Tris-Glycine Running Buffer 10X (SDS-PAGE)

<strong>Tris-Glycine Running Buffer 10X (SDS-PAGE)_x000D_ </strong>_x000D_ <table width="1028">_x000D_ <tbody>_x000D_ <tr>_x000D_ <td width="285">Catalog number:</td>_x000D_ <td width="743">B2010037</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Lot number:</td>_x000D_ <td>Batch Dependent</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Expiration date:</td>_x000D_ <td>Batch Dependent</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Volume/Weight</td>_x000D_ <td>100 mL</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Provided as</td>_x000D_ <td>10X concentrate (dilute with di-water to 1X before use)</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>pH</td>_x000D_ <td>8.5-8.7</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>CAS Number</td>_x000D_ <td>288-32-4</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Color</td>_x000D_ <td>Colorless</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Shelf-Life</td>_x000D_ <td>2 years from date of manufacture</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Storage:</td>_x000D_ <td>4°C to 25°C</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Keywords:</td>_x000D_ <td>SDS PAGE running buffer, running buffer, tris-glycine running buffer</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Grade</td>_x000D_ <td>Biotechnology grade. All components are highly pure (minimum 99%). All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered on a 0.22 um.</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>References</td>_x000D_ <td width="743">1: Haider SR, Sharp BL, Reid HJ. A comparison of Tris-glycine and Tris-tricine_x000D_ buffers for the electrophoretic separation of major serum proteins. J Sep Sci._x000D_ 2011 Sep;34(18):2463-7.2: Zhang Y, Wang Y, Li Y. Major cause of antibody artifact bands on non-reducing_x000D_ SDS-PAGE and methods for minimizing artifacts. Protein Expr Purif. 2019_x000D_ Dec;164:105459.3: Hachmann JP, Amshey JW. Models of protein modification in Tris-glycine and_x000D_ neutral pH Bis-Tris gels during electrophoresis: effect of gel pH. Anal Biochem._x000D_ 2005 Jul 15;342(2):237-45. doi: 10.1016/j.ab.2005.04.015. PMID: 15935323._x000D_ _x000D_ 4: Litovchick L. Resolving Proteins for Immunoblotting by Gel Electrophoresis._x000D_ Cold Spring Harb Protoc. 2018 Oct 1;2018(10)._x000D_ _x000D_ 5: Ramos Y, Besada V, Castellanos-Serra L. Peptide fractionation by SDS-free_x000D_ polyacrylamide gel electrophoresis for proteomic analysis via DF-PAGE. Methods_x000D_ Mol Biol. 2012;869:197-204._x000D_ _x000D_ 6: Moebius J, Denker K, Sickmann A. Ruthenium (II) tris-bathophenanthroline_x000D_ disulfonate is well suitable for Tris-Glycine PAGE but not for Bis-Tris gels._x000D_ Proteomics. 2007 Feb;7(4):524-527._x000D_ _x000D_ 7: Ladner-Keay CL, Turner RJ, Edwards RA. Fluorescent Protein Visualization_x000D_ Immediately After Gel Electrophoresis Using an In-Gel Trichloroethanol_x000D_ Photoreaction with Tryptophan. Methods Mol Biol. 2018;1853:179-190._x000D_ _x000D_ 8: Jimenez MS, Luque-Alled JM, Gomez T, Castillo JR. Evaluation of agarose gel_x000D_ electrophoresis for characterization of silver nanoparticles in industrial_x000D_ products. Electrophoresis. 2016 May;37(10):1376-83._x000D_ _x000D_ 9: Jiménez MS, Rodriguez L, Bertolin JR, Gomez MT, Castillo JR. Evaluation of_x000D_ gel electrophoresis techniques and laser ablation-inductively coupled plasma-_x000D_ mass spectrometry for screening analysis of Zn and Cu-binding proteins in_x000D_ plankton. Anal Bioanal Chem. 2013 Jan;405(1):359-68._x000D_ _x000D_ 10: Marshall T, Williams KM. Analysis of snake venoms by sodium dodecyl sulfate-_x000D_ polyacrylamide gel electrophoresis and two-dimensional electrophoresis. <a href="https://pubmed.ncbi.nlm.nih.gov/7811763/">Appl</a>_x000D_ Theor Electrophor. 1994;4(1):25-31.</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td>Related Products</td>_x000D_ <td><a href="https://moleculardepot.com/product-category/buffers/">Biochemical Buffers and Solutions</a></td>_x000D_ </tr>_x000D_ </tbody>_x000D_ </table>