orbitrap, by Thermo Fisher Scientific (1 mentions) Fluoview fv10i confocal laser scanning microscope, by Olympus (1 mentions) Axio imager m1 microscope, by Zeiss (1 mentions) Spectramax m5, by Molecular Devices (1 mentions) F 7000, by Hitachi (1 mentions) Lc 20ap, by Shimadzu (1 mentions)

4 protocols using xbridge beh130 prep c18

Antioxidant Peptide Purification by RP-HPLC

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Fractions from gel-filtration chromatography with the highest antioxidant
activity were further separated using RP-HPLC (Waters, Milford, MA, USA). 5
mg of the peptide fractions were dissolved in 2 mL of sodium phosphate
buffer (10 mM, pH 7.2) before being filtered with a 0.22 μm filter.
200 μL of the sample was then loaded onto XBridge BEH130 Prep C18
(10×250 mm, 5 μm) (Waters, Milford, MA, USA). The solvents
involved are; solvent A, 0.1% (v/v) trifluoroacetic acid (TFA) in deionized
water; solvent B, 0.1% (v/v) TFA in 100% (v/v) acetonitrile solution. The
flow rate was 4.73 mg/min and the UV absorbance of the eluents was measured
at 214 nm. The samples are then put into a centrifugal concentrator at
380×g for 3 h, which are then used for ABTS radical scavenging
activity.

Nadalian M., Kamaruzaman N., Yusop M.S., Babji A.S, & Yusop S.M. (2019). Isolation, Purification and Characterization of Antioxidative Bioactive Elastin Peptides from Poultry Skin. Food Science of Animal Resources, 39(6), 966-979.

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Synthesis and Purification of Fluorescent Peptide Conjugates

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All amino acids and resins were purchased from AAPPTec LLC (Louisville, KY, USA), Chem-Impex International Inc. (Wood Dale, IL, USA), and CEM Corporation (Matthews, NC, USA). All organic solvents were purchased from Millipore Sigma Corporation (St. Louis, MO, USA), Fischer Scientific (Pittsburgh, PA, USA), and Gyros Protein Technologies, Inc (Tucson, AZ, USA). Anticancer agents Doxorubicin (Dox) and Docetaxel (Doce) were purchased from LC laboratories (Woburn, MA, USA). Masses of intermediate and final products were confirmed by high-resolution matrix-assisted laser desorption/ ionization time-of-flight (MALDI-TOF) mass spectrometer from Bruker Inc. (GT 0264, Billerica, MA, USA) or Applied Biosystems (4800 MALDI TOF/TOF Analyzer, Foster City, CA, USA). Intermediate and final compounds were purified by reversed-phase high-performance liquid chromatography (RP-HPLC) from Shimadzu (Prominence, Columbia, MD, USA) using a gradient system of acetonitrile and water with 0.1% trifluoroacetic acid using reverse phase C18 column (XBridge BEH130 Prep C18), from Waters Corporation (Milford, MA, USA). 5(6)-Carboxyfluorescein diisobutyrate (CFDI) was used to synthesize fluorescently-label peptide (USBiological Life Science, Swampscott, MA, USA).

Park S.E., Shamloo K., Kristedja T.A., Darwish S., Bisoffi M., Parang K, & Tiwari R.K. (2019). EDB-FN Targeted Peptide–Drug Conjugates for Use against Prostate Cancer. International Journal of Molecular Sciences, 20(13), 3291.

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Comprehensive Biophysical Characterization Methods

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Unless otherwise noted, all solvents and reagents were obtained from commercial suppliers and used without further purification. The peptide fragments analysis and purification were carried out on an Agilent Technologies 1200 HPLC system (Agilent, USA) equipped with UV-VIS and fluorescence detector using XBridge BEH C18 Column (10 μm, 150 mm × 4.6 mm, Waters Corp., USA) and XBridge BEH130 Prep C18 (10 μm, 250 mm × 10 mm, Waters Corp., USA). Mass spectra were acquired on a MALDI-TOF, Voyager-DETM STR Biospectrometry Workstation (Applied Biosystems Inc., USA) and a high-resolution electrospray ionization mass spectrometry (HR-ESI-MS, Thermo Finnigan, LTQ-Orbitrap). Fluroescence spectra were acquired by a fluorescence spectrophotometer (Hitachi F-7000, Japan). Cell images were collected using an Axioimager M1 microscope (Zeiss, Germany) and tumor spheroids were observed with FluoView FV10i confocal laser scanning microscope (Olympus, Japan). UV absorption for WST-1 assay was measured by SpectraMax M5 (Molecular Devices, USA). All in vivo data and images were taken on an IVIS Spectrum imaging system (Caliper, USA). The histological images were obtained from optical microscope (BX 51, Olympus, Japan).

Cho H.J., Lee S.J., Park S.J., Paik C.H., Lee S.M., Kim S, & Lee Y.S. (2016). Activatable iRGD-based peptide monolith: targeting, internalization, and fluorescence activation for precise tumor imaging. Journal of controlled release : official journal of the Controlled Release Society, 237, 177-184.

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Peptide Synthesis and Purification

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All Fmoc-protected amino acids and resins were purchased from AAPPTEC (Louisville, KY, USA). All the other chemicals and reagents were purchased from MilliporeSigma (Milwaukee, WI, USA). The chemical structures of the final purified peptides were confirmed by high-resolution MALDI-TOF (GT 0264) from Bruker Inc (Fremont, CA, USA). Final peptides were purified by a reversed-phase HPLC (LC-20AP) from Shimadzu (Canby, OR, USA) using a gradient system of water and acetonitrile and a reversed-phase preparative column (Waters, XBridge BEH130 Prep C18).

Sanner M.F., Zoghebi K., Hanna S., Mozaffari S., Rahighi S., Tiwari R.K, & Parang K. (2021). Cyclic Peptides as Protein Kinase Inhibitors: Structure-Activity Relationship and Molecular Modeling. Journal of chemical information and modeling, 61(6), 3015-3026.

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