Snakeskin dialysis tubing 10 k mwco

Manufactured by Thermo Fisher Scientific

Sourced in United States

Snakeskin Dialysis Tubing 10 K MWCO is a semi-permeable membrane used for dialysis. It has a molecular weight cut-off (MWCO) of 10,000 Daltons, allowing the passage of molecules below this size while retaining larger molecules. The tubing is made from regenerated cellulose and has a unique snakeskin-like appearance.

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10 protocols using snakeskin dialysis tubing 10 k mwco

Biotinylation of US28 protein interactors

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HEK293T cells were transfected with only 250 ng pcDEF3-US28 Bio ID2 or 250 ng pcDEF3-US28 Bio ID2 and 2 μg pcDEF3-nanobody-mVenus. During the same day of transfection, medium was replaced with medium containing a final concentration of 50 μM biotin. The next day, cells were lysed in native lysis buffer (25 mM Tris HCL pH7.4, 150 mM NaCl, 1 mM EDTA, 1% NP-40, 5% Glycerol, 1 mM NaF, 1 mM NaVO₃, cOmplete protease inhibitor cocktail) for 10 min on ice. Cell debris was removed by centrifugation at 13,000 × g. Cell lysate was dialyzed overnight using Snakeskin Dialysis Tubing 10 K MWCO (Thermo Fisher Scientific) to remove the excess of biotin. Protein concentration of lysates was determined by Pierce BCA protein assay kit (Thermo Fisher Scientific) and same protein quantities were separated on a 10% SDS-PAGE gel under reducing conditions and transferred to 0.45 μm PVDF blotting membrane (GE healthcare, Chicago, IL, USA). Biotinylated proteins were detected using neutravidin-HRP (1:2000 in 5% BSA/TBS-T, A2664, Thermo Fisher Scientific). Blots were developed using Western Lightning Plus-ECL (Perkin-Elmer, Waltham, MA, USA) and visualized with Chemidoc (Bio-Rad).

De Groof T.W., Bergkamp N.D., Heukers R., Giap T., Bebelman M.P., Goeij-de Haas R., Piersma S.R., Jimenez C.R., Garcia K.C., Ploegh H.L., Siderius M, & Smit M.J. (2021). Selective targeting of ligand-dependent and -independent signaling by GPCR conformation-specific anti-US28 intrabodies. Nature Communications, 12, 4357.

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Purification of Xylanase Enzymes

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The transformed cells were grown in LB medium containing 50 μg/mL kanamycin at 37 °C to an A_{600 nm} of 0.6. Protein expression was induced by addition of isopropyl-β-d-thiogalactopyranoside (IPTG) at a final concentration of 0.4 mM at 25 °C for 18 h. The cells were harvested by centrifugation (6000× g, 4 °C, 10 min) and lysed using B-PER™ Direct Bacterial Protein Extraction Kit (Thermo Scientific, Waltham, MA, USA) The crude enzyme was collected (12,000× g, 4 °C, 10 min) and dialyzed against 20 mM sodium phosphate buffer (pH 7.4) at 4 °C overnight in a SnakeSkin™ Dialysis Tubing 10k MWCO (Thermo Scientific, Waltham, MA, USA). To purify the His-tagged proteins, the crude enzyme was loaded onto a Ni-NTA Superflow column (Qiagen, Hilden, Germany) equilibrated with 20 mM sodium phosphate buffer (pH 7.4) and 50 mM imidazole. The enzymes were eluted with a linear gradient of 50–500 mM imidazole in 20 mM phosphate buffer (pH 7.4) containing 500 mM NaCl. Upon elution, fractions containing the XynRA2 and XynRA2ΔCBM were respectively pooled and dialyzed against 20 mM sodium phosphate buffer (pH 7.4) at 4 °C overnight to remove the remaining salts. The purity and apparent molecular mass of XynRA2 and XynRA2ΔCBM were validated by SDS-PAGE. The activity of the purified enzymes was assayed as described below.

Teo S.C., Liew K.J., Shamsir M.S., Chong C.S., Bruce N.C., Chan K.G, & Goh K.M. (2019). Characterizing a Halo-Tolerant GH10 Xylanase from Roseithermus sacchariphilus Strain RA and Its CBM-Truncated Variant. International Journal of Molecular Sciences, 20(9), 2284.

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In Vitro Curcumin Release Assay

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In vitro release of curcumin was carried out in 10% w/v aqueous Tween 80 at 37 °C to ensure sink conditions [16 (link),17 (link)]. An aliquot (10 mg) of freeze-dried CU-NS or curcumin powder was added to the donor compartment (1 mL) and separated from the receptor compartment by 10 KDa cellulose membrane (Snakeskin Dialysis Tubing 10K MWCO, ThermoFisher Scientific, Altrincham, Cheshire, UK). The ratio of volumes between the donor and the receptor compartment was kept at ten to ensure sink condition. At each time point, 1 mL was withdrawn from the receptor compartment and replaced by 1 mL fresh 10% w/v Tween 80. Curcumin in the samples was subsequently analysed by high performance liquid chromatography (HPLC).

