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300sb c8 column

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The 300SB-C8 column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of a wide range of compounds. The column features a silica-based stationary phase with C8 alkyl ligands, providing a balanced selectivity for both polar and non-polar analytes. The column dimensions are 4.6 mm internal diameter and 150 mm length, with a particle size of 5 micrometers. This column is suitable for a variety of HPLC applications, including pharmaceutical, environmental, and industrial analyses.

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Lab products found in correlation

Acquity uplc system, by Waters Corporation (4 mentions) Hplc system, by Agilent Technologies (1 mentions) Agilent 6210 time of flight mass spectrometer, by Agilent Technologies (1 mentions) Masshunter qualitative analysis program, by Agilent Technologies (1 mentions) Pngase f, by New England Biolabs (1 mentions) 1290 infinity 2 lc, by Agilent Technologies (1 mentions) Jetstream source, by Agilent Technologies (1 mentions) 6230 lc tof system, by Agilent Technologies (1 mentions) 6530 lc q tof system, by Agilent Technologies (1 mentions) Lc 6a, by Shimadzu (1 mentions)

Close spelling variants of this product

300SB-C8 reverse phase analytical column Poroshell 300SB-C8 column Zorbax 300SB-C8 column 300SB-C8 C8 column

10 protocols using 300sb c8 column

1

Dde-Lys(Fmoc) and AcVitE Synthesis

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Example 10

The title compound was prepared according to the procedure as described in Example 4 substituting Dde-Lys(Fmoc)-OH in place of Fmoc-Leu-OH at position 30 and α-Tocopheryloxyacetic Acid (AcVitE) (8) in place of palmitic acid in step 3. Product purification was performed using an Agilent 300SB C8 column (21×250 mm, 100 Å, 5 μm) at rt. The mobile phase consisted of a gradient elution of Buffer A (0.1% TFA in water) and Buffer B (0.1% TFA in MeCN) ranging from an initial concentration of 30% B to an intermediate concentration of 40% B (21 mpm) over 10 min, and then to a final concentration of 55% B (21 mpm) over 35 min. Impure product-containing fractions were re-purified using a modified gradient from an initial concentration of 35% B to an intermediate concentration of 43% B (21 mpm) over 5 min, and then to a final concentration of 58% B (10.5 mpm) over 40 min.

US10961293B2. Cyclic peptide tyrosine tyrosine compounds as modulators of neuropeptide Y receptors (2021-03-30). Janssen Pharmaceutica NV [BE]. Inventors: Mark Macielag [US], Raymond J. Patch [US], Rui Zhang [US], Martin A. Case [US], Mark J. Wall [US], Yue-Mei Zhang [US].
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2

Characterization of mAb Sequence and Structure

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The sequences of the purified mAbs and respective F(ab’)2 and Fc fragments were evaluated by LC-MS using a PoroShell 300SB-C8 column (5 µm, 75 × 1.0 mm) on the Agilent HPLC system followed by analysis in the Agilent 6210 time-of-flight mass spectrometer (Agilent Technologies). The composition of the mobile phase A was 99% water, 1% acetonitrile, and 0.1% formic acid, and that of mobile phase B was 95% acetonitrile, 5% water, and 0.1% formic acid. The gradient started with 20% B at 0 min and increased to 85% B at 10 min with the constant flow rate of 50 µL/min. Each sample was subjected to a native run, a reduced run after incubation with TCEP (Sigma), and a deglycosylated run after incubation with TCEP and PNGase F (New England Biolabs). The MassHunter Qualitative Analysis program (version B.06.00, Agilent, Santa Clara, CA, USA) was used to deconvolute the raw data.
Yang D., Kroe-Barrett R., Singh S, & Laue T. (2019). IgG Charge: Practical and Biological Implications. Antibodies, 8(1), 24.
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3

Lipopeptide Synthesis using Fmoc and AcVitE

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Example 10

The title compound was prepared according to the procedure as described in Example 4 substituting Dde-Lys(Fmoc)-OH in place of Fmoc-Leu-OH at position 30 and α-Tocopheryloxyacetic Acid (AcVitE) (8) in place of palmitic acid in step 3. Product purification was performed using an Agilent 300SB C8 column (21×250 mm, 100 Å, 5 μm) at rt. The mobile phase consisted of a gradient elution of Buffer A (0.1% TFA in water) and Buffer B (0.1% TFA in MeCN) ranging from an initial concentration of 30% B to an intermediate concentration of 40% B (21 mpm) over 10 min, and then to a final concentration of 55% B (21 mpm) over 35 min. Impure product-containing fractions were re-purified using a modified gradient from an initial concentration of 35% B to an intermediate concentration of 43% B (21 mpm) over 5 min, and then to a final concentration of 58% B (10.5 mpm) over 40 min.

