Amicon ultra 0.5 centrifugal filter unit 3 kda

Manufactured by Merck Group

Sourced in Germany

The Amicon Ultra-0.5 Centrifugal Filter Unit 3 kDa is a laboratory filtration device designed for the concentration and purification of macromolecules, such as proteins and peptides, with molecular weights greater than 3 kDa. The unit features a centrifugal design that facilitates rapid sample processing. The filter membrane has a 3 kDa molecular weight cutoff, allowing the efficient separation of target molecules from smaller contaminants.

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Amicon Ultra (740 citations) Amicon filters (181 citations) Amicon centrifugal filters (166 citations) Centrifugal filter units (146 citations) Amicon Ultra filters (132 citations) Centrifugal filter (122 citations) Amicon Ultra-0.5 (105 citations) Amicon filter units (21 citations) Amicon centrifugal units (20 citations) Amicon Ultra centrifugal units (17 citations)

4 protocols using amicon ultra 0.5 centrifugal filter unit 3 kda

Carbohydrate Profiling: Standards and Preparation

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Standards of mono- and disaccharides: d-fructose, d-glucose, d-galactose, d-(+)-sucrose, d-lactose monohydrate, and ammonia solution (25%, LC-MS LiChropur™ grade) were obtained from Sigma-Aldrich (Darmstadt, Germany). Glucose-¹³C₆ (Glu-¹³C₆, U-¹³C₆, 99%, chemical purity 98%) and lactose monohydrate (Lac-¹³C₆, UL-¹³C₆glc, 98%+) were procured from Cambridge Isotope Laboratories Inc. (Tewksbury, MA, USA). Ultrapure water (18.2 MΩ.cm) was prepared with MilliQ^® Direct-Q^® UV (Merck KGaA, Darmstadt, Germany). Acetonitrile (MeCN; LiChrosolv, HPLC gradient grade), and guanidine hydrochloride (GuHCl; ≥99%) were acquired from Sigma-Aldrich (Darmstadt, Germany). Biotage Isolute® PLD+, C18 and NH₂ were procured from Biotage Sweden AB (Uppsala, Sweden). Amicon Ultra-0.5 centrifugal filter unit (3 kDa) and Millex-LCR filters (Pore size 0.2 µm, Filter Dimension 13 mm) were obtained from Merck KGaA (Darmstadt, Germany) and Microsep Advance Centrifugal Devices with Omega Membrane 1K filter unit was purchased from Pall Corporation (Port Washington, NY, USA).

Pismennõi D., Kiritsenko V., Marhivka J., Kütt M.L, & Vilu R. (2021). Development and Optimisation of HILIC-LC-MS Method for Determination of Carbohydrates in Fermentation Samples. Molecules, 26(12), 3669.

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Quantitative Analysis of Bacterial Cyclases

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Overnight cultures of E. coli harboring the Pycsar systems and negative controls were diluted 1:100 in 250 ml MMB medium (with or without arabinose, as described in Table S4) and grown at 37°C (250 rpm) until reaching OD₆₀₀ of 0.3. The cultures containing the cyclase from E. coli E831 were infected by T5, and cells containing the Pycsar system from X. perforans GEV1001 were infected by T7 at a final MOI of 2. Following the addition of phage, at 15, 30, and 40 min post infection for T5- (WT or mutant) infected cells, or at 5 and 10 min post infection for T7-infected cells (plus an uninfected control sample). 50 ml samples were taken and centrifuged for 5 min at 3200×g. The culture pellets were flash frozen using dry ice and ethanol. The pellets were re-suspended in 600 μl of 100 mM phosphate buffer at pH 8 and supplemented with 4 mg ml⁻¹ lysozyme. The samples were then transferred to a FastPrep Lysing Matrix B 2 ml tube (MP Biomedicals cat. #116911100) and lysed using a FastPrep bead beater for 40 s at 6 m s⁻¹ (two cycles). Tubes were then centrifuged at 4°C for 15 min at 15,000×g. Supernatant was transferred to Amicon Ultra-0.5 Centrifugal Filter Unit 3 kDa (Merck Millipore cat. #UFC500396) and centrifuged for 45 min at 4°C at 12,000×g. Filtrate was taken and used for LC-MSMS analysis.

