Pyroglutamate Aminopeptidase from Pyrococcus furiosus, Recombinant from E. coli

• Description:

  Pyroglutamate Aminopeptidase from Pyrococcus furiosus, Recombinant from E. coli_x000D_ Catalog number: B2017789_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 1 Pkg_x000D_ Molecular Weight or Concentration: ~28000 kDa_x000D_ Supplied as: Powder_x000D_ Applications: a molecular tool for various biochemical applications_x000D_ Storage: -20°C_x000D_ Keywords: Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidone Carboxyl Peptidase_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: Tsunasawa S, Nakura S, Tanigawa T, Kato I. Pyrrolidone carboxyl peptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: cloning and overexpression in Escherichia coli of the gene, and its application to protein sequence analysis J Biochem. 1998 Oct;124(4):778-83._x000D_ 2: Liu YD, Goetze AM, Bass RB, Flynn GC. N-terminal glutamate to pyroglutamate conversion in vivo for human IgG2 antibodies J Biol Chem. 2011 Apr 1;286(13):11211-7._x000D_ 3: Sokabe M, Kawamura T, Sakai N, Yao M, Watanabe N, Tanaka I. The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii J Struct Funct Genomics. 2002;2(3):145-54._x000D_ 4: Tanaka H, Chinami M, Mizushima T, Ogasahara K, Ota M, Tsukihara T, Yutani K. X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant J Biochem. 2001 Jul;130(1):107-18._x000D_ 5: Kaushik JK, Ogasahara K, Yutani K. The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus J Mol Biol. 2002 Mar 1;316(4):991-1003._x000D_ 6: Ogasahara K, Nakamura M, Nakura S, Tsunasawa S, Kato I, Yoshimoto T, Yutani K. The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding Biochemistry. 1998 Dec 15;37(50):17537-44._x000D_ 7: Werner WE, Wu S, Mulkerrin M. The removal of pyroglutamic acid from monoclonal antibodies without denaturation of the protein chains Anal Biochem. 2005 Jul 1;342(1):120-5._x000D_ 8: Suzuki Y, Motoi H, Sato K. Quantitative analysis of pyroglutamic acid in peptides J Agric Food Chem. 1999 Aug;47(8):3248-51._x000D_ 9: Mizuguchi M, Takeuchi M, Ohki S, Nabeshima Y, Kouno T, Aizawa T, Demura M, Kawano K, Yutani K. Structural characterization of a trapped folding intermediate of pyrrolidone carboxyl peptidase from a hyperthermophile Biochemistry. 2012 Aug 7;51(31):6089-96._x000D_ 10: Hellström JL, Vehniäinen M, Mustonen M, Lövgren T, Lamminmäki U, Hellman J. Unfolding of the immunoglobulin light and heavy chains is required for the enzymatic removal of N-terminal pyroglutamyl residues Biochim Biophys Acta. 2006 Nov;1764(11):1735-40. _x000D_ _x000D_ Products Related to Pyroglutamate Aminopeptidase from Pyrococcus furiosus, Recombinant from E. coli can be found at Proteins

• Short Description:

  Catalog Number: B2017789 (1 Pkg)

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height:

  0.5

• Height :

  0.5

• CAS Number:

  9000-83-3