Tsk gel g2000 swxl column

Manufactured by Tosoh

Sourced in Japan, United States

The TSK gel G2000 SWXL column is a size exclusion chromatography column designed for the separation and analysis of molecules based on their size and molecular weight. It is suitable for the analysis of a wide range of biomolecules, including proteins, peptides, and other macromolecules.

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Lab products found in correlation

Bacitracin, by Merck Group (3 mentions) Aprotinin, by Merck Group (3 mentions) Hplc system, by Shimadzu (3 mentions) E2695 hplc system, by Tosoh (2 mentions) Tskgel swxl guard column, by Tosoh (2 mentions) Irdye 700dx nhs ester, by LI COR (2 mentions) Amicon ultra centrifugal filter unit, by Merck Group (2 mentions) Lc 15c, by Shimadzu (2 mentions) Bis tris gel, by Thermo Fisher Scientific (1 mentions) Silverxpress silver staining kit, by Thermo Fisher Scientific (1 mentions) Agilent 1260 hplc system, by Agilent Technologies (1 mentions) Carbon film coated 400 mesh copper grid, by Electron Microscopy Sciences (1 mentions) Beckman system gold hplc, by Beckman Coulter (1 mentions) Waters 2695 hplc system, by Waters Corporation (1 mentions) Ir700dye nhs ester, by Merck Group (1 mentions) High performance liquid chromatography (hplc), by Shimadzu (1 mentions) Tripeptide ggg, by Merck Group (1 mentions) Tetrapeptide ggyr, by Merck Group (1 mentions) Cytochrome c, by Merck Group (1 mentions) Apd m20a, by Shimadzu (1 mentions)

Spelling variants of this product

TSK gel G2000 SWXL analytical column (2 citations)

29 protocols using tsk gel g2000 swxl column

PhaC Enzyme Purification and Characterization

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The reaction mixture consisting of PhaC, 3HB-CoA, and
100 mM sodium phosphate (pH 7.5) in a total volume of 10 μL
was incubated for 15 min at 25 °C. For TCEP treatment, the reaction
mixtures were incubated for 60 min at 37 °C in the presence of
10 mM TCEP. The reaction mixtures were then loaded onto a TSKgel G2000
SWXL column (TOSOH, Tokyo, Japan) equilibrated with 20 mM NaPi (pH
7.0) containing 200 mM Na₂SO₄ at 25 °C.
The reaction mixture containing PhaC was eluted with the same buffer
at a flow rate of 1 mL/min at 25 °C. The molecular weight was
determined from the calibration curve prepared using the following
molecular weight standards: alcohol dehydrogenase (150 kDa, 7.7 min),
BSA (66 kDa, 8.4 min), ovalbumin (44 kDa, 9.1 min), C2 (16 kDa, 10.9
min), and aprotinin (6.5 kDa, 11.8 min).
Native PAGE was carried
out using precast gradient (4–12%) Bis-Tris gels (Invitrogen,
Carlsbad, CA), according to standard protocols. The gels were visualized
by silver staining using a SilverXpress Silver Staining Kit (Invitrogen,
Carlsbad, CA).

Higuchi-Takeuchi M., Motoda Y., Kigawa T, & Numata K. (2017). Class I Polyhydroxyalkanoate Synthase from the Purple Photosynthetic Bacterium Rhodovulum sulfidophilum Predominantly Exists as a Functional Dimer in the Absence of a Substrate. ACS Omega, 2(8), 5071-5078.

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Molecular Weight Analysis of TPA

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The experimental method is based on Wan et al. (2020) (link). The concentration of the sample solution was 20 mg/mL. The molecular weight distribution of TPA was determined by Gel Permeation Chromatography (GPC) methods in Agilent 1260 HPLC system with the following conditions: TSKgel G2000SWXL column (300 mm × 7.8 mm, Tosoh Corporation, Japan); Mobile phase: 0.1% TFA-acetonitrile: 0.1% TFA-water = 20:80 (v/v), monitoring wavelength 220 nm, flow rate 0.5 mL/min, column temperature 35 °C, injection volume 5 μL. Cytochrome C (M:12355), aprotinin (M:6511), bacitracin (M:1422), L-oxidized glutathione (M:612.63) and phenylalanine (M:165.2) were used as relative molecular mass standards. The standard curve of log of molecular weight (logMw) and elution time (t) of the standard was logMw = −0.0144t2+0.2552t+3.1123 (R² = 0.9991).

Zhao X., Cai B., Chen H., Wan P., Chen D., Ye Z., Duan A., Chen X., Sun H, & Pan J. (2023). Tuna trimmings (Thunnas albacares) hydrolysate alleviates immune stress and intestinal mucosal injury during chemotherapy on mice and identification of potentially active peptides. Current Research in Food Science, 7, 100547.

