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| Product | Description | |
|---|---|---|
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. |  |
| Adenosine deaminase Bovine, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Protein determined by biuret. Applications: Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays. adenosine deaminase is a potential target for treatments of combined immunodeficiency disease. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 32.5-33 kDa. Activity: 60-130 units/mg protein; > 130 units/mg protein; 150-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0. Source: E. coli. Species: Bovine. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-0032. | |
| Adenosine deaminase from Human, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Applications: Adenosine deaminase (ada) is a key enzyme in purine metabolism and is essential for normal immune function. it is important in the study of immune system diseases such as rheumatoid arthritis. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Activity: >1 U/mL. Storage: Store at -20°C. Source: E. coli. Species: Human. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1583. | |
| Adenosine deaminase, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. Purity: > 90 %. ADA. Mole weight: About 53kDa (SDS-PAGE). Activity: 200U/mg protein. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Source: E. coli. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1009. | |
| α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277. | |
| α(2-3) Neuraminidase S from Streptococcus pneumoniae, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neurami...;2-3 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 74000 daltons. Activity: 160,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM EDTA. Source: E. coli. Species: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase S; α(2-3) Neuraminidase. Cat No: NATE-1275. | |
| α-tubulin N-acetyltransferase | The enzyme from Chlamydomonas flagella also acetylates mammalian brain α-tubulin. Group: Enzymes. Synonyms: α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Enzyme Commission Number: EC 2.3.1.108. CAS No. 99889-90-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2046; α-tubulin N-acetyltransferase; EC 2.3.1.108; 99889-90-4; α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Cat No: EXWM-2046. | |
| aminopeptidase B | Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Enzyme Commission Number: EC 3.4.11.6. CAS No. 9073-92-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4027; aminopeptidase B; EC 3.4.11.6; 9073-92-1; arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Cat No: EXWM-4027. | |
| Brassicasterol-(2,2',3,4,4',6-D6) | Brassicasterol-(2,2',3,4,4',6-D6) is derived from Brassicasterol (B676850), which is a phytosterol found in canola oil, rapeseed oil, marine algae and shellfish. This compound has been shown to inhibit sterol Δ24-reductase, an enzyme involved in the mammalian cholesterol biosynthesis pathway. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1mg, 2.5mg. Molecular Formula: C28H40D6O, Molecular Weight: 404.7. US Biological Life Sciences. |  Worldwide |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| CAY10594 | Phospholipase D (PLD) is an enzyme which cleaves the head group from phospholipids, producing the second messenger phosphatidic acid. There are two mammalian isoforms of PLD, which are PLD1 and PLD2. CAY10594 is a potent phospholipase D2 inhibitor (PLD2), which also prevents the invasive migration of breast cancer cells. It ameliorates acetaminophen-induced acute liver injury by regulating the phosphorylated-GSK-3β/JNK axis. Synonyms: CAY 10594; CAY-10594. Grades: ≥98%. CAS No. 1130067-34-3. Molecular formula: C26H28N4O2. Mole weight: 428.5. |  |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| D-2-hydroxyacid dehydrogenase (quinone) | The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors. Group: Enzymes. Synonyms: (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.1.5.10. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0428; D-2-hydroxyacid dehydrogenase (quinone); EC 1.1.5.10; (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Cat No: EXWM-0428. | |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| farnesylcysteine lyase | A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine. Group: Enzymes. Synonyms: FC lyase; FCLY. Enzyme Commission Number: EC 1.8.3.6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1663; farnesylcysteine lyase; EC 1.8.3.6; FC lyase; FCLY. Cat No: EXWM-1663. | |
