Protease from Aspergillus saitoi

<strong>Protease from Aspergillus saitoi</strong>_x000D_ <strong>Catalog number:</strong> B2010521_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1 g_x000D_ <strong>Molecular Weight or Concentration:</strong> ≥0.6 unit/mg solid_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various protease-related research studies_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> Molsin_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: Chiba Y, Midorikawa T, Ichishima E. Cloning and expression of the_x000D_ carboxypeptidase gene from Aspergillus saitoi and determination of the catalytic_x000D_ residues by site-directed mutagenesis. Biochem J. 1995 Jun 1;308 ( Pt 2)(Pt_x000D_ 2):405-9._x000D_ _x000D_ 2: GABELOTEAU C, DESNUELLE P. [On the activation of bovine trypsinogen by a_x000D_ crystallized protease from Aspergillus saitoi]. Biochim Biophys Acta. 1960 Aug_x000D_ 12;42:230-7. French._x000D_ _x000D_ 3: Tanaka N, Takeuchi M, Ichishima E. Purification of an acid proteinase from_x000D_ Aspergillus saitoi and determination of peptide bond specificity. Biochim_x000D_ Biophys Acta. 1977 Dec 8;485(2):406-16._x000D_ _x000D_ 4: Ichishima E, Taya N, Ikeguchi M, Chiba Y, Nakamura M, Kawabata C, Inoue T,_x000D_ Takahashi K, Minetoki T, Ozeki K, Kumagai C, Gomi K, Yoshida T, Nakajima T._x000D_ Molecular and enzymic properties of recombinant 1, 2-alpha-mannosidase from_x000D_ Aspergillus saitoi overexpressed in Aspergillus oryzae cells. Biochem J. 1999_x000D_ May 1;339 ( Pt 3)(Pt 3):589-97._x000D_ _x000D_ 5: Menon V, Rao M. A low-molecular-mass aspartic protease inhibitor from a novel_x000D_ Penicillium sp.: implications in combating fungal infections. Microbiology_x000D_ (Reading). 2012 Jul;158(Pt 7):1897-1907._x000D_ _x000D_ 6: Chiba Y, Yamagata Y, Iijima S, Nakajima T, Ichishima E. The carbohydrate_x000D_ moiety of the acid carboxypeptidase from Aspergillus saitoi. Curr Microbiol._x000D_ 1993 Nov;27(5):281-8._x000D_ _x000D_ 7: Irie M, Watanabe H, Ohgi K, Harada M. Site of alkylation of the major_x000D_ ribonuclease from Aspergillus saitoi with iodoacetate. J Biochem. 1986_x000D_ Mar;99(3):627-33._x000D_ _x000D_ 8: Nishinoaki M, Asakura T, Watanabe T, Kunizaki E, Matsumoto M, Eto W, Tamura_x000D_ T, Minami M, Obata A, Abe K, Funaki J. Application of an Aspergillus saitoi_x000D_ protease preparation to soybean curd to modify its functional and rheological_x000D_ properties. Biosci Biotechnol Biochem. 2008 Feb;72(2):587-90._x000D_ _x000D_ 9: Ohgi K, Watanabe H, Irie M. The effect of elimination of amino acids from the_x000D_ carboxyl-terminal of the minor ribonuclease from Aspergillus saitoi by_x000D_ carboxypeptidase A on the enzymatic activity. Chem Pharm Bull (Tokyo). 1978_x000D_ Feb;26(2):627-30._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/17485851/">10: Fang HL, Lai JJ, Lin WL, Lin WC. A fermented substance from Aspergillus_x000D_ phoenicis reduces liver fibrosis induced by carbon tetrachloride in rats. Biosci_x000D_ Biotechnol Biochem. 2007 May;71(5):1154-61. </a>_x000D_ _x000D_ <strong>Products Related to Protease from Aspergillus saitoi</strong> <a href="https://moleculardepot.com/product-category/Enzymes/">: Enzymes</a>