Tal N., Morehouse B.R., Millman A., Stokar-Avihail A., Avraham C., Fedorenko T., Yirmiya E., Herbst E., Brandis A., Mehlman T., Oppenheimer-Shaanan Y., Keszei A.F., Shao S., Amitai G., Kranzusch P.J, & Sorek R. (2021). Cyclic CMP and cyclic UMP mediate bacterial immunity against phages. Cell, 184(23), 5728-5739.e16.

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Metabolomic Analysis of Bacterial SARM1 Domains

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Overnight cultures of bacteria containing WT or mutated SARM1 TIR domains were diluted 1:100 in 200 mL MMB and incubated at 37°C with shaking (200 r.p.m.) until reaching OD₆₀₀ of 0.3. At this point, IPTG was added to a concentration of 1 mM and the temperature was dropped to 30°C for an additional 4 hours. 50 mL samples were collected and centrifuged at 4°C for 10 min to pellet the cells. The supernatant was discarded and the tube was frozen at −80°C. To extract the metabolites, 600 μl of 100 mM Na phosphate buffer at pH 8 was added to each pellet. The thawed samples were transferred to a FastPrep Lysing Matrix B 2 mL tube (MP Biomedicals catalogue no. 116911100) and lysed using FastPrep bead beater for 40 s at 6 m s⁻¹ in two rounds. Tubes were then centrifuged at 4°C for 15 min at 15,000g. Supernatant was transferred to Amicon Ultra-0.5 Centrifugal Filter Unit 3 kDa (Merck Millipore catalogue no. UFC500396) and centrifuged for 45 min at 4°C at 12,000g. Where specified, filtrate was incubated with cmTad1 as previously described in Leavitt et al., 2022. Filtrate was taken and used for ThsA activity assays and for liquid chromatography mass spectrometry (LC-MS) analyses.

Garb J., Amitai G., Lu A., Ofir G., Brandis A., Mehlman T., Kranzusch P.J, & Sorek R. (2024). The SARM1 TIR domain produces glycocyclic ADPR molecules as minor products. PLOS ONE, 19(4), e0302251.

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Phage Infection Dynamics in E. coli

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Overnight cultures of E. coli harboring the defensive system and negative controls were diluted 1:100 in 250 mL MMB medium (with or without 0.2% arabinose, as described in Table S4 and grown at 37°C (250 rpm) until reaching OD₆₀₀ of 0.3. The cultures were infected by T2 or T4 at a final MOI of 2. Following the addition of phage, at 5, 15 and 60 or 120 min post infection (plus an uninfected control sample), 50 mL samples were taken and centrifuged for 5 min at 15,000 × g. Pellets were flash frozen using dry ice and ethanol. The pellets were re-suspended in 600 μL of 100 mM phosphate buffer at pH 8 and supplemented with 4 mg mL⁻¹ lysozyme. The samples were then transferred to a FastPrep Lysing Matrix B 2 mL tube (MP Biomedicals cat. #116911100) and lysed using a FastPrep bead beater for 40 s at 6 m s⁻¹ (two cycles). Tubes were then centrifuged at 4°C for 15 min at 15,000 × g. Supernatant was transferred to Amicon Ultra-0.5 Centrifugal Filter Unit 3 kDa (Merck Millipore cat. #UFC500396) and centrifuged for 45 min at 4°C at 12,000 × g. Filtrate was taken and used for LC-MS analysis.

Duncan-Lowey B., Tal N., Johnson A.G., Rawson S., Mayer M.L., Doron S., Millman A., Melamed S., Fedorenko T., Kacen A., Brandis A., Mehlman T., Amitai G., Sorek R, & Kranzusch P.J. (2023). Cryo-EM structure of the RADAR supramolecular anti-phage defense complex. Cell, 186(5), 987-998.e15.

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