Spin x centrifuge tube filter

Manufactured by Corning

Sourced in United States

The Spin-X centrifuge tube filters are a laboratory product designed for the separation and filtration of samples. They feature a centrifuge tube with a built-in filter membrane that allows the rapid separation of particulates from liquids during centrifugation.

Automatically generated - may contain errors

Lab products found in correlation

Turbo dnase, by Thermo Fisher Scientific (3 mentions) Microcentrifuge tube, by Eppendorf (2 mentions) Micropipette tips, by Starlab (2 mentions) Qsert clear glass insert lc vials, by Merck Group (2 mentions) Repli g wta single cell kit, by Qiagen (2 mentions) Qiaquick pcr purification kit, by Qiagen (2 mentions) Novaseq platform, by Illumina (2 mentions) Qiaamp minelute virus kit, by Qiagen (2 mentions) Qubit 3, by Thermo Fisher Scientific (2 mentions) Rnase 1, by Promega (2 mentions) Nebnext ultra 2 fs dna library prep kit, by Illumina (2 mentions) Protein g high performance multitrap 96 well plate, by GE Healthcare (2 mentions) Multitrap, by Cytiva (2 mentions) Soc media, by New England Biolabs (2 mentions) Maximum recovery vial, by Waters Corporation (2 mentions) Ti70 rotor, by Beckman Coulter (2 mentions) Anti gapdh antibody, by Abcam (2 mentions) Dnase, by Thermo Fisher Scientific (2 mentions) Edta free protease inhibitor mixture tablet, by Thermo Fisher Scientific (2 mentions) Ultimate 3000, by Thermo Fisher Scientific (2 mentions)

Spelling variants of this product

Spin-X (55 citations) Spin-X filters (25 citations) Centrifuge tubes (25 citations) Spin-X centrifuge tube (11 citations) Spin-X tubes (4 citations) Spin-X™ Centrifuge Tube Filters CA Membrane (2 citations)

72 protocols using spin x centrifuge tube filter

Purification and Fab Generation from Rabbit IgG

Check if the same lab product or an alternative is used in the 5 most similar protocols

To purify polyclonal rabbit IgG, 1 mL of rabbit serum was incubated overnight with 250 μL of protein G agarose beads (ThermoScientific). The next day, IgGs were eluted using 0.1 M glycine, pH 2.5 after which the elution buffer was neutralized with 2 M Tris, pH 8.0. Following concentration and buffer exchange to PBS with Vivaspin filters (10 kDa molecular weight cutoff; GE Healthcare), IgG concentrations were measured using the Nanodrop method. Next, to generate Fabs, purified IgG was incubated, shaking, with immobilized papain resin (ThermoScientific; 100 μL resin/mg of IgG) for 5 h at 37 °C in phosphate buffer saline, 10 mM EDTA, 20 mM cysteine, pH 7.4. After 5 h the resin was removed by spin centrifugation using Spin-X^® centrifuge tube filters (Corning Inc.). The flow-through was then incubated with Protein A agarose resin (ThermoScientific; 200 μL resin/mg of Ig) for 2 h, shaking at RT to remove Fc and non-digested IgGs. After removing the resin by spin centrifugation using Spin-X^® centrifuge tube filters (Corning Inc.), the flow-through was buffer exchanged to PBS and concentrated using Vivaspin filters (10 kDa molecular weight cutoff; GE Healthcare).

Brouwer P.J., Antanasijevic A., de Gast M., Allen J.D., Bijl T.P., Yasmeen A., Ravichandran R., Burger J.A., Ozorowski G., Torres J.L., LaBranche C., Montefiori D.C., Ringe R.P., van Gils M.J., Moore J.P., Klasse P.J., Crispin M., King N.P., Ward A.B, & Sanders R.W. (2021). Immunofocusing and enhancing autologous Tier-2 HIV-1 neutralization by displaying Env trimers on two-component protein nanoparticles. NPJ Vaccines, 6, 24.

