6520 q tof lc ms

Manufactured by Agilent Technologies

Sourced in United States

The 6520 Q-TOF LC/MS is a high-resolution mass spectrometry system designed for accurate mass measurements. It combines a quadrupole and a time-of-flight mass analyzer to provide high-quality data for diverse applications.

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Lab products found in correlation

Jsm 7500f scanning electron microscope, by JEOL (1 mentions) Smartlab diffractometer, by Rigaku (1 mentions) Esquire 6000, by Bruker (1 mentions) Deuterated solvent, by Cambridge Isotopes (1 mentions) Prism software, by GraphPad (1 mentions) Cary eclipse, by Agilent Technologies (1 mentions) Ascend 400 mhz, by Bruker (1 mentions) J 715 cd spectrophotometer, by Jasco (1 mentions) Uv 2700, by Shimadzu (1 mentions) Fv1000, by Olympus (1 mentions) Sep pak c18 cartridge, by Waters Corporation (1 mentions) Saturn 724 ccd diffractometer, by Rigaku (1 mentions) Av 400 spectrometer, by Bruker (1 mentions) Waters alliance 2695 system, by Waters Corporation (1 mentions) Tsc sp8, by Leica (1 mentions) Arx 400, by Bruker (1 mentions) Lcms 20ad, by Shimadzu (1 mentions) Esi l low concentration tuning mix, by Agilent Technologies (1 mentions) 1200 system, by Phenomenex (1 mentions) Gemini c18, by Agilent Technologies (1 mentions)

Close spelling variants of this product

LC-Q-TOF-MS 6520 spectrometer Agilent 6520 Accurate-Mass Q-TOF LC/MS System Agilent 6520 Q-TOF LC-MS mass spectrometer HPLC/6520 Accurate-Mass Q-TOF LC/MS analysis Agilent 6520 Accurate Mass Q-TOF LC/MS 6520 Accurate-Mass Q-TOF LC/MS system 6520 Q-TOF LC/MS mass spectrometer 6520 Accurate‐Mass Q‐TOF LC/MS apparatus Accurate-Mass-Q-TOF LC/MS 6520 instrument 6520 Q‐TOF LC–MS (HRMS

24 protocols using 6520 q tof lc ms

Mass Spectrometry Analysis of Trastuzumab-GCSF Fusion Proteins

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Example 29

10 μg of purified trastuzumab-coil-hGCSF (CDRH2), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 23A The expected molecular weight for trastuzumab-coil-hGCSF (CDRH2) HC is 71,472 Da. The observed molecular weight for trastuzumab-coil-hGCSF (CDRH2) HC was 72,300 Da. The observed molecular weight correlates to O-glycosylation on hGCSF. 10 μg of purified trastuzumab-coil-hGCSF (CDRL3), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 23B. The expected molecular weight for trastuzumab-coil-hGCSF (CDRL3) LC is 45,746 Da. The observed molecular weight for trastuzumab-coil-hGCSF (CDRL3) LC was 46,692 Da. The observed molecular weight correlates to O-glycosylation on hGCSF.

US11673959B2. Coiled coil immunoglobulin fusion proteins and compositions thereof (2023-06-13). THE SCRIPPS RESEARCH INSTITUTE [US]. Inventors: Feng Wang [US], Yong Zhang [US], Yan Liu [US], Peter G. Schultz [US].

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Characterization of Trastuzumab-coil Fusion Proteins

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Example 39

10 μg of purified Trastuzumab-coil-hGCSF/EPO dual fusion protein (SEQ ID NOs: 62, 63), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 31A. The expected molecular weight for trastuzumab-coil hGCSF (CDRL3) LC is 45,746 Da. The observed molecular weight for trastuzumab-coil hGCSF (CDRL3) LC was 46,690 Da. The observed molecular weights correlates to O-glycosylation on hGCSF.

10 μg of purified Trastuzumab-coil-hGCSF/EPO dual fusion protein (SEQ ID NOs: 62, 63), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 31B. The expected molecular weight for trastuzumab-coil hEPO (CDRH3) HC is 70,307 Da. The observed molecular weights for trastuzumab-coil-hEPO (CDRH3) HC was 70,179 Da (correlating to the mass of trastuzumab-coil hEPO (CDRH3) HC without the first amino acid glutamic acid) and 71,126 Da (correlating to O-glycosylation on hEPO).