| glucan 1,4-α-glucosidase | Most forms of the enzyme can rapidly hydrolyse 1,6-α-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions. Group: Enzymes. Synonyms: glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase. Enzyme Commission Number: EC 3.2.1.3. CAS No. 9032-08-0. Glucoamylase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3893; glucan 1,4-α-glucosidase; EC 3.2.1.3; 9032-08-0; glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase. Cat No: EXWM-3893. | |
| Glyceraldehyde-3-phosphate dehydrogenase from Human, Recombinant | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a tetramer of 36 kDa subunits, is a catalytic enzyme involved in glycolysis. GAPDH catalyzes the reversible reduction of glyceraldehyde-3-phosphate to 3-phosphoglycerol phosphate in the presence of NAD+. Besides functioning as a glycolytic enzyme in the cytoplasm, mammalian GAPDH is also involved in a variety of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. Glyceraldehyde-3-phosphate dehydrogenase was also found to bind to mutant polyglutamine proteins formed in neurodegenerative diseases such as Huntingto...horylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Mole weight: 37,984 Da. Activity: > 80 units/mg protein. Stability: Store at -20°C. Form: Lyophilized from a buffered solution with stabilizers. Source: E. coli. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate | |
| glycylpeptide N-tetradecanoyltransferase | The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein. Group: Enzymes. Synonyms: peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Enzyme Commission Number: EC 2.3.1.97. CAS No. 110071-61-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2279; glycylpeptide N-tetradecanoyltransferase; EC 2.3.1.97; 110071-61-9; peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Cat No: EXWM-2279. | |
| heme oxygenase (biliverdin-producing) | This mammalian enzyme participates in the degradation of heme. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. The enzyme requires NAD(P)H and EC 1.6.2.4, NADPH-hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin). Group: Enzymes. Synonyms: ORP33 proteins; haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating). Enzyme Commission Number: EC 1.14.14.18. CAS No. 9059-22-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0915; heme oxygenase (biliverdin-producing); EC 1.14.14.18; 9059-22-7; ORP33 proteins; haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating). Cat No: EXWM-0915. | |
| heme oxygenase (biliverdin-producing, ferredoxin) | The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4, NADPH-hemoprotein reductase. Group: Enzymes. Synonyms: HO1 (gene name); HY1 (gene name); HO3 (gene name); HO4 (gene name); pbsA1 (gene name). Enzyme Commission Number: EC 1.14.15.20. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0945; heme oxygenase (biliverdin-producing, ferredoxin); EC 1.14.15.20; HO1 (gene name); HY1 (gene name); HO3 (gene name); HO4 (gene name); pbsA1 (gene name). Cat No: EXWM-0945. | |
| [heparan sulfate]-glucosamine 3-sulfotransferase 3 | Two major substrates contain the tetrasaccharides: ? undetermined 2-sulfo-uronic acid? GlcN2S? IdoA2S? GlcN*? and ? undetermined 2-sulfo-uronic acid? GlcN2S? IdoA2S? GlcN6S*? (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk). Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)]. Group: Enzymes. Enzyme Commission Number: EC 2.8.2.30. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3390; [heparan sulfate]-glucosamine 3-sulfotransferase 3; EC 2.8.2.30. Cat No: EXWM-3390. | |
| inositol-polyphosphate 5-phosphatase | One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids. Group: Enzymes. Synonyms: type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP3/Ins(1,3,4,5)P4 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-. Enzyme Commission Number: EC 3.1.3.56. CAS No. 106283-14-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3661; inositol-polyphosphate 5-phosphatase; EC 3.1.3.56; 106283-14-1; type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP3/Ins(1,3,4,5)P4 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-phosphatase; D-myo-inositol 1,4,5-trisphosphate 5-phosphatase; L-myo-inositol 1,4,5-trisphosphate-monoesterase; inositol phosphate 5-phosphomonoesterase; inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase; Ins(1,4,5)P3 5-phosphatase; D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase; inositol 1,4,5-trisphosphate phosphatase; inositol polyphosphate-5-phosphatase; myo-inositol-1,4,5-trisphosphate 5-phosphatase; inositol-1,4,5-trisphosphate 5-phosphatase. Cat No: EXWM-3661. | |
| legumain | Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13. Group: Enzymes. Synonyms: asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Enzyme Commission Number: EC 3.4.22.34. CAS No. 149371-18-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4209; legumain; EC 3.4.22.34; 149371-18-6; asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Cat No: EXWM-4209. | |