+ Open protocol

+ Expand

Characterization of GBS Virulence Factor

Check if the same lab product or an alternative is used in the 5 most similar protocols

GBS clinical isolate COH1 (serotype III) [74 (link)], 515 (serotype Ia) [20 (link)], the recent meningitis isolate 90356 (serotype III) [75 (link)] and their isogenic ΔbspC mutants were used for the experiments. GBS strains were grown in THB (Hardy Diagnostics) at 37°C, and growth was monitored by measuring the optical density at 600 nm (OD₆₀₀). Lactococcus lactis strains were grown in M17 medium (BD Biosciences) supplemented with 0.5% glucose at 30°C. For antibiotic selection, 2 μg/mL chloramphenicol (Sigma) and 5 μg/mL erythromycin (Sigma) were incorporated into the growth medium. BspC and CshA recombinant proteins, and the BspC antibody were purified as described previously [15 (link), 76 (link)]. The anti-BspC polyclonal antibody was further adsorbed (as described in [77 (link)]) against COH1ΔbspC bacteria to remove natural rabbit antibodies that react with bacterial surface antigens. Briefly, anti-BspC antibody was diluted to 2.28 mg/mL in PBS and incubated with COH1ΔbspC bacteria overnight at 4°C, with rotation. Bacteria were pelleted by centrifugation and the supernatant was collected and filtered using 0.22 μM cellulose acetate SpinX centrifuge tube filters (Costar). A normal rabbit IgG antibody (Invitrogen) was adsorbed as described above, and utilized as a negative isotype control.

Deng L., Spencer B.L., Holmes J.A., Mu R., Rego S., Weston T.A., Hu Y., Sanches G.F., Yoon S., Park N., Nagao P.E., Jenkinson H.F., Thornton J.A., Seo K.S., Nobbs A.H, & Doran K.S. (2019). The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis. PLoS Pathogens, 15(6), e1007848.

+ Open protocol

+ Expand

Paramecium Electroporation for Protein Delivery

Check if the same lab product or an alternative is used in the 5 most similar protocols

P. octaurelia culture prepared as above was resuspended in a fresh volume (100 mL) of MSS buffer for 60 min to prevent autofluorescence.¹² After spinning down and another wash cell viability was examined under a binocular microscope. The buffer G in which recombinant proteins were eluted from the affinity gel was exchanged as follows: 0.5 mL of Sephadex G-25 was loaded on the Spin-X centrifuge tube filters (0.45 µm, Costar Corning) and rinsed fivefold with 0.3 mL of MSS buffer followed by 1 min spin (1000 x g). Recombinant protein solution (130 µL) was overlaid on the column and spun for 4 min. Purified recombinant protein in MSS (50 µg in 50 µL) was mixed with 250 µL of Paramecium suspension (64,000 cells) in a 0.4 mm gap cuvette and electroporation was performed in a Gene Pulser II Electroporator (Bio-Rad) at the settings: 60 V, 200 µF, 300 Ω. After electroporation cells were transferred into sterile Eppendorf tubes and gently mixed for 4 h at 27°C (i.e., under the cell cultivation conditions) and next processed for confocal imaging.

Wyroba E., Kwaśniak P., Miller K., Kobyłecki K, & Osińska M. (2016). Site-Directed Mutagenesis, in Vivo Electroporation and Mass Spectrometry in Search for Determinants of the Subcellular Targeting of Rab7b Paralogue in the Model Eukaryote Paramecium Octaurelia. European Journal of Histochemistry : EJH, 60(2), 2612.

+ Open protocol

+ Expand

Purification and Condensation of FUS Protein

Cited 2 times

Check if the same lab product or an alternative is used in the 5 most similar protocols

Protein purification for FUS and RNA Pol II CTD was performed essentially as previously described, with FUS eluted in phosphate-buffered saline (PBS) with 100 mM imidazole.^{4 (link),29 (link)} Dynamic light scattering (DLS) was performed using a Wyatt DynaPro Nanostar. To form condensates, FUS (>10 μM) was incubated in PBS at room temperature for ≤24 h. Condensates were cross-linked with 1% formaldehyde for 20 min and quenched with 1.5 mM glycine. Condensates were removed by filtration using 0.22 μm Costar SpinX centrifuge tube filters.

Thompson V.F., Victor R.A., Morera A.A., Moinpour M., Liu M.N., Kisiel C.C., Pickrel K., Springhower C.E, & Schwartz J.C. (2018). Transcription-Dependent Formation of Nuclear Granules Containing FUS and RNA Pol II. Biochemistry, 57(51), 7021-7032.

