Unless otherwise described, all commercial reagents and solvents were purchased from commercial suppliers and used without further purification. All reactions were performed under a N2 atmosphere in flame-dried glassware. Reactions were monitored using TLC with 0.25 mm E. Merck precoated silica gel plates (60 F254). Reaction progress was monitored using TLC analysis using a UV lamp, ninhydrin, or p-anisaldehyde stain for detection purposes. All solvents were purified using standard techniques. Purification of reaction products was carried out using silica gel column chromatography with Kieselgel 60 Art. 9385 (230–400 mesh). Purities of all compounds were ≥95%, and mass spectra and purities of all compounds was accessed using Waters LC/MS system (Waters QDA Detector, Waters 2998 Photodiode Array Detector, Waters SFO System Fluidics Organizer, Water 2545 Binary Gradient Module, Waters 2767 Sample Manager) using SunFire C18 column (4.6 × 50 mm, 5 μm particle size): solvent gradient = 30% B at 0.00 min, 30% B at 1.00 min, 100% B at 7.00 min, 100% B at 8.00 min, 30% B at 8.01 min, 30% B at 10.00 min. Solvent A = 0.1% HCOOH in H2O; Solvent B = 0.1% HCOOH in MeOH; flow rate = 0.8 mL/min. 1H and 13C NMR spectra were obtained using Bruker 400 MHz FT-NMR (400 MHz for 1H, and 100 MHz for 13C) spectrometer. Standard abbreviations are used for denoting the signal multiplicities.
Sfo system fluidics organizer
Manufactured by Waters Corporation
Sourced in United States
The SFO System Fluidics Organizer is a modular and configurable laboratory equipment designed to manage and organize fluid handling systems. It provides a structured and efficient way to arrange and connect various fluidic components, such as tubing, valves, and sensors, within a laboratory environment.
Automatically generated - may contain errors
Lab products found in correlation
2535 quaternary gradient module, by Waters Corporation (5 mentions)
Waters 2767 sample manager, by Waters Corporation (4 mentions)
515 hplc pump, by Waters Corporation (4 mentions)
Waters 2998 photodiode array detector, by Waters Corporation (3 mentions)
Waters 3100 mass detector, by Waters Corporation (2 mentions)
2767 sample manager, by Waters Corporation (2 mentions)
Reagent manager, by Waters Corporation (2 mentions)
Masslynx 4, by Waters Corporation (2 mentions)
Water 2545 binary gradient module, by Waters Corporation (1 mentions)
400 mhz ft nmr, by Bruker (1 mentions)
Waters 515 hplc pump, by Waters Corporation (1 mentions)
1260 infinity hplc system, by Thermo Fisher Scientific (1 mentions)
Lcq decaxp ms detector, by Thermo Fisher Scientific (1 mentions)
1525 binary hplc pump, by Waters Corporation (1 mentions)
Typhoon 9410 variable mode imager, by GE Healthcare (1 mentions)
Enf 260c fe hand hang uv lamp, by Spectroline (1 mentions)
2545 binary gradient module, by Waters Corporation (1 mentions)
2998 photodiode array detector, by Waters Corporation (1 mentions)
3100 mass detector, by Waters Corporation (1 mentions)
Avance 300, by Bruker (1 mentions)
8 protocols using sfo system fluidics organizer
1
General Organic Synthesis Protocol
2
Biophysical Characterization of Biomolecules
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
In-gel fluorescence scanning was performed using a Typhoon 9410 variable mode imager (excitation 532 nm, emission 580 nm). Isothermal titration calorimetry measurements were performed on a MicroCal iTC200 titration calorimeter (Malvern Instruments, United Kingdom). Peptides were purified on a preparative HPLC system with Waters (Milford, MA) 2535 Quaternary Gradient Module, Waters 515 HPLC pump, Waters SFO System Fluidics Organizer, and Waters 2767 Sample Manager. Enzymatic reactions were monitored by an LC-MS system with Waters 1525 Binary HPLC Pump, Waters 2998 Photodiode Array Detector, and Waters 3100 Mass Detector. Detection of O-Cr-ADPR was carried out by Agilent (Santa Clara, CA) 1260 Infinity HPLC system connected to a Thermo Fisher Scientific LCQ DecaXP MS detector.
