0.22 μm syringe filter

Manufactured by Thermo Fisher Scientific

Sourced in United States, United Kingdom

The 0.22 μm syringe filter is a lab equipment product designed to remove particulates and microorganisms from liquids. It features a 0.22 μm pore size membrane that effectively filters out particles and microbes from solutions prior to analysis or further processing.

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Lab products found in correlation

Tryptic soy broth (tsb), by Merck Group (2 mentions) Ni nitrilotriacetic acid nta superflow resin, by Qiagen (2 mentions) Kta fast protein liquid chromatographer, by GE Healthcare (2 mentions) Syringe pump, by Harvard Apparatus (1 mentions) Bca assay, by Thermo Fisher Scientific (1 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by Thermo Fisher Scientific (1 mentions) Ptrchis, by Thermo Fisher Scientific (1 mentions) 96 well round bottom plate, by Sarstedt (1 mentions) Fasudil hydrochloride, by Merck Group (1 mentions)

Close spelling variants of this product

Syringe filter (24 citations)

10 protocols using 0.22 μm syringe filter

Preparation of Staphylococcus Bacterial Cultures

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S. epidermidis (ATCC^® Catalog No.12228) and S. Aureus 113 (ATCC^® Catalog No. 35556^™) were acquired from ATCC. S. Epidermidis 1457 was a kind donation from the Gallo Lab (UCSD). Preparation of bacterial cultures was performed as follows: Bacterial stocks frozen at − 80 °C in TSB (Sigma-Aldrich, St. Louis, MO) with 20% glycerol were inoculated into 5 mL TSB. The culture was aerated by shaking at 120 rpm at 37 °C and grown overnight.
To define a concentration of 10⁶, the bacteria grown overnight were quantified by a spectrophotometer to Measure OD600 by using UNICO 1100 (OD600 = 1 is equal to 3 × 10⁸ CFU/mL). The bacterial culture was then centrifuged at 4000rpm, 15min. and filtered sterile using 0.22 μm syringe filters (Fisher Scientific, Waltham, MA). Aliquots of the same supernatant were kept at − 80 °C.

Apfel C.M., Evers S., Hubschwerlen C., Pirson W., Page M.G, & Keck W. (2001). Peptide Deformylase as an Antibacterial Drug Target: Assays for Detection of Its Inhibition in Escherichia coli Cell Homogenates and Intact Cells. Antimicrobial Agents and Chemotherapy, 45(4), 1053-1057.

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Amperometric Detection of Catechol

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With the embedded gold working electrode, a three-electrode system was utilized, with a Ag/AgCl reference electrode and a 250 μm platinum wire auxiliary electrode being placed in the reservoir at the channel exit. Amperometric detection of catechol was completed for all devices using the Amperometric i-t Curve technique in the CH1812C program. The voltage was fixed at +0.9 V vs Ag/AgCl for oxidative analysis. All catechol solutions, buffer, isopropanol (IPA), and water were filtered with 0.22 μm syringe filters (Fisherbrand, St. Louis, MO) before they were used in the device. Samples ranging from 0.2 −12.5 μM were made from a 7.45 mM catechol stock solution and diluted with PBS. A 1 mL gastight syringe was used to flow PBS buffer into the device. This syringe was connected to a 4-port valve (Valco Instruments Co. Inc., Houston, TX) with a 1 μL internal rotor by using capillary tubing with a NanoTight Tubing Sleeves (IDEX). The 3D-microfluidic device was connected to the system by another NanoTight Tubing Sleeve and an in-line filter in place before the device. The flow was controlled at 10 μL/min via syringe pump (Harvard Apparatus, Holliston, MA). Analysis of catechol was performed starting with a PBS blank and working up in concentration (0.1 – 12.5 μM).

Castiaux A.D., Currens E.R, & Martin R.S. (2020). Direct Embedding and Versatile Placement of Electrodes in 3D Printed Microfluidic-Devices. The Analyst, 145(9), 3274-3282.

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Preparation of Staphylococcus Bacterial Cultures

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Nardo A.D., Chang Y.L., Alimohammadi S., Masuda-Kuroki K., Wang Z., Sriram K, & Insel P.A. (2023). Mast cell tolerance in the skin microenvironment to commensal bacteria is controlled by fibroblasts. Cell reports, 42(5), 112453.