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Characterization of ND-MPLA/CpG Nanocarriers

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The loading efficiency of MPLA in ND-MPLA was measured by HPLC equipped with an evaporative light scattering detector (ELSD) as described before [34 (link)]. The loading efficiency of CpG was measured by gel permeation chromatography (GPC), as we reported previously [33 (link)]. Briefly, ND samples were injected in a Shimadzu HPLC system equipped with a TSKgel G2000SWxl column (7.8mm ID×30 cm, Tosoh Bioscience LLC), and the amount of CpG was quantified with the detection wavelength set at 280 nm. The particle size of ND-MPLA/CpG was measured by dynamic light scattering (DLS) on a Malvern Zetasizer (Westborough, MA). The ND morphology was assessed by transmission electron microscopy (TEM). Properly diluted ND sample solution was deposited on a carbon film-coated 400 mesh copper grid (Electron Microscopy Sciences) and dried for 1min. The ND samples were then negatively stained with 1% (w/v) uranyl formate, and the grid was dried before TEM observation. All specimens were imaged on a 100 kV Morgagni TEM equipped with a Gatan Orius CCD.

Kuai R., Sun X., Yuan W., Ochyl L.J., Xu Y., Najafabadi A.H., Scheetz L., Yu M.Z., Balwani I., Schwendeman A, & Moon J.J. (2018). Dual TLR agonist nanodiscs as a strong adjuvant system for vaccines and immunotherapy. Journal of controlled release : official journal of the Controlled Release Society, 282, 131-139.

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Quantifying Soluble Protein Aggregates

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Size exclusion HPLC (SE-HPLC) was conducted with a Beckman Gold HPLC system (Beckman Coulter, Fullertown California) to detect soluble aggregates of rhIL-1ra. Samples were centrifuged at 15,000 g (4 °C) for 20 minutes prior to injecting 50 μl of sample into a TSK_gel G2000SW_xl column (Tosoh Biosciences, Montgomeryville Pennsylvania). Eluent was monitored at 280 nm using a System Gold 168 detector while operating at a flow rate of 0.6 ml/min with a mobile phase consisting of 10 mM sodium citrate with 140 mM sodium chloride (pH 6.5).

Snell J.R., Zhou C., Carpenter J.F, & Randolph T.W. (2016). Particle Formation and Aggregation of a Therapeutic Protein in Nanobubble Suspensions. Journal of pharmaceutical sciences, 105(10), 3057-3063.

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Determining Molecular Weight Distribution

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The molecular weight (MW) distribution of SPH-FD and SPH-SD was determination by size exclusion chromatography using a Waters e2695 HPLC system equipped with a TSK-gel G2000 SW_XL column (7.8 mm × 300 mm, Tosoh, Tokyo, Japan). The chromatographic conditions were as follows: the eluent was 45% acetonitrile/55% water/0.1% trifluoroacetic acid, the flow rate was 0.5 mL/min, and the UV detector was monitored at 220 nm. HHL (429 Da), bacitracin (1422 Da), aprotinin (6.5 kDa), and cytochrome C (12.4 kDa) were used as standards to obtain the MW calibration curve: lg (M) = −0.2008t + 6.8668, R² = 0.9761.

Dong Y., Yan W, & Zhang Y.Q. (2022). Effects of Spray Drying and Freeze Drying on Physicochemical Properties, Antioxidant and ACE Inhibitory Activities of Bighead Carp (Aristichthys nobilis) Skin Hydrolysates. Foods, 11(14), 2083.

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Molecular Weight Distribution Analysis

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The molecular weight distribution of the hydrolysates was characterized by a Waters 2695 HPLC system fitted with a TSK-Gel G2000 SW_XL column (7.8 mm × 300 mm, Tosoh, Tokyo, Japan) and a TSK-Gel SW_XL guard column (6.0 mm × 40 mm, Tosoh, Tokyo, Japan). The supernatant (20 μL) was loaded onto the column after filtering with a 0.45 μm membrane filter. The elution was carried out using 45% (v/v) acetonitrile containing 0.1% (v/v) trifluoroacetic acid (TFA) at 0.5 mL/min and its absorbance was monitored at 220 nm. A molecular weight calibration curve (lg(M) = −0.219t + 7.192, R² = 0.996) was obtained using a set of standards from Sigma-Aldrich: HHL (429 Da), bacitracin (1,422.69 Da), aprotinin (6,511.4 Da), cytochrome C (12,500 Da) and carbonic anhydrase (29,000 Da).

Zhang Y., Tu D., Shen Q, & Dai Z. (2019). Fish Scale Valorization by Hydrothermal Pretreatment Followed by Enzymatic Hydrolysis for Gelatin Hydrolysate Production. Molecules, 24(16), 2998.