US10683353B2. Coiled coil immunoglobulin fusion proteins and compositions thereof (2020-06-16). THE SCRIPPS RESEARCH INSTITUTE [US]. Inventors: Feng Wang [US], Yong Zhang [US], Yan Liu [US], Peter G. Schultz [US].

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Characterization of Trastuzumab-Coil Fusion Proteins

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Example 39

10 μg of purified Trastuzumab-coil-hGCSF/EPO dual fusion protein (SEQ ID NOs: 62, 63), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 31A The expected molecular weight for trastuzumab-coil hGCSF (CDRL3) LC is 45,746 Da. The observed molecular weight for trastuzumab-coil hGCSF (CDRL3) LC was 46,690 Da. The observed molecular weights correlates to O-glycosylation on hGCSF.

10 μg of purified Trastuzumab-coil-hGCSF/EPO dual fusion protein (SEQ ID NOs: 62, 63), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 31B. The expected molecular weight for trastuzumab-coil hEPO (CDRH3) HC is 70,307 Da. The observed molecular weights for trastuzumab-coil-hEPO (CDRH3) HC was 70,179 Da (correlating to the mass of trastuzumab-coil hEPO (CDRH3) HC without the first amino acid glutamic acid) and 71,126 Da (correlating to 0-glycosylation on hEPO).

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Mass Spectrometry Analysis of Trastuzumab-GCSF Fusion

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Example 29

10 μg of purified trastuzumab-coil-hGCSF (CDRH2), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 23A. The expected molecular weight for trastuzumab-coil-hGCSF (CDRH2) HC is 71,472 Da. The observed molecular weight for trastuzumab-coil-hGCSF (CDRH2) HC was 72,300 Da. The observed molecular weight correlates to O-glycosylation on hGCSF. 10 μg of purified trastuzumab-coil-hGCSF (CDRL3), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 23B. The expected molecular weight for trastuzumab-coil-hGCSF (CDRL3) LC is 45,746 Da. The observed molecular weight for trastuzumab-coil-hGCSF (CDRL3) LC was 46,692 Da. The observed molecular weight correlates to O-glycosylation on hGCSF.

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Deglycosylation and Mass Spectrometry of Trastuzumab-Coil-Exendin-4

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Example 13

10 μg of purified trastuzumab-coil-exendin-4 heavy chain (HC) fusion (SEQ ID NOs: 71 and 19), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 13. The expected molecular weight for trastuzumab-coil-exendin-4 HC is 56,880 Da. The observed molecular weight for trastuzumab-coil-exendin-4 HC was 56,748 Da. The observed molecular weight correlates to the expected molecular weight without the first amino acid glutamic acid (E).

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Comprehensive Characterization of Materials

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The fluorescence spectra were obtained on a Hitachi Model FL-4500 fluorescence spectrometer using a quartz cell with a 1 cm path length at room temperature. The UV-vis absorption spectrum was recorded by a UV-3600 visible spectrophotometer (Shimadzu, Japan) at room temperature. A Rigaku Smart Lab diffractometer (Rigaku, Japan) was utilized to record powder X-ray diffraction spectrometry (PXRD) patterns with a 2θ range from 2–30° and monochromated Cu Kα radiation (λ = 1.5418 Å). A JSM-7500F scanning electron microscope (SEM) (JEOL, Japan) was used to obtain the morphology of the materials. Thermogravimetric analyses (TGA) were performed by a TG 8121 analyzer at heating rate of 15 °C min⁻¹ from room temperature to 700 °C (Rigaku, Japan). A MAGNA-IR 560 spectrometer (Nicolet, USA) was used to recorded Fourier-transform infrared (FT-IR) spectrum in the range 3000–400 cm⁻¹ with KBr tablet method. The mass spectral was recorded by 6520 Q-TOF LC/MS (Agilent, USA). An ICS-1100 ion chromatograph (IC) was used to measure anions in seawater, which equipped with Dionex IonPac™ AS14 column (Thermo, USA). The measurement of Eu³⁺ and mental ions in sea water was carried out on a Spectro Blue inductively coupled plasma-optical emission spectroscopy (ICP-OES) (Spectro, Germany).