| long-chain fatty acid ω-monooxygenase | The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4). Group: Enzymes. Synonyms: CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Enzyme Commission Number: EC 1.14.13.205. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0807; long-chain fatty acid ω-monooxygenase; EC 1.14.13.205; CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Cat No: EXWM-0807. | |
| methylglyoxal reductase (NADH) | This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Enzyme Commission Number: EC 1.1.1.78. CAS No. 37250-16-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0361; methylglyoxal reductase (NADH); EC 1.1.1.78; 37250-16-1; methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Cat No: EXWM-0361. | |
| N1-acetylpolyamine oxidase | The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase). Group: Enzymes. Synonyms: hPAO-1; PAO (ambiguous); mPAO; hPAO; po. Enzyme Commission Number: EC 1.5.3.13. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1540; N1-acetylpolyamine oxidase; EC 1.5.3.13; hPAO-1; PAO (ambiguous); mPAO; hPAO; polyamine oxidase (ambiguous). Cat No: EXWM-1540. | |
| Native Alcaligenes faecalis 3-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Is an enzyme produced by microorganisms. this product shall be used for a diag...Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Mole weight: 60±5 kDa (TSK G-3000SW); 30±5 kDa (SDS-PAGE). Activity: > 1,500 U/mg. Appearance: White powder. Storage: -20°C. Form: Freeze dried powder. Source: Alcaligenes faecalis. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0005. | |
| Native Arthrobacter ureafaciens α (2?3,6,8,9) Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Applications: Neuraminidase is an important deglycosyl... resulting in partial or complete o-deglycosylation. sds-page and maldi-tof ms are typically utilized in purification, structural analysis, and sequencing process. these techniques also remove heterogeneity and charge from the glycoprotein. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Storage: 2-8°C. Form: Lyophilized powder. Source: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0756. | |
| Native Bacillus polymyxa Neutral Protease (Dispase) | Neutral protease (Dispase) is a non-mammalian animal origin free (AOF) metallo, neutral protease. Its mild proteolytic action makes the enzyme especially suitable for the preparation of primary cells and secondary (subcultivation) cell culture, since it is gentle on cell membranes. This protease is also used as a secondary enzyme in cell isolation and tissue dissociation applications, commonly used with collagense. Chromatographically purified. a lyophilized powder. Applications: Tissue disaggregation and subcultivation; prevention of unwanted cell clumping; preparation of cells for culture; separation of intact epidermis from dermis and intact epithelial sheet in c...se; Neutral Protease (Dispase). Enzyme Commission Number: EC 3.4.24.28. CAS No. 9001-92-7. Purity: Chromatographically purified. Neutral Protease. Mole weight: 32.5 kDa. Activity: > 4 units per mg dry weight. Stability: Stable at 2-8°C for 12 months. Aliquot and Store at -20°C after reconstitution with water or commonly used balanced salt solutions or media. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bacillus polymyxa. Bacillolysin; EC 3.4.24.28; Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase; Neutral Protease (Dispase). Cat No: NATE-0482. | |
| Native Bacillus stearothermophilus Phosphofructokinase | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 ...cs reagent. Applications: Useful for enzymatic determiantion of fructose-6-phosphate. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Mole weight: 72 kDa (gel filtration); 35 kDa (SDS-PAGE). Activity: > 250 U/mg. Appearance: White to pale yellow powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilus. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: NATE-0551. | |
| Native Bovine Phenylethanolamine N-Methyl Transferase | Phenylethanolamine N-methyltransferase (PNMT) is the enzyme which catalyzes the N-methylation of norepinephrine thereby resulting in the formation of epinephrine as shown below: Norepinephrine + S-Adenosyl methionine (SAM) -------> Epinephrine. The mechanism involves transfer of an active methyl group from S-adenosylmethionine (SAM) to the primary amino group of norepinephrine. Although it is primarily localized in the adrenal medulla, PNMT activity has also been demonstrated in the brain and heart tissues of several mammalian species including humans. PNMT purified from ox, rat and rabbit adrenal medulla have molecular weights in the range of 37,000-38,000. Analys...yl-L-methionine:phenylethanolamine-N-methyltransferase; EC 2.1.1.28. Enzyme Commission Number: EC 2.1.1.28. PNMT. Mole weight: 37-38 kDa. Activity: 50-100 U/mg protein. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Bovine Adrenal Medulla. Species: Bovine. phenylethanolamine N-methyltransferase; noradrenaline N-methyltransferase; noradrenalin N-methyltransferase; norepinephrine methyltransferase; norepinephrine N-methyltransferase; phenethanolamine methyltransferase; phenethanolamine N-methyltransferase; Phenylethanolamine N-Methyl Transferase; PNMT; S-adenosyl-L-methionine:phenylethanolamine-N-methyltransferase; EC 2.1.1.28. Cat No: NATE-0871. | |
