Enzymes dans les Protéines Recombinantes

LPL Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with N-10xHis tag.

PTPRB Protein, Human, Recombinant (His) is expressed in Yeast.

The improved, thermostable X-ShiningTM Luciferase is suitable for any luciferin-luciferase-based assay using D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins). Examples of its typical applications include ATP tests in hygiene monitoring, ATP tests in drug screenings and bacteria identification in microbial assays. The thermostable luciferase X-ShiningTM has been optimized by genetic engineering for strongly increased thermostability and storage stability. In temperature stress tests, the enzyme survives temperatures of 60°C for over an hour, whereas a wild type luciferase from firefly is inactivated after only a few minutes. The extraordinary stability makes it user-friendly and eliminates some of the main disadvantages and limitations of the commonly used wild type luciferase. X-ShiningTM Luciferase is supplied as aqueous solution with glycerol or as a lyophilisate (BX180145), and it may be stored for months at room temperature without significant loss of function. Find out more about our innovative X-Shining range here X-Shining | Innovation | Cymit Quimica Carbosynth.

Reelin Protein, Human, Recombinant (E. coli, His) is expressed in E. coli.

Choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the following reaction: choline + O2 + H20 ⇌ betaine aldehyde + H2O2One unit of choline oxidase will form 1 μmole of H2O2 by oxidizing choline to betaine aldehyde per min at pH 8.0 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.

ST6GAL1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Immobilized lipase is an advanced enzymatic product, which is derived from lipases, enzymes primarily sourced from microbial, plant, or animal origins. This product operates through a catalytic mechanism where the lipase is attached to a solid support, enhancing its stability and reusability in various reactions. This immobilization allows the enzyme to maintain activity over a wide range of conditions, including different pH levels and temperatures. The applications of immobilized lipase are extensive in the field of biotechnology. It is widely used in the synthesis of biodiesel through transesterification of triglycerides and alcohols. Additionally, it plays a crucial role in the food industry for the modification of fats and oils and in pharmaceuticals for enantioselective transformations. The stability and reusability of immobilized lipases make them invaluable for industrial processes, where they facilitate efficient and sustainable production. Their ability to catalyze reactions without contaminating products underscores their importance in processes requiring high purity, thereby providing a superior alternative to free enzyme systems.

Tyrosine-Protein Kinase Blk (BLK) contains one protein kinase domain, one SH2 domain and one SH3 domain.

NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is

LYZL1 Protein, Human, Recombinant (His & SUMO) is expressed in E.

Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT203 Glucosyltransferase, please see Table 1 that lists the available GTases with GT203 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed. Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.

A cytochrome P450 monooxygenase involved in the metabolism of fatty acids.

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome.

NDST1 Protein, Human, Recombinant (His & SUMO) is expressed in E.

LacBuster™-S 5000 is an enzymatic product, specifically a beta-lactamase, which originates from microbial sources known for their ability to produce enzymes that break down antibiotics. This product functions by hydrolyzing the beta-lactam ring of relevant antibiotics, thereby neutralizing their antibacterial activity. The primary applications of LacBuster™-S 5000 include its utilization in laboratory settings where beta-lactam antibiotics are present, allowing researchers to study microbial interactions without the interference of antibiotic activity. It is particularly valuable in experiments requiring selective deactivation of beta-lactam antibiotics to facilitate the growth of specific bacterial strains or when it’s necessary to clear antibiotics from samples without damaging the sample integrity. The use of this product is critical for understanding antibiotic resistance mechanisms and for experimental setups where antibiotic interference could skew results. As such, LacBuster™-S 5000 serves as a powerful tool in microbiological research and antibiotic resistance studies.

SMARCA2 Protein, Human, Recombinant (His) is expressed in Yeast.

Aldehyde dehydrogenase 1 family, member A1 (ALDH1A1), also known as Aldehyde dehydrogenase 1 (ALDH1), or Retinaldehyde Dehydrogenase 1 (RALDH1), is an enzyme

B4GALT1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.

ACSL4 Protein, Mouse, Recombinant (His) is expressed in E. coli.