Protease Subtilisin A (from Bacillus licheniformis)

• Description:

  Protease Subtilisin A (from Bacillus licheniformis)_x000D_ Catalog number: B2014487_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 50 mg_x000D_ Molecular Weight or Concentration: 30.2 kDa_x000D_ Supplied as: Powder_x000D_ Applications: molecular tool for various biochemical applications_x000D_ Storage: -20°C_x000D_ Keywords: subtilisin; subtilisin A_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: Fan H, Liu Z, Zhang R, Wang N, Dou K, Mijiti G, Diao G, Wang Z. Functional analysis of a subtilisin-like serine protease gene from biocontrol fungus Trichoderma harzianum J Microbiol. 2014 Feb;52(2):129-38._x000D_ 2: Frankaer CG, Moroz OV, Turkenburg JP, Aspmo SI, Thymark M, Friis EP, Stahl K, Nielsen JE, Wilson KS, Harris P. Analysis of an industrial production suspension of Bacillus lentus subtilisin crystals by powder diffraction: a powerful quality-control tool Acta Crystallogr D Biol Crystallogr. 2014 Apr;70(Pt 4):1115-23._x000D_ 3: Xiao S, Hu D, Gao Y, Ai Y, Luo S, Chen S, Wang B, Zhou L, Dong Y, Wang Y. Safety assessment of subtilisin QK in rats BMC Pharmacol Toxicol. 2021 Jun 26;22(1):38._x000D_ 4: van der Laan JC, Gerritse G, Mulleners LJ, van der Hoek RA, Quax WJ. Cloning, characterization, and multiple chromosomal integration of a Bacillus alkaline protease gene Appl Environ Microbiol. 1991 Apr;57(4):901-9._x000D_ 5: Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R. The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site Structure. 1997 Apr 15;5(4):521-32._x000D_ 6: Wang C, Xu J, Ban R. Metabolic engineering of Bacillus subtilis for high-level production of uridine from glucose Lett Appl Microbiol. 2022 Oct;75(4):824-830._x000D_ 7: Ferjancic A, Puigserver A, Gaertner H. Subtilisin-catalysed peptide synthesis and transesterification in organic solvents Appl Microbiol Biotechnol. 1990 Mar;32(6):651-7._x000D_ 8: Santos AM, González M, Pacheco Y, Griebenow K. Comparison of theoretical and experimental data to evaluate substrate diffusional limitations for crown ether- and methyl-beta-cyclodextrin-activated serine protease subtilisin Carlsberg in tetrahydrofuran Biotechnol Bioeng. 2003 Nov 5;84(3):324-31._x000D_ 9: Vossenberg P, Beeftink R, Stuart MC, Tramper H. Effect of enzyme dehydration on alcalase-catalyzed dipeptide synthesis in near-anhydrous organic media Biotechnol Prog. 2013 Jul-Aug;29(4):870-5._x000D_ 10: Ru MT, Dordick JS, Reimer JA, Clark DS. Optimizing the salt-induced activation of enzymes in organic solvents: effects of lyophilization time and water content Biotechnol Bioeng. 1999 Apr 20;63(2):233-41. _x000D_ _x000D_ Products Related to Protease Subtilisin A (from Bacillus licheniformis) can be found at Enzymes

• Short Description:

  Catalog Number: B2014487 (50 mg)_x000D_ Protease Subtilisin A (from Bacillus licheniformis) is a high quality Protease (Subtilisin A from Bacillus licheniformis) (Powder). 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