Alpha 1,3 Mannosidase

<strong>Alpha 1,3 Mannosidase</strong>_x000D_ <strong>Catalog number:</strong> B2019376_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1,000 units_x000D_ <strong>Molecular Weight or Concentration:</strong> N/A_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> RT_x000D_ <strong>Keywords:</strong> Alpha 1,3 Mannosidase_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: Ashraf U, Ding Z, Deng S, Ye J, Cao S, Chen Z. Pathogenicity and virulence of Japanese encephalitis virus: Neuroinflammation and neuronal cell damage Virulence. 2021 Dec;12(1):968-980._x000D_ 2: Shen D, Lu X, Li W, Zou L, Tong Y, Wang L, Rao L, Zhang Y, Hou L, Sun G, Chen L. Identification and characterization of an α-1,3 mannosidase from Elizabethkingia meningoseptica and its potential attenuation impact on allergy associated with cross-reactive carbohydrate determinant Biochem Biophys Res Commun. 2023 Sep 10;672:17-26._x000D_ 3: Selinger M, Věchtová P, Tykalová H, Ošlejšková P, Rumlová M, Štěrba J, Grubhoffer L. Integrative RNA profiling of TBEV-infected neurons and astrocytes reveals potential pathogenic effectors Comput Struct Biotechnol J. 2022 May 30;20:2759-2777._x000D_ 4: Kołaczkowski BM, Moroz OV, Blagova E, Davies GJ, Møller MS, Meyer AS, Westh P, Jensen K, Wilson KS, Krogh KBRM. Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis Acta Crystallogr D Struct Biol. 2023 May 1;79(Pt 5):387-400._x000D_ 5: Kóňa J, Šesták S, Wilson IBH, Poláková M. 1,4-Dideoxy-1,4-imino-D- and L-lyxitol-based inhibitors bind to Golgi α-mannosidase II in different protonation forms Org Biomol Chem. 2022 Nov 23;20(45):8932-8943._x000D_ 6: Lu D, Zhu S, Sobala LF, Bernardo-Seisdedos G, Millet O, Zhang Y, Jiménez-Barbero J, Davies GJ, Sollogoub M. From 1,4-Disaccharide to 1,3-Glycosyl Carbasugar: Synthesis of a Bespoke Inhibitor of Family GH99 Endo-α-mannosidase Org Lett. 2018 Dec 7;20(23):7488-7492._x000D_ 7: Bonay P, Roth J, Hughes RC. Subcellular distribution in rat liver of a novel broad-specificity (alpha 1----2, alpha 1----3 and alpha 1----6) mannosidase active on oligomannose glycans Eur J Biochem. 1992 Apr 1;205(1):399-407._x000D_ 8: Gomathinayagam S, Mitchell T, Zartler ER, Heiss C, Azadi P, Zha D, Houston-Cummings NR, Jiang Y, Li F, Giaccone E, Porambo RJ, Anderson CL, Sethuraman N, Li H, Stadheim TA. Structural elucidation of an α-1,2-mannosidase resistant oligosaccharide produced in Pichia pastoris Glycobiology. 2011 Dec;21(12):1606-15._x000D_ 9: Daniel PF, Evans JE, De Gasperi R, Winchester B, Warren CD. A human lysosomal alpha(1----6)-mannosidase active on the branched trimannosyl core of complex glycans Glycobiology. 1992 Aug;2(4):327-36._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/20301507">10: Sparks SE, Krasnewich DM. Congenital Disorders of N-Linked Glycosylation and Multiple Pathway Overview 2005 Aug 15 [updated 2017 Jan 12]. In: Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE, Amemiya A, editors. GeneReviews(®) [Internet]. Seattle (WA): University of Washington, Seattle; 1993–2024.</a>_x000D_ _x000D_ <strong>Products Related to Alpha 1,3 Mannosidase can be found at</strong> <a href="https://moleculardepot.com/product-category/Chemicals/"> Chemicals</a>