Wei Y, & Xia Y. (2020). A dual emission metal–organic framework for rapid ratiometric fluorescence detection of CO32− in seawater. RSC Advances, 10(42), 24764-24771.

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Analytical Procedures for Small Molecules

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All reagents
and solvents were purchased from
Sigma–Aldrich, Alfa Aesar, or Toronto Research Chemicals, except
for deuterated solvents, which were purchased from Cambridge Isotope
Laboratories. Flash chromatography was performed on a Biotage SP1
instrument with HP-Sil columns. NMR spectroscopy was performed on
a 400 MHz Varian spectrometer (Oxford AS-400) operating at 25 °C,
unless otherwise specified. Spectra were referenced to the solvent
peak according to published values,^{50 (link)} except
for ³¹P spectra, which were referenced to orthophosphate
or phosphoric acid (0 ppm). High-resolution mass spectrometry was
carried out on a Waters Q-TOF micro LC-MS or an Agilent 6520 QTOF
LC-MS. Low resolution electrospray ionization mass spectrometry (ESI-MS)
was performed on a Bruker Esquire 6000 with direct injection. Preparative
high-performance liquid chromatography (HPLC) purification was performed
on a Varian ProStar instrument with a Dynamax Microsorb C18 column
(250 mm × 21.4 mm). Data analysis was performed using Prism software
(GraphPad).

Blain J.C., Ricardo A, & Szostak J.W. (2014). Synthesis and Nonenzymatic Template-Directed Polymerization of 2′-Amino-2′-deoxythreose Nucleotides. Journal of the American Chemical Society, 136(5), 2033-2039.

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Synthesis and Characterization of Adamantane-Modified cRGD

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All chemical reagents and solvents for synthesis were purchased from commercial sources (Aladdin Industrial Corporation, Tokyo Chemical Industry and Sigma-Aldrich Chemical) and were used without further purification. Adamantane modified cRGD was purchased from GL Biochem (Shanghai) Ltd All moisture-sensitive reactions were carried out under an atmosphere of nitrogen. Ultrapure water was used after passing through a water ultra-purification system. ¹H NMR and ¹³C NMR spectra were recorded on an Ascend 400 MHz (BRUKER) at room temperature. High-resolution mass spectra (HRMS) were measured on a 6520 Q-TOF LC/MS (Agilent). Absorption spectra were recorded on a UV-vis spectrophotometer (UV-2700, Shimadzu), and steady-state fluorescence emission spectra were recorded in a conventional quartz cell (10 × 10 × 45 mm) at 25 °C on a Varian Cary Eclipse equipped with a Varin Cary single-cell Peltier accessory to control temperature. Absolute fluorescence quantum yields were recorded on a FLS980 instrument (Edinburgh Instruments Ltd, Livingstone, UK). CD spectra were recorded on a Jasco J 715 CD spectrophotometer. Confocal fluorescence and bright-field imaging were recorded with an FV1000 (Olympus).

Liu Z., Zhou W., Li J., Zhang H., Dai X., Liu Y, & Liu Y. (2020). High-efficiency dynamic sensing of biothiols in cancer cells with a fluorescent β-cyclodextrin supramolecular assembly. Chemical Science, 11(18), 4791-4800.

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Deglycosylation and Mass Analysis of Trastuzumab-Coil-Exendin-4 Fusion

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Example 13

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Characterization of Trastuzumab-coil-hEPO Fusion Protein

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Example 34

10 μg of purified trastuzumab-coil-hEPO (CDRH3), in PBS (pH 7.4) was treated overnight at 37° C. with 1 μL (500 units) of peptide-N-glycosidase (NEB), followed by the addition of 50 mM DTT. The fusion protein was analyzed by ESI-MS using a 6520 Q-TOF LC/MS from Agilent Technology. The chromatograph is shown in FIG. 27. The expected molecular weight for trastuzumab-coil-hEPO (CDRH3) HC is 70,307 Da. The observed molecular weight for trastuzumab-coil-hEPO (CDRH3) HC was 70,177 Da. The observed molecular weight correlates to O-glycosylation on hEPO and the absence of the first amino acid glutamic acid (E).

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