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69066 Recombinant Enterokinase

69066
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      Plastic ampoule 50 u
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      Description
      OverviewRecombinant Enterokinase (rEK) is a highly purified preparation of the catalytic subunit of bovine enterokinase, a serine protease which recognizes the identical cleavage site as the native enzyme (AspAspAspAspLys↓) and has similar enzymatic activity. This enzyme is produced in E. coli and purified to yield the highest activity available, and is qualified for specific cleavage of appropriate fusion proteins. Supplied as a solution in 50% glycerol. EC 3.4.21.9, M.W. 26,300.
      Catalogue Number69066
      Brand Family Novagen®
      References
      ReferencesCollins-Racie, L.A. et al. 1995. Bio/Technology 13, 982.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will cleave 50 µg of fusion protein in 16 hours at 23°C, in a buffer containing 20 mM Tris-HCl pH 7.4, 50 mM NaCl, 2 mM CaCl₂.
      Components
      Quality LevelMQ400
      Applications
      Biological Information
      Physicochemical Information
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      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Shipped with Blue Ice or with Dry Ice
      Toxicity Multiple Toxicity Values, refer to MSDS
      Storage -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
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      Supplemental Information
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      Documentation

      Recombinant Enterokinase Certificates of Analysis

      TitleLot Number
      69066

      References

      Reference overview
      Collins-Racie, L.A. et al. 1995. Bio/Technology 13, 982.

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      Bulk packaging
      Protein Purification and Detection Tools

      Citations

      Title
    • Wu. L., et al. (2009) Structural Basis for Proteolytic Specificity of the Human Apoptosis-Inducing Granzyme M J. Immunol. 183, 421.
    • Tanja Knill, et al. (2008) Arabidopsis branched-chain aminotransferase 3 functions in both amino acid and glucosinolate biosynthesis. Plant Physiology 146, 1028-1039.
    • Kenji Kojima, et al. (2008) Roles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptase. Journal of Biological Chemistry 283, 2478-2487.
    • Chester Kuei, et al. (2007) R3(Bδ23 27)R/I5 chimeric peptide, a selective antagonist for GPCR135 and GPCR142 over relaxin receptor LGR7: in vitro and in vivo characterization. Journal of Biological Chemistry 282, 25425-25435.
    • Hann Ling Wong, et al. (2007) Regulation of rice NADPH oxidase by binding of rac GTPase to its N-terminal extension. Plant Cell 19, 4022-4034.
    • Athanasios Michos, et al. (2006) Enhancement of streptolysin O activity and intrinsic cytotoxic effects of the group A streptococcal toxin, NAD-glycohydrolase. Journal of Biological Chemistry 281, 8216-8223.
    • Rachelle M. Smith and Stanly B. Williams. (2006) Circadian rhythms in gene transcription imparted by chromosome compaction in the cyanobacterium Synechococcus elongatus. Proceedings of the National Academy of Sciences (USA) 103, 8564-8569.
    • Jingcai Chen, et al. (2005) Identification and pharmacological characterization of prokineticin 2β as a selective ligand for prokineticin receptor 1. Molecular Pharmacology 67, 2070-2076.
    • Marcelo Comini, et al. (2005) Trypanothione synthesis in Crithidia revisited. Journal of Biological Chemistry 280, 6850-6860.
    • Akari Fukuda, et al. (2005) Differential distribution of proteins expressed in companion cells in the sieve element-companion cell complex of rice plants. Plant and Cell Physiology 46, 1779-1786.
    • Laigeng Li, et al. (2005) Clarification of cinnamoyl co-enzyme a reductase catalysis in monolignol biosynthesis of aspen. Plant and Cell Physiology 46, 1073-1082.
    • Changlu Liu, et al. (2005) INSL5 is a high affinity specific agonist for GPCR142 (GPR100). Journal of Biological Chemistry 280, 292-300.
    • Francisco J. Sandoval and Sanja Roje. (2005) An FMN hydrolase is fused to a riboflavin kinase homolog in plants. Journal of Biological Chemistry 280, 38337-38345.
    • Oliver Schilling, et al. (2005) Exosite modules guide substrate recognition in the ZiPD/ElaC protein family. Journal of Biological Chemistry 280, 17857-17862.
    • Jaime J. Smith, et al. (2005) Differential phospholipid binding by site 3 and site 4 toxins: Implications for structural variability between voltage-sensitive sodium channel domains. Journal of Biological Chemistry 280, 11127-11133.
    • Akiko Takahashi-Terada, et al. (2005) Maize phosphoenolpyruvate carboxylase: mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. Journal of Biological Chemistry 280, 11798-11806.
    • M. Claire H. Holland and John D. Lambris. (2004) A Functional C5a anaphylatoxin receptor in a teleost species. Journal of Immunology 172, 349-355.
    • Deanne M. Compaan and W. Ross Ellington. (2003) Functional consequences of a gene duplication and fusion event in an arginine kinase. 206, 1545-1556.
    • Heinz C. Schroeder, et al. (2003) Emergence and disappearance of an immune molecule, an antimicribioal lectin, in basal metazoa. Journal of Biological Chemistry 278, 32810-32817.
    • Gerald M. Wilson, et al. (2003) Phosphorylation of p40AUF1 regulates binding to A+U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure. Journal of Biological Chemistry 278, 33039-33048.
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      TB150