US11732019B2. Cyclic peptide tyrosine tyrosine compounds as modulators of neuropeptide Y receptors (2023-08-22). Janssen Pharmaceutica NV [BE]. Inventors: Mark Macielag [US], Raymond J. Patch [US], Rui Zhang [US], Martin A. Case [US], Mark J. Wall [US], Yue-Mei Zhang [US].
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4

Analyzing V272M DBD-PAT Interaction by MS

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Protein buffer of V272M DBD was replaced by 200 mM ammonium acetate buffer (pH 7.0) using dialysis device. V272M DBD was mixed with PAT at a molar ratio of 1 : 1 and the mixture was divided into two same samples. The mass of the two samples were immediately determined, without an incubation step, by native MS and denatured MS, respectively. The mass of V272M DBD without PAT treatment was also determined in the same way. Native MS was carried out on a 1290 Infinity II LC coupled with a 6230 LC/TOF system equipped with an Agilent Jet Stream source. LC separation was obtained with PolyHYDROXYETHYL ATM column (200 3 2.1 mm, 5 mm, 200 A ˚). In denatured MS, a 1290 Infinity II LC coupled with a 6530 LC/QTOF system and an Agilent 300SB-C8 column (50 3 2.1 mm, 3.5 mm) were used for denatured protein determination. All experimental MS data of the samples were processed using Agilent MassHunter Qualitative Analysis 7.0 software. Experimental molecular weights (MW) were determined from MS peak maxima with average MW and standard deviations calculated from identified charge states.
Tang Y., Song H., Wang Z., Xiao S., Xiang X., Zhan H., Wu L., Wu J., Xing Y., Tan Y., Liang Y., Yan N., Li Y., Li J., Wu J., Zheng D., Jia Y., Chen Z., Li Y., Zhang Q., Zhang J., Zeng H., Tao W., Liu F., Wu Y, & Lu M. (2022). Repurposing antiparasitic antimonials to noncovalently rescue temperature-sensitive p53 mutations. Cell reports, 39(2).
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5

RP-UPLC Separation of Anti-Ebola mAbs

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Example 7

RP-UPLC of the co-formulation comprising the three anti-Ebola mAbs of similar molecular weights, protein structures, and charge properties is evaluated. RP-UPLC separates mAbs by hydrophobicity. A Waters Acquity UPLC system is used. A ZORBAX 300SB-C8 column is used, and the column is run at 80° C. The mobile phase includes 60-90% acetonitrile in 0.1% TFA. FIG. 19 depicts a chromatogram of the RP-UPLC. As shown, there is significant overlap between elution times of mAb A and mAb B. Thus, RP-UPLC is a sub-optimal method for separating the three anti-MERS mAbs of similar molecular weight.

US11020686B2. Methods for quantitating individual antibodies from a mixture (2021-06-01). Regeneron Pharmaceuticals, Inc. [US]. Inventors: Dingjiang Liu [US], Lin Luo [US], Long Xu [CN].
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6

Characterization of Cyclosporine A Formulations

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In order to investigate the characteristics of the CsA in the formulations, Fourier transform infrared spectroscopy (FTIR) was applied by the KBr pellet method using a Nicolet IS 10 apparatus (Madison, WI, USA). The samples were scanned at a resolution of 0.4 cm−1 in the wavenumber region of 4000–400 cm−1.
The content (%) of CsA was measured by dissolving ~25 mg formulation in 25 mL of ethanol and water with a volume ratio of 50:50, and CsA content was quantified by the HPLC method with slight modifications, according to the literature (Jiang et al., 2022). Briefly, the Agilent 1260 Infinity Ⅱ HPLC system (Palo Alto, CA, USA) was used, and the ZORBAX 300 SB C8 column (250 mm × 4.6 mm, 5.0 μm) was selected for separation of CsA at 60 °C. The mobile phases were acetonitrile/water (60:40, v/v), and the flow rate was 1.0 mL/min. The injection volume was 10 μL, and the detection wavelengths were 205 nm.
Huang Y., Tang H., Meng X., Zhao Z., Liu Y., Liu D., Chen B, & Zou Z. (2023). Development of Large Hollow Particles for Pulmonary Delivery of Cyclosporine A. Pharmaceutics, 15(9), 2204.
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7

