Catalase from Micrococcus lysodeikticus

<strong>Catalase from Micrococcus lysodeikticus</strong>_x000D_ <strong>Catalog number:</strong> B2016583_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 50 mL_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> 2-8°C_x000D_ <strong>Keywords:</strong> Catalase from Micrococcus lysodeikticus_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: Kimoto H, Yoshimune K, Matsuyma H, Yumoto I. Characterization of catalase from psychrotolerant Psychrobacter piscatorii T-3 exhibiting high catalase activity Int J Mol Sci. 2012;13(2):1733-1746._x000D_ 2: Murshudov GN, Melik-Adamyan WR, Grebenko AI, Barynin VV, Vagin AA, Vainshtein BK, Dauter Z, Wilson KS. Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 A resolution FEBS Lett. 1992 Nov 9;312(2-3):127-31._x000D_ 3: Shi X, Qiu S, Ji L, Lu H, Wu S, Chen Q, Zou X, Hu Q, Feng T, Chen S, Cui W, Xu S, Jiang M, Cai R, Geng Y, Bai Q, Huang D, Liu P. Pathogenetic characterization of a Micrococcus luteus strain isolated from an infant Front Pediatr. 2023 Dec 22;11:1303040._x000D_ 4: FEW AV, FRASER MJ, GILBY AR. The intracellular catalase of Micrococcus lysodeikticus Biochim Biophys Acta. 1957 May;24(2):306-14._x000D_ 5: Benecky MJ, Frew JE, Scowen N, Jones P, Hoffman BM. EPR and ENDOR detection of compound I from Micrococcus lysodeikticus catalase Biochemistry. 1993 Nov 9;32(44):11929-33._x000D_ 6: Yumoto I, Ichihashi D, Iwata H, Istokovics A, Ichise N, Matsuyama H, Okuyama H, Kawasaki K. Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity J Bacteriol. 2000 Apr;182(7):1903-9._x000D_ 7: Fox RH. Differentiation of Micrococcus luteus and Micrococcus varians on the basis of catalase isoenzymes J Gen Microbiol. 1976 Apr;93(2):272-7._x000D_ 8: Chen D, Li J, Jiao F, Wang Q, Li J, Pei Y, Zhao M, Song X, Guo X. ZmACY-1 Antagonistically Regulates Growth and Stress Responses in Nicotiana benthamiana Front Plant Sci. 2021 Jul 23;12:593001._x000D_ 9: Murshudov GN, Grebenko AI, Brannigan JA, Antson AA, Barynin VV, Dodson GG, Dauter Z, Wilson KS, Melik-Adamyan WR. The structures of Micrococcus lysodeikticus catalase, its ferryl intermediate (compound II) and NADPH complex Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1972-82._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/17198371">10: Hara I, Ichise N, Kojima K, Kondo H, Ohgiya S, Matsuyama H, Yumoto I. Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates Biochemistry. 2007 Jan 9;46(1):11-22. </a>_x000D_ _x000D_ <strong>Products Related to Catalase from Micrococcus lysodeikticus can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>