| Native Bovine Protein Phosphatase 2C | Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619. | |
| Native Calf Adenosine Deaminase | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 33 kDa (SDS-PAGE). Activity: 150~200U/mg protein. Storage: Storage: Temperature 2-8 centigrade. Source: Calf Spleen. Species: Calf. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: DIA-271. | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Mammalian Ubiquitin Conjugating Enzyme Fractions | Ubiquitin-conjugating enzymes perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. Applications: Ubiquitin conjugating enzyme fractions mammalian may be used in transferring the activated ubiquitin from e1 to the substrate through an additional high energy thiol ester intermediate e2-s-ubiquitin. ubiquitin-conjugating enzymes, also known as e2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. Group: Enzymes. Synonyms: Ubiquitin con. Ubiquitin Conjugating Enzyme. Storage: -70°C. Source: Mammalian. Ubiquitin conjugating enzymes; Ubiquitin Conjugating Enzyme Fractions; E2 enzymes; ubiquitin-carrier enzymes. Cat No: NATE-0727. | |
| Native Phosphofructokinase from Thermophillic bacteria | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation. Applications: Diagnostic tests. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: DIA-403. | |
| Native Porcine Lipoamide Dehydrogenase | Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ ? Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000. Group: Enzymes. Synonyms: NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Enzyme Commission Number: EC 1.6.4.3. LD. Mole weight: 100-114 kDa. Activity: 25 U/mg protein. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Porcine Heart. Species: Porcine. NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Cat No: NATE-0894. | |
| Native Protein Methylase II | Methylation of proteins is one of the key reactions in the post-translational modification of protein amino acid residues in the cell. It has been established that the basic and acidic amino acid residues of certain proteins are methylated in vivo. Protein methylase II methylates the free carboxyl groups of dicarboxylic acid residues in a protein molecule. Existence of this enzyme, in mammalian tissues, was first reported by Liss and Edelstein. Protein methylase II from ox brain has been purified by Iqbal and Steenson. Group: Enzymes. Synonyms: S-adenosylmethionine:protein Carboxyl O-methyltransferase; EC 2.1.1.24; Protein Methylase II. Enzyme Commission Number: EC 2.1.1.24. Protein Methylase II. S-adenosylmethionine:protein Carboxyl O-methyltransferase; EC 2.1.1.24; Protein Methylase II. Cat No: NATE-0895. | |
| Native Pseudomonas lemoignei β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3-hy...1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: > 200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sucrose, β-NAD and Tris buffer salts. Source: Pseudomonas lemoignei. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0003. | |
| Native Pseudomonas sp. Acyl-coenzyme A Synthetase | The Long chain fatty acyl-CoA synthetase enzyme is a member of the ligase family that activates the breakdown of complex fatty acids. Long chain fatty acyl-CoA synthetase plays a crucial role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. It is an enzyme present in all organisms from bacteria to Humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorpoRated in phospholipids. Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells. Applications: Acyl-coenzyme a synthetase may be used to study fatty acid metabolism and lipid metabolism. it has been used to study its interaction with fatty acid transport proteins, which has been found to be involved in the efficient cellular uptake of long-chain fatty acids in adipocyte. Group: Enzymes. Synonyms: acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. Activity: > 2 units/mg protein. Storage: -20°C. Source: Pseudomonas sp. acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synt | |
