Autoflex 2 spectrometer

Manufactured by Bruker

Sourced in Germany

The Autoflex II is a spectrometer manufactured by Bruker. It is designed for the analysis of samples using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The Autoflex II provides high-performance mass analysis capabilities for a variety of applications.

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Lab products found in correlation

Jnm ecp400, by JEOL (1 mentions) Silica gel 60n, by Kanto Chemical (1 mentions) Jnm eca600, by JEOL (1 mentions) Jnm ecx400, by JEOL (1 mentions) Ifs 66v s ftir spectrometer, by Bruker (1 mentions) D8 x ray diffractometer, by Brucker (1 mentions) Jsm 6700f, by Thermo Fisher Scientific (1 mentions) Tecnai g2 f20 s twin, by Thermo Fisher Scientific (1 mentions) Sta 449c, by Netzsch (1 mentions) Flashsmart elemental analyzer, by Thermo Fisher Scientific (1 mentions) M 565 apparatus, by Büchi (1 mentions) Avance neo 500, by Bruker (1 mentions) Ft ir 4700 spectrophotometer, by Jasco (1 mentions) Ziptipc18 pipette tip, by Merck Group (1 mentions) Sequencing grade modified trypsin, by Promega (1 mentions)

Close spelling variants of this product

Autoflex II MALDI-TOF/TOF mass spectrometer Autoflex II ToF/ToF spectrometer Autoflex II ToF/FoF spectrometer Autoflex II MALDI-TOF mass spectrometer Autoflex II mass spectrometer Autoflex II TOF/TOF mass spectrometer Autoflex II Bruker spectrometers

6 protocols using autoflex 2 spectrometer

Spectroscopic and Computational Analysis

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¹H NMR (400 MHz and 600 MHz) and ¹³C NMR (151 MHz) spectra were recorded with a JEOL JNM-ECX 400, a JEOL JNM-ECP 400 and a JEOL JNM-ECA 600 spectrometers by using tetramethylsilane as an internal standard. The HR-MALDI-TOF mass spectra were measured by a Bruker Autoflex II spectrometer using positive ion mode.
UV/Vis absorption spectra were measured with a JASCO UV/Vis/NIR spectrophotometer V-570.
TLC and gravity column chromatography were performed on Art. 5554 (Merck KGaA) plates and silica gel 60N (Kanto Chemical), respectively. All other solvents and chemicals were reagent-grade quality, obtained commercially, and used without further purification. For spectral measurements, spectral-grade solvents were purchased from Nacalai Tesque.
All DFT calculations were performed with a Gaussian 09 program package. The geometries were fully optimized at the Becke's three-parameter hybrid functional combined with the Lee–Yang–Parr correlation functional abbreviated as the B3LYP level of density functional theory. The 6-31G(d) bases set implemented was used for structure optimizations and frequency analyses.

Mei P., Matsumoto A., Hayashi H., Suzuki M., Aratani N, & Yamada H. (2018). 1,3-Phenylene-bridged naphthalene wheels synthesized by one-pot Suzuki–Miyaura coupling and the complex of the hexamer with C60. RSC Advances, 8(37), 20872-20876.

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Comprehensive Materials Characterization

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The crystal structures of the materials were studied by XRD (Brucker D8 X‐ray diffractometer) with Cu Kα radiation (λ = 1.5418) at room temperature. IR spectra were measured with KBr pellets on a Bruker IFS‐66 V/S FTIR spectrometer. Thermogravimetric measurement was performed on preweighed samples in a nitrogen stream using a Netzsch STA 449C apparatus with a heating rate of 10 °C min⁻¹ under N₂ atmosphere. The morphologies of the materials were investigated using a field emission SEM (JEOL JSM‐6700F) and TEM (FEI Tecnai G2 F20 S‐TWIN). XPS was performed on ESCALAB 250 with Mg Kα as the X‐ray source. The Raman spectroscopy was tested using a Renishaw in via Raman microscope with Ar‐ion laser excitation (λ = 514.5 nm). MALDI‐TOF mass spectroscopy was recorded on a Bruker Autoflex II spectrometer. PAQS was measured in positive ion mode using trans‐2‐[3‐(4‐tert‐butylphenyl)‐2‐methyl‐2‐propenylidene]malononitrile (DCTB) as the matrix.

Zhang S., Zhu Y., Wang D., Li C., Han Y., Shi Z, & Feng S. (2022). Poly(Anthraquinonyl Sulfide)/CNT Composites as High‐Rate‐Performance Cathodes for Nonaqueous Rechargeable Calcium‐Ion Batteries. Advanced Science, 9(14), 2200397.