+ Open protocol

+ Expand

Ferrlecit Plasma Calibration Curve

Check if the same lab product or an alternative is used in the 5 most similar protocols

For the calibration curve for the DBI, Ferrlecit (Sanofi-Aventis), abbreviated as SFG, spiked into plasma was utilized. Prepared plasma was collected from the University of Maryland Medical Center blood bank and combined to ensure a uniform plasma solution. The plasma solution was separated into conical tubes and stored at −20 °C. Prior to calibration and sample preparation, the plasma was thawed under warm water and thoroughly mixed via vortex. To prepare the DBI calibration curve, a new vial of Ferrlecit was opened, and a calibration curve consisting of 9 points was prepared from serial dilutions of Ferrlecit ranging from 12.5–12 500 ppm with 10 mM Tris. The prepared diluted stocks of SFG (50 μL) were then spiked into the thawed plasma (350 μL). Aliquots (80 μL) of the prepared SFG calibration samples were diluted with 10 mM Tris (320 μL), transferred to Corning Costar Spin-X centrifuge tube filters (cellulose acetate membrane, pore size 0.22 μm), and centrifuged at 14 000g for 5 min. The samples were then transferred to HPLC vials equipped with 200 μL inserts.

Neu H.M., Alexishin S.A., Brandis J.E., Williams A.M., Li W., Sun D., Zheng N., Jiang W., Zimrin A., Fink J.C., Polli J.E., Kane M.A, & Michel S.L. (2019). Snapshots of Iron Speciation: Tracking the Fate of Iron Nanoparticle Drugs via a Liquid Chromatography–Inductively Coupled Plasma–Mass Spectrometric Approach. Molecular pharmaceutics, 16(3), 1272-1281.

+ Open protocol

+ Expand

Quantifying Transferrin Biomarkers in Human Plasma

Check if the same lab product or an alternative is used in the 5 most similar protocols

Crystallized human holo-transferrin (Sigma-Aldrich) was used to prepare a TBI calibration curve to quantify TBI, PBI, and LI in human plasma. A stock solution (stock 1) was prepared by dissolving 0.036 g of holo-transferrin in 10 mL of 10 mM Tris buffer and mixing via vortex. The protein stock was kept on ice. A calibration curve consisting of 11 points was prepared from serial dilutions of stock 1 with 10 mM Tris ranging from 100–5000 ppb. An aliquot (300 μL) of each calibration sample was transferred to Corning Costar Spin-X centrifuge tube filters (cellulose acetate membrane, pore size 0.22 μm) and then centrifuged at 14 000g for 5 min. The samples were then transferred to HPLC vials equipped with 200 μL inserts. To prepare the 100 ppb holo-transferrin internal standard solution, 1 mL of stock 1 was diluted with 49 mL of 10 mM Tris.

+ Open protocol

+ Expand

Amino Acid Quantification in Cells

Check if the same lab product or an alternative is used in the 5 most similar protocols

The serum (100 μL) collected from mice was diluted twice with 10% trichloroacetic acid and centrifuged at 9730×g for 15 min. The supernatants were collected and processed in 0.22 μM SPIN-X Centrifuge Tube Filters (Corning Costar) and used for the analyses. CT26 mock control cells and Arg1 OE cells (5 × 10⁶) were cultured in 100-mm cell culture dishes for 24 h. After washing with PBS, the cells were collected and centrifuged at 2430×g for 5 min. Methanol (1 mL) was added to the cell pellets and incubated at room temperature for 10 min, and then H₂O (0.5 mL) and chloroform were further added before centrifugation at 21,880×g for 15 min. The supernatants were collected and processed with 10-kDa centrifugal filter units (Millipore) and used for analysis. The prepared samples were analyzed with an amino acid analyzer (L-8900; Hitachi High-Technologies Corporation, Tokyo, Japan) in the Global Facility Center at Hokkaido University.

Wang X., Xiang H., Toyoshima Y., Shen W., Shichi S., Nakamoto H., Kimura S., Sugiyama K., Homma S., Miyagi Y., Taketomi A, & Kitamura H. (2023). Arginase-1 inhibition reduces migration ability and metastatic colonization of colon cancer cells. Cancer & Metabolism, 11, 1.