| Native Rat Histamine N-Methyl Transferase | (HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------> (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to histamine. Histamine is present in most of mammalian tissues and HNMT is the enzyme responsible for inactivation of histamine in mammals. Methylation is major route of histamine metabolism. HNMT has been used to measure histamine by radio-enzymatic method. HNMT has been purified from rat kidney. Molecular weight equals 33,400, pH optimum is 8.00-8.25. We have also purified it from bovine kidney which seems to be very similar to rat kidney. Group: Enzymes. Synonyms: Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Enzyme Commission Number: EC 2.1.1.8. CAS No. 9029-80-5. HNMT. Mole weight: 33.4 kDa. Activity: 50-100 U/mg. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Rat Kidney. Species: Rat. Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Cat No: NATE-0898. | |
| Native Rat Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| Native Rhodopseudomonas sphaeroides β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3...nase; EC 1.1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: 250-750 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rhodopseudomonas sphaeroides. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0004. | |
| Native Xanthine Dehydrogenase from Bovine milk | Xanthine oxidoreductase (XOR) catalyzes the formation of uric acid from hypoxanthine and xanthine, last two steps of purine catabolism. The mammalian enzyme is synthesized as a xanthine dehydrogenase form (XDH, EC 1.17.1.4), which uses NAD as the electron acceptor, but is converted into an xanthine oxidase form (XO, EC 1.1.3.22) by reversible (through sulfhydryl group oxidation) or irreversible (proteolysis) manner. Since most industrial protocols of XOR purification includes proteolysis step, commercial XOR enzyme is available only as oxidase form unable to use NAD as a an electron acceptor. Group: Enzymes. Synonyms: xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Form: Lyophilized. Source: Bovine milk. Species: Bovine. xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Cat No: NATE-1065. | |
| N-sulfoglucosamine-3-sulfatase | The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue. Group: Enzymes. Synonyms: chondroitinsulfatase. Enzyme Commission Number: EC 3.1.6.15. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3748; N-sulfoglucosamine-3-sulfatase; EC 3.1.6.15; chondroitinsulfatase. Cat No: EXWM-3748. | |
| oviductin | The egg envelope of the South African clawed frog (Xenopus laevis) is modified during transit of the egg through the pars rectus oviduct, changing the egg envelope from an unfertilizable form to a fertilizable form. This process involves the conversion of glycoprotein gp43 to gp41 (ZPC) by the pars recta protease oviductin. It is thought that the enzymically active protease molecule comprises the N-terminal protease domain coupled to two C-terminal CUB domains, which are related to the mammalian spermadhesin molecules implicated in mediating sperm-envelope interactions. The enzyme is also found in the Japanese toad (Bufo japonicus). Belongs in peptidase family S1. Group: Enzymes. Synonyms: oviductal protease. Enzyme Commission Number: EC 3.4.21.120. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4116; oviductin; EC 3.4.21.120; oviductal protease. Cat No: EXWM-4116. | |
| pancreatic elastase | Formed by activation of proelastase from mammalian pancreas by trypsin. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.11. Group: Enzymes. Synonyms: pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase. Enzyme Commission Number: EC 3.4.21.36. CAS No. 9004-6-2. ELA1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4130; pancreatic elastase; EC 3.4.21.36; 9004-06-2; pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase. Cat No: EXWM-4130. | |
| pancreatic elastase II | A peptidase of family S1 (trypsin family) formed by activation of proelastase II from mammalian pancreas by trypsin. Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II. Group: Enzymes. Synonyms: pancreatic elastase 2. Enzyme Commission Number: EC 3.4.21.71. CAS No. 75603-19-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4163; pancreatic elastase II; EC 3.4.21.71; 75603-19-9; pancreatic elastase 2. Cat No: EXWM-4163. | |
| peptidyl-dipeptidase B | A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence and shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II. Group: Enzymes. Synonyms: dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase. Enzyme Commission Number: EC 3.4.15.4. CAS No. 147014-93-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4054; peptidyl-dipeptidase B; EC 3.4.15.4; 147014-93-5; dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase. Cat No: EXWM-4054. | |
