Endoglycoceramidase II from Rhodococcus sp.

<strong>Endoglycoceramidase II from Rhodococcus sp.</strong>_x000D_ <strong>Catalog number:</strong> B2013025_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 MU_x000D_ <strong>Molecular Weight or Concentration:</strong> 58.9 kDa_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> EGCase, ceramide glycanase, glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase, oligoglycosylglucosyl(1↔1)ceramide glycohydrolase, oligoglycosylglucosylceramide glycohydrolase_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Ito M, Yamagata T. Purification and characterization of glycosphingolipid-specific endoglycosidases (endoglycoceramidases) from a mutant strain of Rhodococcus sp. Evidence for three molecular species of endoglycoceramidase with different specificities J Biol Chem. 1989 Jun 5;264(16):9510-9._x000D_ 2: Izu H, Izumi Y, Kurome Y, Sano M, Kondo A, Kato I, Ito M. Molecular cloning, expression, and sequence analysis of the endoglycoceramidase II gene from Rhodococcus species strain M-777 J Biol Chem. 1997 Aug 8;272(32):19846-50._x000D_ 3: Sakaguchi K, Okino N, Sueyoshi N, Izu H, Ito M. Cloning and expression of gene encoding a novel endoglycoceramidase of Rhodococcus sp. strain C9 J Biochem. 2000 Jul;128(1):145-52._x000D_ 4: Ishida J, Hinou H, Naruchi K, Nishimura S. Synthesis of neoglycosphingolipid from methoxyamino-functionalized ceramide Bioorg Med Chem Lett. 2014 Feb 15;24(4):1197-200._x000D_ 5: Ben Bdira F, Jiang J, Kallemeijn W, de Haan A, Florea BI, Bleijlevens B, Boot R, Overkleeft HS, Aerts JM, Ubbink M. Hydrophobic Interactions Contribute to Conformational Stabilization of Endoglycoceramidase II by Mechanism-Based Probes Biochemistry. 2016 Aug 30;55(34):4823-35._x000D_ 6: Han YB, Chen LQ, Li Z, Tan YM, Feng Y, Yang GY. Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases J Biol Chem. 2017 Mar 24;292(12):4789-4800._x000D_ 7: Ito M, Ikegami Y, Omori A, Yamagata T. Conversion of endoglycoceramidase-activator II by trypsin to the 27.9 kDa polypeptide possessing full activity: purification of activator for endoglycoceramidase by trypsin treatment followed by trypsin-inhibitor agarose column application J Biochem. 1991 Sep;110(3):328-32._x000D_ 8: Ishibashi Y, Kobayashi U, Hijikata A, Sakaguchi K, Goda HM, Tamura T, Okino N, Ito M. Preparation and characterization of EGCase I, applicable to the comprehensive analysis of GSLs, using a rhodococcal expression system J Lipid Res. 2012 Oct;53(10):2242-2251._x000D_ 9: Karlsson H, Halim A, Teneberg S. Differentiation of glycosphingolipid-derived glycan structural isomers by liquid chromatography/mass spectrometry Glycobiology. 2010 Sep;20(9):1103-16._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/1850427">10: Ito M, Ikegami Y, Yamagata T. Activator proteins for glycosphingolipid hydrolysis by endoglycoceramidases. Elucidation of biological functions of cell-surface glycosphingolipids in situ by endoglycoceramidases made possible using these activator proteins J Biol Chem. 1991 Apr 25;266(12):7919-26.</a>_x000D_ _x000D_ <strong>Products Related to Endoglycoceramidase II from Rhodococcus sp. can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>