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Preparation of IR700-Conjugated Anti-CEA Antibody

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A water-soluble silicon-phthalocyanine derivative, IRDye 700DX NHS ester, was obtained from LI-COR Bioscience (Lincoln, NE). 2 mg (~ 14 nmol) of chimeric anti-CEA antibody (Genara Biosciences LLC, Morgan Hill, CA) at a concentration of 2 mg/ml in 0.1 M Na₂HPO₄ (pH= 8.6) was incubated for 2 hours at room temperature with IR700dye NHS ester (135 ug, 70 nmol) prepared in anhydrous DMSO at 5 mmol/L. After the incubation period, the IR700-conjugate was buffer exchanged and purified with phosphate buffer saline (PBS, pH= 7.1) using Amicon Ultra Centrifugal Filter Units (EMD Millipore Corporation, Billerica, MA). The IR700-mAb conjugate was repeatedly diluted with 10 ml volumes of PBS and then concentrated using the filter units until less than 2 % of the unconjugated IR700 dye species remained, as determined by size exclusion HPLC (SE-HPLC). Analysis of the conjugates by SE-HPLC was performed using an Agilent 1100 HPLC system fitted with a TSKgel G2000SWxl column (Tosoh Biosciences, Tokyo, Japan). The SE-HPLC elution buffer was 1X PBS (pH =7.1) with a flow rate of 1 ml/min. UV/Vis detection at 280 nm and 690 nm was used to determine the average dye-to-antibody ratio (DAR) for each conjugates. With this sample, a purity of 97.6% with 0.5% free dye and a DAR of 4.1 was achieved.

Maawy A.A., Hiroshima Y., Zhang Y., Garcia-Guzman M., Luiken G.A., Kobayashi H., Hoffman R.M, & Bouvet M. (2015). Photoimmunotherapy lowers recurrence after pancreatic cancer surgery in orthotopic nude mouse models. The Journal of surgical research, 197(1), 5-11.

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Collagen Hydrolysate Molecular Weight Analysis

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The molecular weight distribution of collagen hydrolysate was analyzed by high-performance liquid chromatography (HPLC, Shimadzu, Kyoto, Japan) equipped with a TSK gel G2000 SW_XL column (7.8 × 300 mm, Tosoh, Tokyo, Japan) according to the method previously described [63 (link)]. The mobile phase used was 45% acetonitrile containing 0.1% (v/v) trifuoroacetic acid. HPLC was performed at a flow rate of 0.5 mL/min and monitored at 220 nm at 30 °C. The molecular weight distribution was calibrated with five molecular mass markers: cytochrome C (Mr 12500), aprotinin (Mr 6500), bacitracin (Mr 1450), tetrapeptide GGYR (Mr 451) and tripeptide GGG (Mr 189). The area of sample chromatograph was integrated at different ranges (<1000 Da, 1000–3000 Da, 3000–5000 Da, 5000–10,000 Da and >10,000 Da). The proportion of each range of peptides in the hydrolysate were expressed as the percentage of area of corresponding molecular weight range to the total chromatograph area.

Cheng J.H., Zhang X.Y., Wang Z., Zhang X., Liu S.C., Song X.Y., Zhang Y.Z., Ding J.M., Chen X.L, & Xu F. (2021). Potential of Thermolysin-like Protease A69 in Preparation of Bovine Collagen Peptides with Moisture-Retention Ability and Antioxidative Activity. Marine Drugs, 19(12), 676.

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Peptide Molecular Weight Analysis by HPLC

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The molecular weight (MW) distribution of peptides was examined on a Waters e2695 HPLC system equipped with a TSKgel G2000 SW_XL column (7.8 mm × 300 mm, Tosoh, Tokyo, Japan) and a TSKgel SW_XL guard column (6.0 mm × 40 mm, Tosoh, Tokyo, Japan). The chromatographic conditions were as follows, according to Zhang et al. [17 (link)]: the eluent was 45% acetonitrile containing 0.1% (v/v) trifluoroacetic acid (TFA), the flow rate was 0.5 mL/min, the injection volume was 10 μL and the absorbance was monitored at 220 nm. The standards used for the molecular weight calibration were as follows: HHL (429 Da), bacitracin (1422 Da), aprotinin (6.5 kDa) and cytochrome C (12.4 kDa).

Dong Y., Yan W., Zhang X.D., Dai Z.Y, & Zhang Y.Q. (2021). Steam Explosion-Assisted Extraction of Protein from Fish Backbones and Effect of Enzymatic Hydrolysis on the Extracts. Foods, 10(8), 1942.

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HPLC Analysis of Molecular Weights

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An LC-20A high-performance liquid chromatography (HPLC) system (Shumadzu, Kyoto, Japan) configured with a TSK gel G2000 SWXL column (300 mm × 7.8 mm, Tosoh, Tokyo, Japan) was used to assess molecular weight distribution. Acetonitrile/water (45:55, v/v) with 0.1% (v/v) trifluoroacetic acid acted as the mobile phase. The elution of samples was performed at a flow rate of 0.5 mL/min and monitored at 220 nm and 30 °C. Molecular weight standards were subjected to tripeptide GGG (MW 189), tetrapeptide GGYR (MW 451), bacitracin (MW 1450), aprotinin (MW 6500), and cytochrome C (MW 12,500) (Sigma Chemical Co., St. Louis, USA).

Liu W.Y., Zhang J.T., Miyakawa T., Li G.M., Gu R.Z, & Tanokura M. (2021). Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten. Scientific Reports, 11, 5206.

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