+ Open protocol

+ Expand

KSHV Tiling Library Construction

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

A KSHV tiling library was designed using custom python scripts. Each NGG PAM was identified in the reference genome [33 (link)] (S1 and S3 Data) along with the corresponding 19 bp guide. Only one copy of sgRNAs that targeted the KSHV genome more than once was included. The library was cloned using a modified protocol from Deans et al 2016[48 (link)]. sgRNAs were synthesized along with primer binding sites and BstXI/BlpI restriction sites using Twist Biosciences. The library was amplified using corresponding primers for 10 cycles. Amplified library was PCR purified (Qiagen MinElute) and restricted using BstXI and BlpI. 34 bp fragment was purified in water using a native 20% PAGE gel and Spin-X centrifuge tube filters (Costar). Fragment was isoproponal precipitated and ligated into a sgRNA expression plasmid (Addgene #89359) using T4 ligase overnight at 16 degrees and electroporated into Lucigen Endura cells (1800V, 600 ohm, 10μF, 1mm) before plating on 4 assay plates (reduced 75% CARB). Colonies were grown at 37 degrees C overnight, pooled, and maxi prepped (Macherey-Nagel).

Morgens D.W., Nandakumar D., Didychuk A.L., Yang K.J, & Glaunsinger B.A. (2022). A Two-tiered functional screen identifies herpesviral transcriptional modifiers and their essential domains. PLoS Pathogens, 18(1), e1010236.

+ Open protocol

+ Expand

Quantification of Azadirachtin and Derivatives in M. azedarach

Check if the same lab product or an alternative is used in the 5 most similar protocols

Freeze-dried M. azedarach material was weighed (∼10 mg) and homogenized using tungsten carbide beads (3 mm; Qiagen) with a TissueLyser (1,000 rpm, 1 min). Samples were extracted in 550 µL 100% methanol (10 µg/mL podophyllotoxin internal standard, Sigma-Aldrich) and agitated at 18 °C for 20 min. Supernatant (400 µL) was transferred and mixed with 140 µL ddH₂O. Defatting was performed by addition of hexane (400 µL) and removal of the upper phase (300 µL) in duplicate. Remaining solvent was evaporated to dryness and extracts were resuspended in 100 µL of methanol. Spin-X centrifuge tube filters (pore size 0.22 µm, Corning Costar) were used to filter extracts by centrifugation. Eluate (50 µL) was diluted in 50 µL of methanol and transferred to a glass insert placed inside a glass autosampler vial for LC-MS analysis (SI Appendix). LCMSsolutions V3 (Shimadzu) was utilized to analyze chromatograms and for peak identification. The internal standard (podophyllotoxin) was used to calculate an estimated concentration of target compound in starting material. Azadirachtin (Sigma-Aldrich), salannin (Greyhound Chromatography), and melianol (4) (SI Appendix) standards were used to confirm retention times and mass adducts.

Hodgson H., De La Peña R., Stephenson M.J., Thimmappa R., Vincent J.L., Sattely E.S, & Osbourn A. (2019). Identification of key enzymes responsible for protolimonoid biosynthesis in plants: Opening the door to azadirachtin production. Proceedings of the National Academy of Sciences of the United States of America, 116(34), 17096-17104.

+ Open protocol

+ Expand

Measuring Fatty Acid β-Oxidation

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cells were labeled with 20 μCi/mL [9,10-³H]-palmitic acid (Perkin Elmer NET043) for 8 hrs at 37 °C. Tracer was removed by washing cells three times in PBS, and cells were serum starved in unlabeled medium for 16 hrs. For longer-term treatment, inhibitors were added for the entire 16-hr duration of the chase period. For shorter-term treatment, following the chase period, cells were pretreated for 1 hr with DGAT1 and 2 inhibitors or etomoxir prior to addition of torin1 for the indicated durations. Medium was refreshed for the final hour of the experiment to quantify production of ³H₂O, indicative of fatty acid β-oxidation. Medium was pelleted for 10 min at maximum speed at room temperature, and 350 μL were applied to 350 mg 1x8 Dowex Chloride Resin (Sigma 44340) that had been prewashed with water and dispensed into Spin-X Centrifuge Tube Filters (Costar). Tubes were centrifuged 3 min at 4000 x g at room temperature. ³H₂O in the flow through was quantified using Emulsifier Safe scintillation cocktail on a Hidex 300 SL counter. Cells were lysed in NP-40 lysis buffer and protein was quantified to normalize ³H₂O produced.

Hosios A.M., Wilkinson M., McNamara M.C., Kalafut K.C., Torrence M.E., Asara J.M, & Manning B.D. (2022). mTORC1 regulates a lysosome-dependent adaptive shift in intracellular lipid species. Nature metabolism, 4(12), 1792-1811.

+ Open protocol

+ Expand

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?

Revolutionizing how scientists
search and build protocols!