79302
Esterase from Bacillus stearothermophilus
recombinant, expressed in E. coli, ≥4.0 U/mg
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Doporučené produkty
recombinant
expressed in E. coli
Quality Level
form
crystalline
crystals
powder or flakes
specific activity
≥4.0 U/mg
storage temp.
−20°C
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Application
Esterase, from Bacillus stearothermophilus, may be used for the characterization of novel esterases . Product 79302 is recombinant and expressed in E. coli.
Biochem/physiol Actions
An esterase is a hydrolase that splits esters into acids and alcohols. The esterase catalyzes the transesterification of 1-phenylethanol.
The esterase catalyzes the transesterification of 1-phenylethanol.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Unit Definition
1 U corresponds to the amount of enzyme which converts 1 μmol 4-nitrophenyl-L-acetate per minute at pH 7.5 and 30°C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Osvědčení o analýze (COA)
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Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.
Characterization and heterologous gene expression of a novel esterase from Lactobacillus casei CL96.
Young J Choi et al.
Applied and environmental microbiology, 70(6), 3213-3221 (2004-06-09)
A novel esterase gene (estI) of Lactobacillus casei CL96 was localized on a 3.3-kb BamHI DNA fragment containing an open reading frame (ORF) of 1,800 bp. The ORF of estI was isolated by PCR and expressed in Escherichia coli, the
Jessica Lusty Beech et al.
RSC advances, 12(13), 8119-8130 (2022-04-16)
Esterase enzymes catalyze diverse hydrolysis reactions with important biological, commercial, and biotechnological applications. For the improvement of these biocatalysts, there is a need for widely accessible, inexpensive, and adaptable activity screening assays that identify enzymes with particular substrate specificities. Natural
Marie C Fortin et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 326-331 (2012-12-12)
Studies on therapeutic drug disposition in humans have shown significant alterations as the result of pregnancy. However, it is not known whether pesticide metabolic capacity changes throughout pregnancy, which could affect exposure of the developing brain. We sought to determine
B Sànchez-Nogué et al.
Environmental science and pollution research international, 20(5), 3480-3488 (2012-12-06)
The common sole, Solea solea (Linneus, 1758), and the Senegalese sole, Solea senegalensis (Kaup, 1858), are two important commercial species that coexist in the NW Mediterranean. In order to assess the species' ability to respond to chemical insults, a comparison
Joshua P Lewis et al.
Pharmacogenetics and genomics, 23(1), 1-8 (2012-11-01)
Carboxylesterase 1 (CES1) is the primary enzyme responsible for converting clopidogrel into biologically inactive carboxylic acid metabolites. We genotyped a functional variant in CES1, G143E, in participants of the Pharmacogenomics of Anti-Platelet Intervention (PAPI) study (n=566) and in 350 patients
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