Protease Subtilisin A (from Bacillus licheniformis)

Référence B2014487

Conditionnement : 50mg

Marque : Molecular Depot

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Protease Subtilisin A (from Bacillus licheniformis)

Catalog Number: B2014487 (50 mg)
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.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

SKU: B2014487 Categories: Enzymes, Proteins Tag: MD 1000

Product Description

Protease Subtilisin A (from Bacillus licheniformis)
Catalog number: B2014487
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 50 mg
Molecular Weight or Concentration: 30.2 kDa
Supplied as: Powder
Applications: molecular tool for various biochemical applications
Storage: -20°C
Keywords: subtilisin; subtilisin A
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.

References:
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

Products Related to Protease Subtilisin A (from Bacillus licheniformis) can be found at Enzymes

Additional Information

Weight 48 oz
Dimensions 8 × 8 × 8 in