Glycosynthase from Mucor hiemalis

<strong>Glycosynthase from Mucor hiemalis</strong>_x000D_ <strong>Catalog number:</strong> B2011050_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 U_x000D_ <strong>Molecular Weight or Concentration:</strong> na_x000D_ <strong>Supplied as:</strong> Lyophilized powder_x000D_ <strong>Applications:</strong> molecular tool for various chemical, biochemical and immunological applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> Endo-M_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: Umekawa M, Li C, Higashiyama T, Huang W, Ashida H, Yamamoto K, Wang LX. Efficient glycosynthase mutant derived from Mucor hiemalis endo-beta-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan J Biol Chem. 2010 Jan 1;285(1):511-21._x000D_ 2: Umekawa M, Huang W, Li B, Fujita K, Ashida H, Wang LX, Yamamoto K. Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities J Biol Chem. 2008 Feb 22;283(8):4469-79._x000D_ 3: Katoh T, Katayama T, Tomabechi Y, Nishikawa Y, Kumada J, Matsuzaki Y, Yamamoto K. Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans J Biol Chem. 2016 Oct 28;291(44):23305-23317._x000D_ 4: Umekawa M, Higashiyama T, Koga Y, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Huang W, Wang LX, Ashida H, Yamamoto K. Efficient transfer of sialo-oligosaccharide onto proteins by combined use of a glycosynthase-like mutant of Mucor hiemalis endoglycosidase and synthetic sialo-complex-type sugar oxazoline Biochim Biophys Acta. 2010 Nov;1800(11):1203-9._x000D_ 5: Haneda K, Oishi T, Kimura H, Inazu T. Development of a microbioreactor for glycoconjugate synthesis Bioorg Med Chem. 2018 May 1;26(8):2092-2098._x000D_ 6: Ashida H, Fujimoto T, Kurihara S, Nakamura M, Komeno M, Huang Y, Katayama T, Kinoshita T, Takegawa K. 1,6-α-L-Fucosidases from Bifidobacterium longum subsp. infantis ATCC 15697 Involved in the Degradation of Core-fucosylated N -Glycan J Appl Glycosci (1999). 2020 Feb 20;67(1):23-29._x000D_ 7: Sakaguchi K, Katoh T, Yamamoto K. Transglycosidase-like activity of Mucor hiemalis endoglycosidase mutants enabling the synthesis of glycoconjugates using a natural glycan donor Biotechnol Appl Biochem. 2016 Nov;63(6):812-819._x000D_ 8: Higashiyama T, Umekawa M, Nagao M, Katoh T, Ashida H, Yamamoto K. Chemo-enzymatic synthesis of the glucagon containing N-linked oligosaccharide and its characterization Carbohydr Res. 2018 Jan 2;455:92-96._x000D_ 9: Hojo H, Tanaka H, Hagiwara M, Asahina Y, Ueki A, Katayama H, Nakahara Y, Yoneshige A, Matsuda J, Ito Y, Nakahara Y. Chemoenzymatic synthesis of hydrophobic glycoprotein: synthesis of saposin C carrying complex-type carbohydrate J Org Chem. 2012 Nov 2;77(21):9437-46._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/19199609">10: Huang W, Li C, Li B, Umekawa M, Yamamoto K, Zhang X, Wang LX. Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans J Am Chem Soc. 2009 Feb 18;131(6):2214-23. </a>_x000D_ _x000D_ <strong>Products Related to Glycosynthase from Mucor hiemalis can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>