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Propolis Extraction and Preparation

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Propolis was collected in October 2019, from five different apiaries of a commercial beekeeping operation in Fayette and Clayton counties in Iowa. Samples were collected from 5–10 colonies at each location, yielding a total of 45 samples. Propolis was collected from the front rim of the top lid of each hive. This location on the hive was chosen because it is the area of most active recent propolis placement by honey bees, due to frequent beekeeper disturbance. Each propolis sample was collected into sterile plastic tubes and stored at −80 °C until further use. Propolis samples were then pulverized with a mortar and pestle, and diluted in 100% ethanol (0.2 g propolis in 1.8 g ethanol). Samples were then mixed at 500 rpm at 30 °C for 48 h in the dark. Samples were filtered using a 0.22 μm syringe filter (Fisher Scientific, Hampton, NH, USA). Filtered samples were then diluted according to specific needs for chemical or antimicrobial analysis.

Orth A.J., Curran E.H., Haas E.J., Kraemer A.C., Anderson A.M., Mason N.J, & Fassbinder-Orth C.A. (2022). Land Use Influences the Composition and Antimicrobial Effects of Propolis. Insects, 13(3), 239.

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Cocaine Hydrochloride Preparation and Formulation

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Cocaine hydrochloride (National
Institute on Drug Abuse, Bethesda, MD) was dissolved in sterile physiological
saline and filtered through a 0.22 μm syringe filter (Fisher
Scientific, Pittsburgh, PA) for sterilization purposes. 74 was mixed into a 10% EtOH, 1% Tween 80 solution.

Dhanya R.P., Sheffler D.J., Dahl R., Davis M., Lee P.S., Yang L., Nickols H.H., Cho H.P., Smith L.H., D’Souza M.S., Conn P.J., Der-Avakian A., Markou A, & Cosford N.D. (2014). Design and Synthesis of Systemically Active Metabotropic Glutamate Subtype-2 and -3 (mGlu2/3) Receptor Positive Allosteric Modulators (PAMs): Pharmacological Characterization and Assessment in a Rat Model of Cocaine Dependence. Journal of Medicinal Chemistry, 57(10), 4154-4172.

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Purification of Bank Vole Prion Protein

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The Bank Vole recombinant prion protein (rPrP^Sen) (residues 23 to 230; Methionine at residue 109; accession no. AF367624) was purified as previously described[53 (link)]. The vectors were transformed into Rosetta (DE3) Escherichia coli and grown in Luria broth medium with the addition of kanamycin and chloramphenicol. The expression of the protein was induced using the autoinduction system[54 ,55 (link)]. Inclusion bodies containing the protein were denatured and the protein was isolated using Ni-nitrilotriacetic acid (NTA) superflow resin (Qiagen) with an ÄKTA fast protein liquid chromatographer (GE Healthcare Life Sciences). Refolding of the protein was done on the column by means of a guanidine HCl reduction gradient. Elution was done with an imidazole gradient as described. Following elution, the protein was extensively dialyzed into 10 mM sodium phosphate buffer (pH 5.8), filtered (0.22-μm syringe filter (Fisher)) and stored at -80°C in 1mL aliquots. The protein concentration was determined by absorbance at 280 nm.

Wang F., Wang X., Orrú C.D., Groveman B.R., Surewicz K., Abskharon R., Imamura M., Yokoyama T., Kim Y.S., Vander Stel K.J., Sinniah K., Priola S.A., Surewicz W.K., Caughey B, & Ma J. (2017). Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity. PLoS Pathogens, 13(7), e1006491.

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Recombinant L1S Protein Expression

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L1S protein was expressed in an E. coli construct with a pTrcHis (Invitrogen) and purified. Briefly, log phase bacteria were incubated for 8 hours with IPTG (Life Technologies) to induce protein expression. Following cell lysis and DNAse treatment, lysates were centrifuged to pellet cellular debris. Supernatants were filtered through a 0.22 μm syringe filter (Fisher Scientific) and loaded onto an ATKA FPLC for nickel (Ni) column (GE Healthcare) for affinity purification of the His-tagged protein. Fractions from the eluted column were evaluated using SDS-PAGE and Coomassie staining. Fractions containing the L1S protein were concentrated using Millipore 10k KD columns (Millipore) and protein concentrations were determined using a BCA assay (Thermo Scientific).