Abdelghany S., Tekko I.A., Vora L., Larrañeta E., Permana A.D, & Donnelly R.F. (2019). Nanosuspension-Based Dissolving Microneedle Arrays for Intradermal Delivery of Curcumin. Pharmaceutics, 11(7), 308.

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Purification of His-Tagged Proteins

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Frozen pellets were suspended in lysis buffer (50 mM Tris pH 8.0, 200 mM NaCl, 10 mM β-mercaptoethanol, 1 mM PMSF and 2% w/v sarkosyl) and incubated at room temperature for overnight lysis. Cells were subsequently lysed using sonication. Lysates were cleared by centrifugation at 15000 × g for 30 min at 4 °C and incubated in Pierce 5 ml columns with Ni-NTA agarose beads (Qiagen) at 4 °C for 1 h. Lysate was allowed to flow through and beads were washed 10 column volumes of wash buffer (50 mM Tris pH 8.0, 200 mM NaCl, 30 mM imidazole, 10 mM β-mercaptoethanol, 0.05% w/v sarkosyl). His tagged protein was eluted using 300 mM imidazole in 50 mM Tris pH 8.0, 200 mM NaCl, 10 mM β-mercaptoethanol and 0.05% w/v sarkosyl. Elution fractions were tested on 12% SDS-PAGE gel and fractions containing protein were pooled and dialyzed overnight at 4 °C using Snakeskin dialysis tubing 10K MWCO (Thermo Scientific) in kinase storage buffer (20 mM Tris pH 8.0, 125 mM NaCl, 10% glycerol, 1 mM DTT). Dialyzed protein was assessed for purity using 12% SDS-PAGE gel and stored at −80 °C. YegI variant proteins were purified using the same protocol. Proteins were stored at −80 °C.

Rajagopalan K, & Dworkin J. (2020). Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane. FEBS letters, 594(21), 3530-3541.

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Affinity Purification of Recombinant Protein

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Infiltrated leaves were homogenized with 1x PBS (phosphate-buffered saline, pH 7.4) and centrifuged at 18,000 g at 4 °C for 30 min. The supernatant was then filtered through a 0.45 µm membrane filter (Merck, Rahway, New Jersey, USA) before loading into a protein A column which was packed with MabSelectSURE protein A bead (Cytiva, Buckinghamshire, UK). After 10 column volumes of washing with 1x PBS pH 7.4, the recombinant protein was eluted with 0.1 M glycine, pH 2.7, and neutralized with 1.5 M Tris pH 8.0. The neutralized recombinant protein was dialyzed against 1x PBS pH 7.4 overnight with SnakeSkin Dialysis Tubing (10 K MWCO) (ThermoFisher Scientific, MA, USA).

Pisuttinusart N., Shanmugaraj B., Srisaowakarn C., Ketloy C., Prompetchara E., Thitithanyanont A, & Phoolcharoen W. (2023). Immunogenicity of a recombinant plant-produced respiratory syncytial virus F subunit vaccine in mice. Biotechnology Reports, 41, e00826.

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In Vitro Release Testing of TBH Nanospheres

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The in vitro release testing (IVRT) of TBH from the nanosphere suspension and the nanosphere-loaded gels was studied using SnakeSkin Dialysis Tubing, 10K MWCO (Thermo Fisher Scientific, Waltham, MA, USA) sandwiched between the donor and receptor chambers of vertical Franz diffusion cells (Logan Instruments, Somerset, NJ, USA) with a receptor volume of 5 mL and an effective diffusion area of 0.64 cm². The receptor compartment was filled with PBS (pH 7.4) containing 40% (v/v) ethanol to achieve sink conditions and contained a 3 mm magnetic stir bar for constant stirring of receptor media at 600 rpm. The assembled Franz cells were placed in FDC-24 heat blocks (Logan Instruments, Somerset, NJ, USA) set at 37 °C, and were allowed to equilibrate for 15 min before applying the formulations in the donor compartment. All formulations were applied in excess to achieve an infinite dose of TBH. Samples of 300 µL were withdrawn through the sampling arm of the Franz cells at predetermined time points followed by immediate replenishment with the same volume of fresh receptor media. The pre-validated HPLC method was used to determine the drug content of each sample, and cumulative drug contents were plotted against the time to obtain the release profile.

Puri V., Froelich A., Shah P., Pringle S., Chen K, & Michniak-Kohn B. (2022). Quality by Design Guided Development of Polymeric Nanospheres of Terbinafine Hydrochloride for Topical Treatment of Onychomycosis Using a Nano-Gel Formulation. Pharmaceutics, 14(10), 2170.

