SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.

Price:
374 EUR
448 USD
310 GBP
known as: SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.
Catalog number: genta-ABS0088
Product Quantity: 1 ml
Category:
Supplier: AbD

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Gene target: glutathione alk phos

Related genes to: SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.

Symbol : Alk NIH gene
chromosome : Un
description : anaplastic lymphoma receptor tyrosine kinase
type of gene : protein-coding
Other designations : ALK tyrosine kinase receptor
Modification date : 2016-02-20
Symbol : PEROXIDASE NIH gene
LocusTag : Csa_4G285730
chromosome : 4
description : peroxidase 2-like
type of gene : protein-coding
Other designations : pre-peroxidase
Modification date : 2016-05-26
Symbol : phoS NIH gene
LocusTag : YE4201
Synonyms : pstS
description : phosphate ABC transporter substrate-binding protein
type of gene : protein-coding
Modification date : 2015-06-26

Related Pathways to: SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.

Gene about :ALK
Pathway :Hs Differentiation Pathway
ALK
Gene about :Peroxidase
Pathway :Hs Eicosanoid Synthesis
Peroxidase
Gene about :Glutathione
Pathway :Rn Selenium Micronutrient Network
Glutathione

Related product to: SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.

Related Articles about: SHEEP ANTI BOVINE GLUTATHIONE PEROXIDASE Alk. Phos.

Real-world first-line treatment and overall survival in non-small cell lung cancer without known EGFR mutations or ALK rearrangements in US community oncology setting.

To establish a baseline for care and overall survival (OS) based upon contemporary first-line treatments prescribed in the era before the introduction of immune checkpoint inhibitors, for people with metastatic non-small cell lung cancer (NSCLC) without common actionable mutations. - Source :PubMed

Expression and characterization of Soybean Seed Coat Peroxidase in Escherichia coli BL21(DE3).

Soybean seed coat peroxidase(SBP) is a valuable enzyme having a broad variety of applications in analytical chemistry, biochemistry and food processing. In the present study, the sscp gene (Gene ID: 548068) was optimized based on the preferred codon usage of Escherichia coli, synthesized, and expressed in E. coli BL21(DE3). SDS-PAGE and western blot analysis of this expressed protein revealed that its molecular weight is approximately 39 kDa. The effects of induction temperature, concentration of IPTG (isopropyl-β-D-thiogalactoside) and hemin, induction time, expression time were optimized to enhance SBP production with a maximum activity of 11.23 U/mL (8.64 U/mg total protein). Furthermore, the kinetics of enzyme-catalyzed reactions of recombinant protein was determined. When 2,2'-azinobis(3-ethylbenzothiazoline 6-sulfonic acid)(ABTS) was used as substrate, optimum reaction temperature and pH of the enzyme were 85°C and 5.0, respectively. The effects of metal ions on the enzymatic reaction were also further investigated. The SBP was successfully expressed in E. coli BL21(DE3) which would provide a more efficient production strategy for industrial applications of SBP. - Source :PubMed

FeCo nanoparticles-embedded carbon nanofibers as robust peroxidase mimics for sensitive colorimetric detection of l-cysteine.

A simple and low cost detection of l-cysteine is essential in the fields of biosensors and medical diagnosis. In this study, we have developed a simple electrospinning, followed by calcination process to prepare FeCo nanoparticles embedded in carbon nanofibers (FeCo-CNFs) as an efficient peroxidase-like mimic for the detection of l-cysteine. FeCo nanoparticles are uniformly dispersed within CNFs, and their diameters are highly influenced by the calcination temperature. The calcination temperature also influences the peroxidase-like catalytic activity, and the maximum activity is achieved at a calcination temperature of 550 °C. Owing to the high catalytic activity of the as-prepared FeCo-CNFs, a colorimetric technique for the rapid and accurate determination of l-cysteine has been developed. The detection limit is about 0.15 μM with a wide linear range from 1 to 20 μM. In addition, a high selectivity for the detection of l-cysteine over other amino acids, glucose and common ions is achieved. This study provides a simple, rapid and sensitive sensing platform for the detection of l-cysteine, which is a promising candidate for potential applications in biosensing, medicine, environmental monitoring. - Source :PubMed

ALK Fusion Detection in Circulating Free DNA: Finding an Important Needle in the Haystack.

- Source :PubMed

Peroxidase Activity of a c-Type Cytochrome b5 in the Non-Native State is Comparable to that of Native Peroxidases.

The design of artificial metalloenzymes has achieved tremendous progress, although few designs can achieve catalytic performances comparable to that of native enzymes. Moreover, the structure and function of artificial metalloenzymes in non-native states has rarely been explored. Herein, we found that a c-type cytochrome b5 (Cyt b5), N57C/S71C Cyt b5, with heme covalently attached to the protein matrix through two Cys-heme linkages, adopts a non-native state with an open heme site after guanidine hydrochloride (Gdn⋅HCl)-induced unfolding, which facilitates H2O2 activation and substrate binding. Stopped-flow kinetic studies further revealed that c-type Cyt b5 in the non-native state exhibited impressive peroxidase activity comparable to that of native peroxidases, such as the most efficient horseradish peroxidase. This study presents an alternative approach to the design of functional artificial metalloenzymes by exploring enzymatic functions in non-native states. - Source :PubMed

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