Enzyme

DNA helicase which plays a role in chromatin-remodeling following DNA damage.

cGMP-dependent 3',5'-cyclic phosphodiesterase, also known as cyclic GMP-stimulated phosphodiesterase and PDE2A, is a peripheral membrane protein that belongs to

Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes.

Human Sulfatase Modifying Factor 1 (SUMF1) is a 42kDa protein.

G protein-coupled receptor kinase 5, also known as G protein-coupled receptor kinase GRK5 and GRK5, is a member of the protein kinase superfamily, AGC Ser/Thr

Carbonic Anhydrase 14 Protein, Human, Recombinant (His), Biotinylated is expressed in HEK293 Cells. The accession number is Q9ULX7.

N/A.

Pyroglutamate aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, is an enzymatic product that specifically targets N-terminal pyroglutamyl residues in peptide chains. This enzyme is derived from the hyperthermophilic archaeon Pyrococcus furiosus, which allows it to exhibit high thermal stability and activity across a broad range of temperatures. Being produced recombinantly in E. coli ensures consistent availability and purity suitable for scientific applications. The mode of action of this aminopeptidase involves the cleavage of pyroglutamyl residues from the N-terminus of peptides, facilitating subsequent analyses and modifications. This enzymatic activity is crucial because pyroglutamate formation can inhibit peptide processing and sequencing reactions, posing challenges in proteomics and protein characterization. Applications of Pyroglutamate aminopeptidase include its use in peptide sequencing workflows, where it enables or enhances the identification of protein and peptide structures by removing blocking pyroglutamyl groups. Its stability at high temperatures also makes it valuable in applications where heat-resistant enzymes are required, allowing for effective peptide modification under various experimental conditions.

FLT1 Protein, Human, Recombinant (aa 1-328, His) is expressed in HEK293 mammalian cells with His tag.

SUMO protease, also known as Ulp, is a highly specific enzyme that removes small ubiquitin-like modifier (SUMO) from recombinant SUMO fusion proteins. Unlike proteases such as enterokinase or TEV, which recognize linear amino acid sequences, SUMO protease recognizes the native tertiary structure of SUMO, allowing precise cleavage without leaving extra residues at the cleavage site. This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification.

tPA Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 28 kDa and the accession number is P00750-1.

Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose.

Angiogenin belongs to the pancreatic ribonuclease family.

Protein-arginine deiminase type-4, also known as HL-6 PAD, Peptidylarginine deiminase IV, Protein-arginine deiminase type I V and PADI4, is a cytoplasm and

NUDT5 (Nudix Hydrolase 5) is a Protein Coding gene.

AKR1C3, is an enzyme which belongs to the aldo/keto reductase family.

Genetic engineers have used glutathione S-transferase to create the GST gene fusion system.

Guanylyl cyclase C (GUCY2C) has canonical centrality in defense of key intestinal homeostatic mechanisms, encompassing fluid and electrolyte balance, epithelial

The recycling of citrulline by argininosuccinate synthase 1 (ASS1) and argininosuccinate lyase (ASL) is crucial to maintain arginine availability and nitric

Kallikrein 14 Protein, Mouse, Recombinant (His) is expressed in E. coli.

GSK3B Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag.

beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated. This type of enzyme is found widespread in many microorganisms, plants and animals. In E. coli for instance, the beta-Gal protein is encoded by the lacZ gene. The enzyme is often used as a reporter for monitoring gene expression. beta-Gal also has good characteristics when conjugated to antibody molecules or streptavidin for use in ELISA kits. In addition, the enzyme is used to determine lactose in biological fluids and it is employed in food processing operations. Traditionally, beta-Gal activity is tested using the X-Gal or ONPG chromogenic substrates. But with the pioneering AquaSpark® beta-D-galactoside a substrate for beta-Gal detection becomes available that provides a previously unseen sensitivity. See here for futher informaiton on AquaSpark®: AquaSpark Chemiluminescence | Cymit Quimica

PARP9 Protein, Human, Recombinant (His & Myc) is expressed in HEK293.

During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation.