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Ethanol-Thiourea-Urea Protein Extraction

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Materials. Ethanol, thiourea (≥ 99%) were purchased from Sigma-Aldrich. Methanol and SnakeSkin dialysis tubing (10K MWCO) were obtained from ThermoFisher Scientific. Urea (99.5 -100.5%), 1,4-Dithio-DL-threitol (DTT, ≥ 99%) were purchased from Chem-Impex.

Zhao Z., Moay Z.K., Lai H.Y., Goh B.H.R., Chua H.M., Setyawati M.I, & Ng K.W. (2021). Characterization of Anisotropic Human Hair Keratin Scaffolds Fabricated via Directed Ice Templating. Macromolecular bioscience, 21(2).

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Fluorescent Labeling of HBc Particles

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Purified HBc particles were reacted with Alexa Fluor™ 488 Succinimidyl Esters (Invitrogen Life Technologies, USA) at 40:1 HBc:dye mass ratio in phosphate-buffered saline (PBS) buffer for 1 h at room temperature with stirring. The mixture was then dialysed using SnakeSkin™ Dialysis Tubing, 10K MWCO (Thermo Scientific, USA) against PBS buffer at 4 °C for overnight to remove free Alexa Fluor™ 488. To evaluate the fluorescence labelling efficiency, a standard curve of Alexa Fluor™ 488-labelled WT-HBc, ΔHBc or Z_HER2- ΔHBc was prepared. Fluorescence intensity was measured at 485 nm and 520 nm excitation and emission wavelengths, respectively, at 25 °C using a BMG FLUOstar Omega fluorometer.

Mohamed Suffian I.F., Wang J.T., Hodgins N.O., Klippstein R., Garcia-Maya M., Brown P., Nishimura Y., Heidari H., Bals S., Sosabowski J.K., Ogino C., Kondo A, & Al-Jamal K.T. (2017). Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo. Biomaterials, 120, 126-138.

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Synthesis and Characterization of UPy-based Polymers

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UPy-isocyanate synthon
(1) and elastomeric chain-extended UPy comprising a poly(hexamethylene
carbonate) backbone (UPyE) material^{34 (link)} was
provided by SupraPolix (Eindhoven, NL). 1,1,1,3,3,3-Hexafluoroisopropanol
(HFIP) was purchased from BioSolve. Hydroxyethyl methacrylate (HEMA),
chloroform, diethyl ether, dibutyltin dilaurate (DBTDL), 2-(methacryloyloxy)ethyl
2-(trimethylammonio)ethylphosphate (MPC), 4-cyano-4 (phenylcarbonothioylthio)pentanoic
acid, 4,4′-azobis 4-cyanovaleric acid (ACVA), chloroform-d, methanol-d₄, PBS tablets,
methanol, N,N-dimethylacetamide
(DMAc), and rhodamine 6G were purchased from Sigma-Aldrich. Alexa-Fluor-488-labeled
BSA and SnakeSkin Dialysis Tubing (10k MWCO) were purchased from Thermo
Fisher Scientific. These reagents were used as received and not purified
unless otherwise indicated.

Feliciano A.J., Soares E., Bosman A.W., van Blitterswijk C., Moroni L., LaPointe V.L, & Baker M.B. (2023). Complementary Supramolecular Functionalization Enhances Antifouling Surfaces: A Ureidopyrimidinone-Functionalized Phosphorylcholine Polymer. ACS Biomaterials Science & Engineering, 9(8), 4619-4631.

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Capsid Monomer Dialysis and Disulfide Bond Formation

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One milliliter of monomeric capsid (5 mg/ml) was dialyzed in SnakeSkin dialysis tubing 10K MWCO (Thermo Scientific) using a buffer that is high in salt and contains a reducing agent (buffer 1: 50 mM Tris, pH 8, 1 M NaCl, 100 mM β-mercaptoethanol) at 4°C for 8 h. Subsequently the protein was dialyzed using buffer 1 without the reducing agent β-mercaptoethanol (buffer 2: 50 mM Tris, pH 8, 1 M NaCl) at 4°C for 8 h. The absence of β-mercaptoethanol in the second dialysis allows the formation of disulfide bonds between Cysteine 14 and 45 inter-capsid monomers in the hexamer. Finally, the protein was dialyzed using buffer 3 (20 mM Tris, pH 8,0, 40 mM NaCl) at 4°C for 8 h. Assembled complexes were kept at 4°C for up to 1 month.

Selyutina A., Persaud M., Simons L.M., Bulnes-Ramos A., Buffone C., Martinez-Lopez A., Scoca V., Di Nunzio F., Hiatt J., Marson A., Krogan N.J., Hultquist J.F, & Diaz-Griffero F. (2020). Cyclophilin A Prevents HIV-1 Restriction in Lymphocytes by Blocking Human TRIM5α Binding to the Viral Core. Cell reports, 30(11), 3766-3777.e6.

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