Jupiter c4 column

Manufactured by Phenomenex

Sourced in United States

The Jupiter C4 column is a reverse-phase liquid chromatography column designed for the separation and analysis of a wide range of analytes. It features a bonded C4 stationary phase that provides good retention and selectivity for a variety of sample types. The column is suitable for use in a range of analytical applications.

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Lab products found in correlation

1200 lc ms system, by Agilent Technologies (3 mentions) Ms chemstation software, by Agilent Technologies (3 mentions) 6130 quadrupole spectrometer, by Agilent Technologies (3 mentions) Prominence series uflc system, by Shimadzu (2 mentions) Avance 3 hd ascend 600 mhz spectrometer, by Bruker (2 mentions) Microplate reader, by Tecan (2 mentions) Infinite m200 microplate reader, by Tecan (2 mentions) Rabbit anti ubiquitin antibody, by Thermo Fisher Scientific (2 mentions) Rabbit anti his6 antibody, by Rockland Immunochemicals (2 mentions) Luna c18 2 column, by Phenomenex (2 mentions) Lc 20ad liquid chromatograph, by Shimadzu (1 mentions) Cbm 20a controller, by Shimadzu (1 mentions) 5977a msd, by Agilent Technologies (1 mentions) 7890b gc system, by Agilent Technologies (1 mentions) Tris glycine gel, by Thermo Fisher Scientific (1 mentions) Procise 494ht, by Thermo Fisher Scientific (1 mentions) Zorbax 300sb c18, by Agilent Technologies (1 mentions) Tskgel g3000swxl column, by Tosoh (1 mentions) Lc 30ad hplc system, by Shimadzu (1 mentions) Tripletof 6600, by AB Sciex (1 mentions)

Spelling variants of this product

Jupiter C4 (15 citations) C4 column (15 citations) Jupiter 5 u C4 300A column (2 citations)

32 protocols using jupiter c4 column

Gradient HPLC Analysis of Samples

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Gradient HPLC analysis was done by using Shimadzu Prominence series UFLC system with a CBM-20A controller bus module, a LC-20 AD liquid chromatograph, a CTO-20A column oven and a SPD-20A UV-visible detector. UV-visible absorption was measured at 295 nm. 20 μL of sample were loaded in the solvent injection ratio: 95% solvent A – 5% solvent B (A = Milli-Q water/TFA 99.9:0.1 v/v; B = CH₃CN/Milli Q water/TFA 90:9.9:0.1 v/v/v) onto a Jupiter C4 column (150 × 4.60 mm, 5 μm, 300 Å, Phenomenex) at a flow rate of 1 mL/min over 5 min. In a second step, samples were eluted by a gradient developed from 5 to 90% of solvent B in solvent A over 15 min. The concentration of solvent B was maintained over 5 min. Then, the concentration of solvent B was decreased to 5% over a period of 5 min to re-equilibrate the system, followed by additional 5 min at this final concentration. Before each sample measurement, a baseline was performed following the same conditions by loading Milli-Q water into the injection loop.

Le Duc G., Roux S., Paruta-Tuarez A., Dufort S., Brauer E., Marais A., Truillet C., Sancey L., Perriat P., Lux F, & Tillement O. (2014). Advantages of gadolinium based ultrasmall nanoparticles vs molecular gadolinium chelates for radiotherapy guided by MRI for glioma treatment. Cancer Nanotechnology, 5(1), 4.

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Analytical Methods for Protein Characterization

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General methods were as previously described.^{29 (link)} Growth media and conditions used for E. coli and Streptomyces strains and standard methods for handling strains were those described previously, unless otherwise noted.³⁰ All DNA manipulations performed following standard procedures.^30b DNA sequencing was carried out at the U. C. Davis Sequencing Facility, Davis, CA or by Genewiz. All proteins were handled at 4 °C, unless otherwise stated. Protein concentrations were determined according to the method of Bradford,^{31 (link)} using a Tecan Infinite M200 Microplate Reader with bovine serum albumin as the standard. Protein purity and size was estimated using both SDS-PAGE gel electrophoresis and an ATKA FPLC System. Accurate protein molecular weight was determined by ESI-MS on an Agilent 6530 Accurate-Mass Q-TOF LC/MS equipped with a Phenomenex Jupiter C4 column (50 mm × 2.00 mm, 5 μm). Substrate binding assays were carried out on the Tecan Microplate Reader. ¹H and ¹³C NMR spectra were obtained on a Bruker Avance III HD Ascend 600 MHz spectrometer. GC-MS analyses were carried out using an Agilent Technologies 5977A MSD with an Agilent Technologies 7890B GC system.