ENPP2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Carbonic Anhydrase 4 Protein, Human, Recombinant (His), Biotinylated is expressed in CHO Stable Cells. The accession number is P22748-1.

PPIL2, is an enzyme that belongs to the cyclophilin family.

Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis.

Catalyst for signal development in immunoassays

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

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium.

hCAIX-IN-5 was a selective hCAIX inhibitor, inhibiting hCAI, hCAII, hCAIV, and hCAIX with Ki values of >10000, >10000, 130.7, and 829.1 nM, respectively.

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).

Staphopain A Protein, S.

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

PAIRED PRODUCTS AVAILABLE: 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate, Substrate, EM03201 4MU-alpha-L-idopyranosiduronic acid, Substrate, EM04841   Alpha-L-iduronidase is a glycoside hydrolase that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate. This enzyme is supplied as a lyophilisate of: 25% (w/w) Iduronidase enzyme (protein), 37% (w/w) sucrose, 38% (w/w) MOPS potassium (buffer, pH 7.4). The enzyme is derived from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as an aqueous solution (FI179383)

PCSK9 Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with mFc tag.

Phosphinothricin N-acetyltransferase (PAT) is an enzyme that acetylates the free NH2 group of L-phosphinothricin (L-PPT) in the presence of acetyl-CoA as a co-

CBR1 Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 32.2 kDa and the accession number is P16152.

The two recurrent dominant mutations in RAB11B leading to a neurodevelopmental syndrome, likely caused by altered GDP/GTP binding that inactivate the protein

Involved in protein export.

RAB27B Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 24.3 kDa and the accession number is O00194.

Rna-dependent RNA polymerase part of the packaging complex that packages the viral RNA segments, replicate them into a double-stranded form and transcribe them.

Poly(ADP-ribose) glycohydrolase is an enzyme, which is derived from various organisms, including eukaryotic cells. It plays a crucial role in the regulation of poly(ADP-ribose) (PAR) metabolism. This enzyme functions by hydrolyzing the glycosidic bonds in poly(ADP-ribose) chains, thereby regulating the cellular levels of PAR by converting it back to ADP-ribose units. Poly(ADP-ribose) glycohydrolase is significantly involved in DNA repair processes and cellular stress responses. PAR chains are primarily synthesized in response to DNA damage and play an integral role in recruiting and modulating the activity of repair proteins. By controlling the turnover of these PAR chains, Poly(ADP-ribose) glycohydrolase maintains cellular homeostasis and facilitates efficient DNA repair. This regulatory mechanism is essential for maintaining genomic stability and preventing pathological conditions such as cancer. Applications of this enzyme extend to research in DNA repair mechanisms, cell death pathways, and the development of therapeutic strategies targeting PAR metabolism. Understanding its function and manipulation can provide insights into cancer treatment and neurodegenerative diseases, where PAR metabolism is often dysregulated.

Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family.

Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling.

3-Oxo-5β-steroid Δ4-dehydrogenase is an enzyme crucial in the metabolic pathway of steroid hormones, facilitating the conversion of androgens and estrogens. It is predominantly found in the liver, but also in other tissues where steroid biosynthesis occurs. This enzyme catalyzes the dehydrogenation at the Δ4 position of 3-oxo-5β-steroids, playing a significant role in the modulation and regulation of steroid hormone levels within cells. The enzyme functions by oxidizing the Δ4 double bond in the steroid structure, which is a critical step in the conversion of active steroids to their inactive metabolites. This action helps maintain a balance in hormone levels, preventing excessive accumulation of potentially biologically active steroids. In scientific research, understanding and manipulating the activity of 3-Oxo-5β-steroid Δ4-dehydrogenase can offer insights into disorders related to steroid metabolism, such as endocrine imbalances and certain cancers. Additionally, studying this enzyme can advance therapeutic strategies that target steroid-related diseases by modulating enzyme activity or expression. Its application extends to pharmaceutical research, where it can be used to evaluate the metabolic profiles of novel steroid-based drugs.

Accepts electrons from ETF and reduces ubiquinone.

CYP11A1 Protein, Human, Recombinant (His & SUMO) is expressed in E.