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NMR Spectroscopy and Characterization Methods

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NMR spectra were acquired at room temperature on a Bruker Avance Neo 500 spectrometer. The chemical shifts (δ) are reported in ppm and are referenced internally to the solvent signals of CDCl₃ (¹H, δ = 7.27 ppm; ¹³C, δ = 77.0 ppm) or externally to CFCl₃ (¹⁹F, 0.0 ppm). The coupling constants J are given in Hz. In the ¹H NMR spectra, the following abbreviations are used to describe the peak patterns: s (singlet), d (doublet), t (triplet), m (multiplet). In the ¹³C NMR spectra, the nature of the carbons (C, CH, CH₂, or CH₃) was determined by performing APT or DEPT experiments. The IR spectra were recorded with a Jasco FT/IR-4700 spectrophotometer equipped with an attenuated total reflectance (ATR) accessory. MALDI-TOF mass spectra were recorded on a Bruker Autoflex II spectrometer in positive detection mode, using dithranol as matrix. Melting points (°C) were measured on a Büchi M-565 apparatus and are uncorrected. Elemental analyses were performed in a Thermo Scientific Flash Smart elemental analyzer (Thermo Scientific, Waltham, MA, USA).

López S., Gracia I., Plaza-Pedroche R., Rodríguez J.F., Pérez-Ortiz J.M., Rodríguez-López J, & Ramos M.J. (2022). In Vitro Antioxidant and Pancreatic Anticancer Activity of Novel 5-Fluorouracil-Coumarin Conjugates. Pharmaceutics, 14(10), 2152.

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Capturing Serum Amyloid A from Plasma

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Affinity pipette tips conjugated with antibody against human serum amyloid A were prepared by Intrinsic Bioprobes of Thermo Fisher Scientific [29 (link),30 (link)]. The affinity pipette tips were used to capture SAA from 10 μL plasma samples from the third protease inhibitor/validation cohort in duplicate. Blinded plasma samples from six KD subjects and six FC subjects from the protease inhibitor/validation cohort were adsorbed to these pipette tips using an automatic stand-mounted multi-channel pipettor (Finnpipette). After extensive washing, the tips were eluted with sinipinic acid directly onto matrix assisted laser desorption ionization (MALDI) sample plates. MALDI mass spectra were acquired using a Bruker Autoflex II spectrometer. Exported spectra were baseline subtracted, minimally smoothed, and calibrated internally using ApoC-I and SAA1 peaks as calibrants using mMass software [31 (link)], and graphed with Datagraph software (Visual Data Tools Inc.).

Whitin J.C., Yu T.T., Ling X.B., Kanegaye J.T., Burns J.C, & Cohen H.J. (2016). A Novel Truncated Form of Serum Amyloid A in Kawasaki Disease. PLoS ONE, 11(6), e0157024.

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Synthesized Modular Peptide Dialysis and Characterization

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All MDPs were synthesized
on a low loading Rink Amide MBHA resin using an automated synthesizer
with protocols previously reported by our lab.^{25 (link),32 (link)} The crude peptides were dissolved in Milli-Q water and the resulting
solutions were dialyzed. K₂(SL)₆K₂ and K₂(TL)₆K₂ were dialyzed using
100–500 Da cutoff bags, K₂(SL)₆K₂GRGDS and K₂(TL)₆K₂GRGDS using 1000 Da cutoff bags and K(SL)₃RG(SL)₃KGRGDS and K(TL)₂SLRG(TL)₃KGRGDS using 2000 Da cutoff bags. Each peptide solution
was dialyzed against Milli-Q water for 3 days, during which the dialysis
water was refreshed twice daily. Postdialysis the peptide was lyophilized
yielding a white peptide powder. MALDI-TOF mass spectrometry was performed
on a Bruker Autoflex II spectrometer to characterize the purified
peptides.

Kang M.K., Colombo J.S., D’Souza R.N, & Hartgerink J.D. (2014). Sequence Effects of Self-Assembling MultiDomain Peptide Hydrogels on Encapsulated SHED Cells. Biomacromolecules, 15(6), 2004-2011.

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MALDI-TOF Identification of Lipase and Foldase

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Spots corresponding to the N-truncated lipase and the N-truncated foldase were excised manually from an SDS-PAGE gel for analysis by matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS). Excised spots were in-gel digested with sequencing grade modified trypsin (Promega, Madison, WI, USA) as described elsewhere [89 ]. The sample was desalted using a ZipTipC₁₈ pipette tip (Millipore Corporation, Billerica, MA, USA) and eluted directly onto the MALDI target plate coated with MALDI matrix (saturated solution of α-cyano-4-hydroxycinnamic acid in 50% (V/V) acetonitrile and 0.1% trifluoroacetic acid). MALDI-TOF data were acquired with an Autoflex II spectrometer (Bruker Daltonics, Bremen, HB, Germany) in the reflector positive ion mode with an acceleration voltage of 20 kV, delay time of 150 ns and acquisition mass range of 800–3200 Da. The mass profiles obtained were compared with the peptide masses predicted by in silico digestion of the His-tagged protein sequence using the PeptideCutter and MS-Digest tools [48 (link)].

Martini V.P., Glogauer A., Müller-Santos M., Iulek J., de Souza E.M., Mitchell D.A., Pedrosa F.O, & Krieger N. (2014). First co-expression of a lipase and its specific foldase obtained by metagenomics. Microbial Cell Factories, 13, 171.

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