LON Protease E. coli Recombinant Protein

• Description:

  LON Protease E. coli Recombinant Protein_x000D_ Catalog number: B2012660_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 50 ug_x000D_ Molecular Weight or Concentration: 88.3 kDa_x000D_ Supplied as: Lyophilized Powder_x000D_ Applications: molecular tool for various biochemical applications_x000D_ Storage: -20°C_x000D_ Keywords: LON PROTEASE Protein, E. coli, Recombinant (His Tag)_x000D_ Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ References:_x000D_ 1: Sonezaki S, Kondo A, Oba T, Ishii Y, Kato Y, Nakayama H. Overproduction and purification of Lon protease from Escherichia coli using a maltose-binding protein fusion system Appl Microbiol Biotechnol. 1994 Nov;42(2-3):313-8._x000D_ 2: Gur E, Vishkautzan M, Sauer RT. Protein unfolding and degradation by the AAA+ Lon protease Protein Sci. 2012 Feb;21(2):268-78._x000D_ 3: Fu GK, Smith MJ, Markovitz DM. Bacterial protease Lon is a site-specific DNA-binding protein J Biol Chem. 1997 Jan 3;272(1):534-8._x000D_ 4: Sonezaki S, Okita K, Oba T, Ishii Y, Kondo A, Kato Y. Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease Appl Microbiol Biotechnol. 1995 Dec;44(3-4):484-8._x000D_ 5: Sonezaki S, Ishii Y, Okita K, Sugino T, Kondo A, Kato Y. Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro Appl Microbiol Biotechnol. 1995 May-Jun;43(2):304-9._x000D_ 6: Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A. Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution J Struct Biol. 2004 Apr-May;146(1-2):113-22._x000D_ 7: Goff SA, Goldberg AL. An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli J Biol Chem. 1987 Apr 5;262(10):4508-15._x000D_ 8: Ishii Y, Sonezaki S, Iwasaki Y, Miyata Y, Akita K, Kato Y, Amano F. Regulatory role of C-terminal residues of SulA in its degradation by Lon protease in Escherichia coli J Biochem. 2000 May;127(5):837-44._x000D_ 9: Lee AY, Tsay SS, Chen MY, Wu SH. Identification of a gene encoding Lon protease from Brevibacillus thermoruber WR-249 and biochemical characterization of its thermostable recombinant enzyme Eur J Biochem. 2004 Feb;271(4):834-44._x000D_ 10: Gonzalez M, Frank EG, Levine AS, Woodgate R. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis Genes Dev. 1998 Dec 15;12(24):3889-99. _x000D_ _x000D_ Products Related to LON Protease E. coli Recombinant Protein can be found at Enzymes

• Short Description:

  Catalog Number: B2012660 (50 ug)_x000D_ LON Protease E. coli Recombinant Protein is a high quality LON Protease E. coli protein His tagged and expressed in E. coli. This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request._x000D_ _x000D_

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height :

  0.5

• CAS Number:

  9000-83-3