Duan L., Jogl G, & Cane D.E. (2016). The Cytochrome P450-Catalyzed Oxidative Rearrangement in the Final Step of Pentalenolactone Biosynthesis: Substrate Structure Determines Mechanism. Journal of the American Chemical Society, 138(38), 12678-12689.

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Comprehensive Characterization of Recombinant EPA Proteins

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The recombinant EPA proteins were fully characterized using similar techniques to those previously reported [13 (link),17 (link),22 (link)]. Protein separation by analytical size exclusion chromatography (SEC)-HPLC was performed on a TSKgel G3000SWxl column (Tosoh Biosciences) with in-line multi-angle light scattering (MALS) (Wyatt Technologies). Reversed-phase (RP)-HPLC analysis was performed on a Jupiter C4 column (Phenomenex) with TFA in water (0.1% w/v) for mobile phase A and TFA in acetonitrile (0.1% w/v) for mobile phase B. SDS-PAGE of the EPA protein was performed on a 4–20% Tris-glycine gel (Invitrogen) and stained with Coomassie blue as per the manufacturer’s instructions. Amino-terminal sequencing was performed by the Research Technology Branch, NIAID, NIH using a Sequenator model Procise 494 HT (Applied Biosystems) as previously described [22 (link),23 (link)]. Intact mass spectrometry was performed on an Agilent G6224A Accurate-Mass TOF with a dual ESI ion source and ion polarity in the positive mode. Protein was separated on a ZORBAX 300SB-C18 (Agilent) water + 0.05% TFA (solvent A) to acetonitrile + 0.05% TFA (solvent B) at a gradient of 0–70% B in 35 min. Acetic acid was added in a mixing tee placed before the electrospray inlet to the mass spectrometer at a ratio of 1:2 acetic acid to column eluent.

Burkhardt M., Reiter K., Nguyen V., Suzuki M., Herrera R., Duffy P.E., Shimp R J.r., MacDonald N.J., Olano L.R, & Narum D.L. (2018). Assessment of the impact of manufacturing changes on the physicochemical properties of the recombinant vaccine carrier ExoProtein A. Vaccine, 37(38), 5762-5769.

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Intact Mass Determination of Proteins

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Proteins were prepared in RutR storage buffer at concentrations of 1 μg/μL for intact mass determination. All samples were analyzed on a Triple TOF 6600 (Sciex) mass spectrometer equipped with a DuoSpray Ion Source that was coupled to a Shimadzu LC30AD HPLC System (Shimadzu). Approximately 100 ng of intact proteins (in 0.1% formic acid in water) were loaded onto a Jupiter C4 column (1 mm × 150 mm, 5 μm, 300 A, Phenomenex) and chromatographically separated at a constant flow rate of 100 μL/min using the following gradient: 20-60% solvent B (0.1% formic acid in acetonitrile) within 6 minutes followed by 85% solvent B for 1 minute and 20% B for 3 minutes. MS1 scans were acquired from 600-1600 m/z with 250 msec accumulation time. MS1 scans were summed across the chromatographic protein peak and the in summary spectra were exported in simple txt format for further analysis in the MagTran 1.02 deconvolution software^{138 (link)}.

Kremer M., Schulze S., Eisenbruch N., Nagel F., Vogt R., Berndt L., Dörre B., Palm G.J., Hoppen J., Girbardt B., Albrecht D., Sievers S., Delcea M., Baumann U., Schnetz K, & Lammers M. (2024). Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism. Nature Communications, 15, 1674.

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Synthesis of Bpy and Protein Analysis

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6,6′-Bis-bromomethyl-[3,3′]bipyridine (Bpy) was prepared using the procedure described previously (19 ). Rabbit anti-ubiquitin antibody was purchased from Thermo Scientific and rabbit anti-His₆ antibody was purchased from Rockland Immunochemicals. Mouse anti-CXCR4 antibody was purchased from R&D Systems. LC-MS was performed using a Finnigan LCQ Advantage IonTrap mass spectrometry coupled with a Surveyor HPLC system. Protein liquid chromatography was run on a Phenomenex Jupiter C4 column (5 μm, 300 Å, 2.00 × 50 mm) with a flow rate of 250 μL/min and a linear gradient of 5–95% acetonitrile/H₂O containing 0.1% formic acid over 30 min.