3
Analytical Characterization of Peptides
Check if the same lab product or an alternative is used in the 5 most similar protocols
1H NMR (300 MHz or 400 MHz), 13C NMR (75 MHz, 100 MHz) were conducted on a Bruker spectrometer at 25 °C and were calibrated using residual undeuterated solvent as an internal reference. Chemical shifts were reported in ppm and coupling constants (J) were quoted to the nearest 0.1 Hz. High resolution mass spectrometry (HRMS) was recorded using a Bruker maXis II High Resolution QTOF. Peptides were analyzed by LC-MS with an Agilent 1260 Infinity HPLC system connected to a Thermo Finnigan LCQ DecaXP MS detector. Peptides were further purified by a preparative HPLC system with Waters 2535 Quaternary Gradient Module, Waters 515 HPLC pump, Waters SFO System Fluidics Organizer and Waters 2767 Sample Manager.
Photo-cross-linking were performed with ENF-260C/FE hand-hang UV lamp (Spectroline). In-gel fluorescence scanning was performed using a Typhoon 9410 variable mode imager from GE Healthcare Life Sciences (excitation 532 nm, emission 580 nm). All images were processed by ImageJ software (National Institutes of Health), and contrast was adjusted appropriately.
+ Expand
1H NMR (300 MHz or 400 MHz), 13C NMR (75 MHz, 100 MHz) were conducted on a Bruker spectrometer at 25 °C and were calibrated using residual undeuterated solvent as an internal reference. Chemical shifts were reported in ppm and coupling constants (J) were quoted to the nearest 0.1 Hz. High resolution mass spectrometry (HRMS) was recorded using a Bruker maXis II High Resolution QTOF. Peptides were analyzed by LC-MS with an Agilent 1260 Infinity HPLC system connected to a Thermo Finnigan LCQ DecaXP MS detector. Peptides were further purified by a preparative HPLC system with Waters 2535 Quaternary Gradient Module, Waters 515 HPLC pump, Waters SFO System Fluidics Organizer and Waters 2767 Sample Manager.
Photo-cross-linking were performed with ENF-260C/FE hand-hang UV lamp (Spectroline). In-gel fluorescence scanning was performed using a Typhoon 9410 variable mode imager from GE Healthcare Life Sciences (excitation 532 nm, emission 580 nm). All images were processed by ImageJ software (National Institutes of Health), and contrast was adjusted appropriately.
4
Purification of Synthesized Proteins
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
All the buffers were prepared with ddH2O using the standard methods. The synthesized proteins were purified on a preparative high performance liquid chromatography (HPLC) system with a Waters 2535 Quaternary Gradient Module, a Waters 515 HPLC pump, a Waters SFO system Fluidics Organizer and a Waters 2767 Sample Manager. The synthesis of compound 1 was performed following a previously reported method.14 (link)
5
Comprehensive Analytical Techniques for Compounds
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Electrothermal Capillary apparatus (Staffordshire, UK) was used to detect all melting points. NMR spectral analyses were performed using a Bruker Avance 300 or 400 spectrometer ((Bruker Bioscience, Billerica, MA, USA) using TMS as standard, and chemical shift values were recorded in ppm. LC–MS analysis was performed using a Waters 3100 mass detector (Milford, USA), Waters 2998 photodiode array detector, Waters SFO system fluidics organizer, Waters 2545 binary gradient module, Waters reagent manager, Waters 2767 sample manager and Sunfire™ C18 column (4.6 × 50 mm, 5 μm particle size); solvent gradient = 95% A at 0min, 1% A at 5min; solvent A: 0.035% trifluoroacetic acid in deionized water; solvent B: 0.035% trifluoroacetic acid in methanol; FR = 3.0 mL/min. The AUC was calculated using Waters MassLynx 4.1 software. All reagents and solvents were purchased from Aldrich chemical Co. and Tokyo Chemical Industry (TCI) Co., and used without further purification.
