Enzymes dans les Protéines Recombinantes

Adenylate Kinase 1 Protein, Rat, Recombinant (His) is expressed in E.

HSD3B1 Protein, Human, Recombinant (His & Myc) is expressed in E.

Lipase 67 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 67 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (37 %), laurate (3 %) and palmitate (0.2 %).

CKMT2 Protein, Rat, Recombinant (His) is expressed in E.

Trypsin-1 Protein, Gadus morhua, Recombinant (His) is expressed in E. coli.

SPO11 Protein, Human, Recombinant (His) is expressed in Baculovirus Insect Cells with C-6xHis. The accession number is Q9Y5K1.

Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively.

N/A.

Lys-gingipain W83 Protein, Porphyromonas gingivalis, Recombinant (His) is expressed in E.

Lipoprotein lipase is a critical enzyme used to modulate lipid processing, primarily sourced from mammalian tissues. It functions by hydrolyzing triglycerides present in circulating chylomicrons and very low-density lipoproteins. This enzymatic process liberates free fatty acids, which can subsequently be utilized as energy by peripheral tissues or stored in adipose tissue. Lipoprotein lipase is pivotal in lipid metabolism, participating in maintaining homeostasis of plasma lipid levels. The enzyme is widely employed in biochemical and physiological research to explore mechanisms underlying lipid metabolism disorders, such as hyperlipidemia and atherosclerosis. Its role in metabolic pathways makes it invaluable for studies aiming to develop therapeutic strategies targeting lipid-related diseases. Additionally, lipoprotein lipase assays are utilized to measure enzymatic activity in various biological samples, facilitating the assessment of lipid metabolism in experimental settings. This enzyme, therefore, not only serves as a tool for scientific inquiry but also enhances our understanding of metabolic health and disease.

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide.

LacBuster®-S 50 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 50 IU beta-lactamase II and 500 IU beta-lactamase I activity per vial.

TrkB Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag.

Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.

Thioredoxin reductase (TR, TrxR) (EC 1.8.1.9) is an enzyme that reduce thioredoxin using NADPH as a co-factor, and also contains FAD. One unit of thioredoxin reductase will raise increase light absorbance by 1.0 per minute at 412nm in the presence of thioredoxin and Ellman's reagent at pH 7.0 and 25 °C.

RIPK3 Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 58.9 kDa and the accession number is Q9Y572.

EP300 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli with N-10xHis, C-Myc. The accession number is B2RWS6.

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

N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family.

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.

SMUG1 Protein, Human, Recombinant (His & SUMO) is expressed in E.

Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industries

Cytochrome C oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain.

Key enzyme for ketone body catabolism.

OGDC-E1 Protein, Human, Recombinant (His & SUMO) is expressed in E.

Ubiquitin-Conjugating Enzyme E2 S (UBE2S) is a member of the Ubiquitin-Conjugating Enzyme family.

CHST5 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag.

Thrombin-like snake venom serine protease that cleaves beta chain of fibrinogen (FGB), releasing fibrinopeptide B.

β-Glucosidase (β-D-glucosidase, systematic name β-D-glucoside glucohydrolase; EC 3.2.1.21) is an enzyme that catalyzes the release the terminal glucose monomers from cellulose and the other oligo- and poly saccharides with β-1,4-linked glucosyl residues. One Unit of β-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic p-nitrophenyl β-glucoside per minute under optimum conditions.