Muppidi A., Doi K., Edwardraja S., Pulavarti S.V., Szyperski T., Wang H.G, & Lin Q. (2014). Targeted Delivery of Ubiquitin-Conjugated BH3 Peptide-Based Mcl-1 Inhibitors into Cancer Cells. Bioconjugate Chemistry, 25(2), 424-432.

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Quantitative Mass Spectrometric Analysis of mAbs

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mAb samples were diluted to 1 mg/mL in 1X D-PBS or 10 mM histidine pH6.5 buffer before analysis. Mass of the entire mAb was determined as follows. Reversed-phase high performance liquid chromatography (RP-HPLC) was performed on a Waters Acquity UPLC system. The mobile phases consisted of water with 0.031% trifluoroacetic acid as solvent A and acetonitrile with 0.03% trifluoroacetic acid as solvent B. A Jupiter C4 column (2 x 150 mm, 5 μm particle size, 300 Å pore, Phenomenex), was used for the RP-HPLC time-of-flight (TOF) mass spectrometric (MS) analysis. The column eluent was directed in-line to a TOF mass spectrometer (Q-TOF Premier, Waters). The initial mobile phase was 20% solvent B, and then it was applied a gradient of 2.5% solvent B per min from 20–50% solvent B. The separation was performed at room temperature at a flow rate of 0.35 mL/min. The electrospray ionization mass spectra were analyzed using OpenLynx protein deconvolution software (Waters).

Cameron B., Dabdoubi T., Berthou-Soulié L., Gagnaire M., Arnould I., Severac A., Soubrier F., Morales J., Leighton P.A., Harriman W., Ching K., Abdiche Y., Radošević K, & Bouquin T. (2020). Complementary epitopes and favorable developability of monoclonal anti-LAMP1 antibodies generated using two transgenic animal platforms. PLoS ONE, 15(7), e0235815.

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Selective Lysozyme Extraction by BSA Concentration

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One-mL solutions containing a constant lysozyme concentration (5 μM) and variable BSA concentrations (5, 10, 20, 40 μM) were prepared in 100 mM MOPS buffered at pH 7.4, and extracted with the nanoassemblies as described in the general extraction procedure. Aliquots of each solution before and after depletion were analyzed by liquid chromatography (LC) on a reversed phase column (Phenomenex Jupiter® C4 column, 5μm, 300 Å, 150 mm × 1.00 mm) coupled to electrospray ionization mass spectrometry (ESI-MS) on a Bruker Esquire ion trap mass spectrometer to separate and measure the proteins in solution. Extraction selectivity and capacity were determined by comparing the LC-MS chromatogram for each protein before and after extraction. For determining the extraction capacity, a calibration curve for BSA was used to calculate the amount of BSA remaining in solution after extraction and consequently the amount of BSA extracted.

Serrano M.A., Gao J., Kelly K.A., Thayumanavan S, & Vachet R.W. (2018). Supramolecular Polymeric Assemblies for the Selective Depletion of Abundant Acidic Proteins in Serum. ACS applied materials & interfaces, 10(47), 40443-40451.

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Standardized Protein Characterization Methods

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General methods were as previously described.^{3 (link),29} Growth media and conditions used for E. coli strains and standard methods for strain manipulation were as described,²⁹ unless otherwise noted. All DNA manipulations performed following standard procedures.²⁹ DNA sequencing was carried out at the U. C. Davis Sequencing Facility, Davis, CA or by Genewiz. All proteins were handled at 4 °C unless otherwise stated. Protein concentrations were determined according to the method of Bradford,^{30 (link)} using a Tecan Infinite M200 Microplate Reader with bovine serum albumin as the standard. Protein purity and size was estimated using SDS-PAGE and visualized using Coomassie Blue stain and analyzed with a Bio-Rad ChemiDoc MP System. Accurate protein molecular weight was determined by ESI-MS on an Agilent 6530 Accurate-Mass Q-TOF LC/MS. Reductase activity assays were carried out on the Tecan Microplate Reader and kinetic assays of KR-catalyzed reductions were also performed by GC/MS. ¹H and ¹³C NMR spectra were obtained on a Bruker Avance III HD Ascend 600 MHz spectrometer. A Thermo LXQ equipped with Surveyor HPLC system and a Phenomenex Jupiter C4 column (150 mm×2 mm, 5.0 μm) was utilized for analysis of diketide-ACP compounds. LC-ESI-MS-MS analysis was carried out in positive ion mode for analysis of pantetheinate ejection fragments.