6
Purification and Characterization of Organic Compounds
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The intermediate compounds as well as the target compounds were purified by flash column chromatography using silica gel 60 (0.040-0.063 mm, 230-400 mesh ASTM)
and technical grade solvents. 1 H NMR and 13 C NMR analyses were carried out on a Bruker Avance 400 spectrometer using tetramethylsilane (TMS) as an internal standard. Melting points were measured on a Walden Precision Apparatus Electrothermal 9300 apparatus and were uncorrected. LC-MS analysis was conducted using the following system: Waters 2998 photodiode array detector, Waters 3100 mass detector, Waters SFO system fluidics organizer, Waters 2545 binary gradient module, Waters reagent manager, Waters 2767 sample manager, Sunfire™ C 18 column (4.6 × 50 mm, 5 μm particle size); Solvent gradient = 95% A at 0 min, 1% A at 5 min; solvent A: 0.035% trifluoroacetic acid (TFA) in water; solvent B: 0.035% TFA in MeOH; flow rate = 3.0 mL/min; the AUC was calculated using Waters MassLynx 4.1 software. The solvents and liquid reagents were transferred using hypodermic syringes. All the solvents and reagents were purchased from commercial companies, and used as such.
and technical grade solvents. 1 H NMR and 13 C NMR analyses were carried out on a Bruker Avance 400 spectrometer using tetramethylsilane (TMS) as an internal standard. Melting points were measured on a Walden Precision Apparatus Electrothermal 9300 apparatus and were uncorrected. LC-MS analysis was conducted using the following system: Waters 2998 photodiode array detector, Waters 3100 mass detector, Waters SFO system fluidics organizer, Waters 2545 binary gradient module, Waters reagent manager, Waters 2767 sample manager, Sunfire™ C 18 column (4.6 × 50 mm, 5 μm particle size); Solvent gradient = 95% A at 0 min, 1% A at 5 min; solvent A: 0.035% trifluoroacetic acid (TFA) in water; solvent B: 0.035% TFA in MeOH; flow rate = 3.0 mL/min; the AUC was calculated using Waters MassLynx 4.1 software. The solvents and liquid reagents were transferred using hypodermic syringes. All the solvents and reagents were purchased from commercial companies, and used as such.
7
Purification and Characterization of Peptides
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
All NMR spectra were recorded on a Bruker 300 or 400 MHz spectrometer. The chemical shifts were reported in ppm, and J values were reported in Hz. Peptides were purified on a Grace VYDACÒ 218TP152025 C18 column connected to a preparative-HPLC system with Waters 2535 Quaternary Gradient Module, Waters 515 HPLC pump, Waters SFO system Fluidics Organizer and Waters 2767 Sample Manager. Analytical HPLC trace after purification was obtained using a Grace VYDACÒ 218TP C18 5m column connected to an HPLC system with Agilent 1260 Infinity Quaternary Pump VL, Agilent 1260 Infinity Manual Injector and Agilent 1260 Infinity Variable Wavelength Detector. The outlet of the above HPLC system was connected to Thermo Finnigan LCQ Deca XP to obtain MS spectrums of purified peptides.
Starting materials for organic synthesis were purchased from common commercial suppliers including Sigma-Aldrich, TCI and Alfa and used without further purification. All reactions were monitored by TLC Silica gel 60 F254 from Merck. Flash column chromatography was performed with silica gel purchased from Grace (40-63 micron). All Fmoc-protected amino acids for and coupling reagents for solid phase peptide synthesis were purchased from GL Biochem (Shanghai, China).
Starting materials for organic synthesis were purchased from common commercial suppliers including Sigma-Aldrich, TCI and Alfa and used without further purification. All reactions were monitored by TLC Silica gel 60 F254 from Merck. Flash column chromatography was performed with silica gel purchased from Grace (40-63 micron). All Fmoc-protected amino acids for and coupling reagents for solid phase peptide synthesis were purchased from GL Biochem (Shanghai, China).
8
Fmoc-based Solid-Phase Peptide Synthesis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
All amino acids and coupling reagents were purchased from GL Biochem (Shanghai, China). All the peptides used in this research were synthesized on Rink-Amide MBHA resin or 2-Chlorotrityl chloride resin following standard Fmoc-based solid-phase peptide synthesis protocol. After the coupling of all amino acids, the removal of protecting groups and cleavage of peptides from the resin were done by incubating the resin with cleavage cocktail containing 95% trifluoroacetic acid (TFA), 2.5% triisopropylsilane, 1.5% water and 1% thioanisole for 2 h. Peptides were purified on a preparative high performance liquid chromatography (HPLC) system (Waters 2535 Quaternary Gradient Module, Waters 515 HPLC pump, Waters SFO system Fluidics Organizer and Waters 2767 Sample Manager) with a Vydac C18 column (22 mm X 250 mm, 10 mm, Garce). Mobile phase used were water with 0.1% TFA and 90% acetonitrile in water with 0.1% TFA. The purity (> 95%) and identity of peptides were confirmed by LC-MS, for details see Supplemental Information.
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!