Bortell N., Aguilera E.R, & Lenz L.L. (2021). Pulmonary insults exacerbate susceptibility to oral Listeria monocytogenes infection through the production of IL-10 by NK cells. PLoS Pathogens, 17(4), e1009531.

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Purification of Recombinant Prion Proteins

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Recombinant prion protein (rPrP^Sen) substrates were purified as previously described [49 (link)]. Briefly, PrP DNA sequences encoding for Syrian golden hamster (residues 23 to 231; accession no. K02234; or residues 90–231), Bank Vole (residues 23 to 230; Methionine at residue 109; accession no. AF367624) or hamster-sheep chimera (Syrian hamster residues 23 to 137 followed by sheep residues 141 to 234 of the R₁₅₄Q₁₇₁ polymorph [accession no. AY907689]) prion protein genes were ligated into the pET41 vector (EMD Biosciences). Vectors were transformed into Rosetta (DE3) Escherichia coli and were grown in Luria broth medium in the presence of kanamycin and chloramphenicol. Protein expression was induced using the autoinduction system [50 (link),51 (link)] and was purified from inclusion bodies under denaturing conditions using Ni-nitrilotriacetic acid (NTA) superflow resin (Qiagen) with an ÄKTA fast protein liquid chromatographer (GE Healthcare Life Sciences). The protein was refolded on the column using a guanidine HCl reduction gradient and eluted using an imidazole gradient as described [49 (link)]. The eluted protein was extensively dialyzed into 10 mM sodium phosphate buffer (pH 5.8), filtered (0.22-μm syringe filter [Fisher]) and stored at -80°C. Protein concentration was determined by measuring absorbance at 280 nm.

Orrú C.D., Groveman B.R., Raymond L.D., Hughson A.G., Nonno R., Zou W., Ghetti B., Gambetti P, & Caughey B. (2015). Bank Vole Prion Protein As an Apparently Universal Substrate for RT-QuIC-Based Detection and Discrimination of Prion Strains. PLoS Pathogens, 11(6), e1004983.

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C2C12 Cells Encapsulation in GelMA Hydrogel

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C2C12 muscle cell line cells were cultured in Gibco Dulbecco’s modified Eagle’s medium (DMEM) high glucose (Fisher Scientific UK Ltd., Loughborough, UK) supplemented with 10% FBS, 2 mM L-Glutamine, 100 U/mL penicillin, and 100 μg/mL streptomycin (PS) (Sigma-Aldrich, Merck Life Sciences UK Ltd., Poole, UK). GelMA hydrogel solution was mixed with LAP until wholly dissolved and sterilised by being passed through a 0.22 μM syringe filter (Fisher Scientific UK Ltd., Loughborough, UK). Next, 100 µL of GelMA was added to each well in a 96-well plate. An amount of 2.5 × 10⁴ of C2C12 cells were added to each sample, followed by gentle mixing to avoid air bubbles. Then, the well plate was placed in a UV curing chamber for 2 min for crosslinking before being incubated at 37 °C in the presence of 5% CO₂.

Aljaber M.B., Verisqa F., Keskin-Erdogan Z., Patel K.D., Chau D.Y, & Knowles J.C. (2023). Influence of Gelatin Source and Bloom Number on Gelatin Methacryloyl Hydrogels Mechanical and Biological Properties for Muscle Regeneration. Biomolecules, 13(5), 811.

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Fasudil Hydrochloride Cytotoxicity Evaluation

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After resuspending the cryovial contents in 1 mL of cell culture media, 50 μL of cell suspension was placed into each well of round bottom 96 well plates (Sarstedt). Fasudil hydrochloride (Sigma) solutions were then prepared at 2× the desired concentration in cell culture media and sterile filtered with a 0.22 μm syringe filter (Fisher Scientific). 50 μL was added to each well. The final fasudil concentration used varied from 40 μM to 1.25 μM. Cells were then incubated at 37 °C and 5% CO₂ for 4 h (timepoint selected after performing optimisation experiments). The plate was subsequently centrifuged at 300g and the media was changed to regular cell culture media (see ESI†). Cell health assessments (such as cell recovery) were performed 24 hours post-thaw. The minimum number of technical replicates per condition was 3.

Gonzalez-Martinez N, & Gibson M.I. (2023). Post-thaw application of ROCK-inhibitors increases cryopreserved T-cell yield. RSC Medicinal Chemistry, 14(10), 2058-2067.

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