Xie X., Garg A., Keatinge-Clay A.T., Khosla C, & Cane D.E. (2016). The Epimerase and Reductase Activities of Polyketide Synthase Ketoreductase Domains Utilize the Same Conserved Tyrosine and Serine Residues. Biochemistry, 55(8), 1179-1186.

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LC-MS Analysis of Protein Complexes

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Liquid chromatography-mass spectrometry (LC-MS) was performed on a Micromass LCT (ESI-TOF-MS) coupled to a Waters Alliance 2790 HPLC using a Phenomenex Jupiter C4 column (250 x 4.6 mm x 5μm). Water:acetonitrile, 95:5 (solvent A) and acetonitrile (solvent B), each containing 0.1% formic acid, were used as the mobile phase at a flow rate of 1.0 mL min^-1. The gradient was programmed as follows: 95% A (5 min isocratic) to 100% B after 15 min then isocratic for 5 min. The electrospray source of LCT was operated with a capillary voltage of 3.2 kV and a cone voltage of 25 V. Nitrogen was used as the nebulizer and desolvation gas at a total flow of 600 L hr^-1. Spectra were calibrated using a calibration curve constructed from a minimum of 17 matched peaks from the multiply charged ion series of equine myoglobin, which was also obtained at a cone voltage of 25V. Total mass spectra were reconstructed from the ion series using the MaxEnt algorithm preinstalled on MassLynx software (v. 4.0 from Waters) according to manufacturerʼs instructions.

Lai H.M., Liu A.K., Ng W.L., DeFelice J., Lee W.S., Li H., Li W., Ng H.M., Chang R.C., Lin B., Wu W, & Gentleman S.M. (2016). Rationalisation and Validation of an Acrylamide-Free Procedure in Three-Dimensional Histological Imaging. PLoS ONE, 11(6), e0158628.

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Preparative and Analytical HPLC Purification of Peptides and Bioconjugates

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The crude peptides and the bioconjugates were purified on a Knauer 2501 HPLC system (H. Knauer, Bad Homburg, Germany). A preparative Phenomenex Luna C18 column (250 × 21.2 mm) with 10 µm silica (100 Å pore size) was used for the crude peptides, while a Phenomenex Jupiter C4 column (250 × 10 mm) with 10 µm silica (300 Å pore size) was used for the bioconjugates (Torrance, CA, USA). Linear gradient elution (0 min 5% B; 5 min 5% B; 50 min 80% B) with eluent A (0.1% TFA in water) and eluent B (0.1% TFA in acetonitrile-water 80:20, v/v) was used at a flow rate of 16 mL/min for the peptides and linear gradient elution (0 min 15% B; 5 min 15% B; 50 min 60% B) with eluent A (0.1% TFA in water) and eluent B (0.1% TFA in acetonitrile) was used at a flow rate of 4 mL/min for the bioconjugates. Peaks were detected at 220 nm.
Analytical RP-HPLC runs were performed on a Knauer 2501 HPLC system using a Macherey–Nagel Nucleosil C18 column (250 × 4.6 mm) with 5 µm silica (100 Å pore size). Linear gradient elution (0 min 2% B; 5 min 2% B; 30 min 90% B) with eluent A (0.1% TFA in water) and eluent B (0.1% TFA in acetonitrile) was used at a flow rate of 1 mL/min. Peaks were detected at 220 nm.

Pethő L., Murányi J., Pénzes K., Gurbi B., Brauswetter D., Halmos G., Csík G, & Mező G. (2019). Suitability of GnRH Receptors for Targeted Photodynamic Therapy in Head and Neck Cancers. International Journal of Molecular Sciences, 20(20), 5027.

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