Fmoc-based Synthesis of Antimicrobial Peptides

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Basing on 9-fluorenylmethoxycarbonyl (Fmoc) chemistry.24 (link) AMPs were synthesized by Fmoc Solid Phase Peptide Synthesis (SPPS) on an 4-methyl-benzhydrylamine (MBHA) resin, then purified by preparative Shimadzu LC-6A reverse-phase high-performance liquid chromatography (RP-HPLC) using a Zorbax 300 SB-C8 column (250-mm×9.6-mm inner diameter, 6.5-μm particle size, 300-Å pore size). Eluent A was 0.1% aqueous solution of trifluoroacetic acid (TFA), and eluent B was 0.1% TFA in acetonitrile solution. Peptides were characterized by mass spectrometry and amino acid analysis.
Zhu J., Huang Y., Chen M., Hu C, & Chen Y. (2019). Functional Synergy Of Antimicrobial Peptides And Chlorhexidine Acetate Against Gram-Negative/Gram-Positive Bacteria And A Fungus In Vitro And In Vivo. Infection and Drug Resistance, 12, 3227-3239.
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8

RP-UPLC Separation of Anti-Ebola mAbs

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Example 7

RP-UPLC of the co-formulation comprising the three anti-Ebola mAbs of similar molecular weights, protein structures, and charge properties is evaluated. RP-UPLC separates mAbs by hydrophobicity. A Waters Acquity UPLC system is used. A ZORBAX 300SB-C8 column is used, and the column is run at 80° C. The mobile phase includes 60-90% acetonitrile in 0.1% TFA. FIG. 19 depicts a chromatogram of the RP-UPLC. As shown, there is significant overlap between elution times of mAb A and mAb B. Thus, RP-UPLC is a sub-optimal method for separating the three anti-MERS mAbs of similar molecular weight.

US11850535B2. Methods for quantitating individual antibodies from a mixture (2023-12-26). Regeneron Pharmaceuticals, Inc. [US]. Inventors: Dingjiang Liu [US], Lin Luo [US], Long Xu [CN].
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9

RP-UPLC Separation of Anti-Ebola mAbs

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Example 7

RP-UPLC of the co-formulation comprising the three anti-Ebola mAbs of similar molecular weights, protein structures, and charge properties is evaluated. RP-UPLC separates mAbs by hydrophobicity. A Waters Acquity UPLC system is used. A ZORBAX 300SB-C8 column is used, and the column is run at 80° C. The mobile phase includes 60-90% acetonitrile in 0.1% TFA. FIG. 19 depicts a chromatogram of the RP-UPLC. As shown, there is significant overlap between elution times of mAb A and mAb B. Thus, RP-UPLC is a sub-optimal method for separating the three anti-MERS mAbs of similar molecular weight.

US11571636B2. Methods for quantitating individual antibodies from a mixture (2023-02-07). Regeneron Pharmaceuticals, Inc. [US]. Inventors: Dingjiang Liu [US], Lin Luo [US], Long Xu [CN].
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10

RP-UPLC Separation of Anti-Ebola mAbs

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Example 7

RP-UPLC of the co-formulation comprising the three anti-Ebola mAbs of similar molecular weights, protein structures, and charge properties is evaluated. RP-UPLC separates mAbs by hydrophobicity. A Waters Acquity UPLC system is used. A ZORBAX 300SB-C8 column is used, and the column is run at 80° C. The mobile phase includes 60-90% acetonitrile in 0.1% TFA. FIG. 19 depicts a chromatogram of the RP-UPLC. As shown, there is significant overlap between elution times of mAb A and mAb B. Thus, RP-UPLC is a sub-optimal method for separating the three anti-MERS mAbs of similar molecular weight.

US11369896B2. Methods for quantitating individual antibodies from a mixture (2022-06-28). Regeneron Pharmaceuticals, Inc. [US]. Inventors: Dingjiang Liu [US], Lin Luo [US], Long Xu [CN].
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