| phosphatidylinositol-4,5-bisphosphate 4-phosphatase | Two pathways exist in mammalian cells to degrade 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P2]. One is catalysed by this enzyme and the other by EC 3.1.3.36, phosphoinositide 5-phosphatase, where the product is PtdIns4P. The enzyme from human is specific for PtdIns(4,5)P2 as substrate, as it cannot use PtdIns(3,4,5)P3, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns5P, PtdIns4P or PtdIns3P. In humans, the enzyme is localized to late endosomal/lysosomal membranes. It can control nuclear levels of PtdIns5P and thereby control p53-dependent apoptosis. Group: Enzymes. Synonyms: phosphatidylinositol-4,5-bisphosphate 4-phosphatase I; phosphatidylinositol-4,5-bisphosphate 4-phosphatase II; type I PtdIns-4,5-P2 4-Ptase; type II PtdIns-4,5-P2 . Enzyme Commission Number: EC 3.1.3.78. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3683; phosphatidylinositol-4,5-bisphosphate 4-phosphatase; EC 3.1.3.78; phosphatidylinositol-4,5-bisphosphate 4-phosphatase I; phosphatidylinositol-4,5-bisphosphate 4-phosphatase II; type I PtdIns-4,5-P2 4-Ptase; type II PtdIns-4,5-P2 4-Ptase; IpgD; PtdIns-4,5-P2 4-phosphatase type I; PtdIns-4,5-P2 4-phosphatase type II; type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase; type 1 4-phosphatase. Cat No: EXWM-3683. | |
| polyprenol reductase | The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length. Group: Enzymes. Synonyms: SRD5A3 (gene name); DFG10 (gene name). Enzyme Commission Number: EC 1.3.1.94. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1364; polyprenol reductase; EC 1.3.1.94; SRD5A3 (gene name); DFG10 (gene name). Cat No: EXWM-1364. | |
| quinol-cytochrome-c reductase | The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase). Group: Enzymes. Synonyms: ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitocho. Enzyme Commission Number: EC 1.10.2.2. CAS No. 9027-3-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0474; quinol-cytochrome-c reductase; EC 1.10.2.2; 9027-03-6; ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxido | |
| Recombinant Adenosine deaminase from Pseudomonas aeruginosa | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. Purity: > 80 %. ADA. Mole weight: 36 kDa. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: Pseudomonas aeruginosa. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1010. | |
| Ribonuclease T2 from Aspergillus oryzae, Recombinant | Aspergillus oryzae Ribonuclease T2 is a member of the RNase T2 family of endonucleases that are present in a wide variety of microbial, plant and animal species. In contrast to Aspergillus oryzae Ribonuclease T1, which is an exclusively guanylic-acid specific endonuclease, all RNase T2-like enzymes are essentially base non-specific. However, RNase T2 endonucleases from different species can show slight base preferences. The fungal enzymes, including Aspargillus oryzae RNaseT2, show slight base preference in the following order: A>G>C, U. RNase T2 cleaves between the 3-phosphate residue of one base and the 5-OH residue of the adjacent nucleotide forming a 2, 3-cyclic phosphate intermediate followed by the generation of oligonucleotides with 3-phosphate residues. This enzyme is also used as a non-mammalian source of RNase in various applications. Group: Enzymes. Synonyms: Ribonuclease T2; RNase T2; Ribonuclease. Enzyme Commission Number: EC 3.1.27.1. Rnase. Mole weight: 36 kDa. Activity: ≥10,000 units per mg protein. Stability: Stable at 12-18 months at 2-8°C. Storage: Store at 2-8°C. Form: Lyophilized powder. Source: Pichia pastoris. Species: Aspergillus oryzae. Ribonuclease T2; RNase T2; Ribonuclease. Cat No: NATE-1930. | |
| spermine oxidase | The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase). Group: Enzymes. Synonyms: PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu. Enzyme Commission Number: EC 1.5.3.16. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1543; spermine oxidase; EC 1.5.3.16; PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu. Cat No: EXWM-1543. | |
| Superoxide Dismutase from Bovine, Recombinant | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Sod from bovine erythr ocytes was the first sod to be found in mammalian tissues. before its enzymatic activity was disc...Superoxide dismutase has been used in a study to investigate where lipoproteins may affect the l-arginine-nitric oxide pathway. superoxide dismutase has also been used in a study to investigate the mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human cu, zn superoxide dismutase. the product has been used to develop an sod assay. this assay used dismutase-mediated inhibition of nadh-dependent nitroblue tetrazolium reduction. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; s | |
| t-plasminogen activator | A peptidase of family S1 (trypsin family) from a wide variety of mammalian tissues, especially endothelial cells. Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin. Activity is considerably enhanced by fibrin. Formerly included in EC 3.4.21.31 and EC 3.4.99.26. Group: Enzymes. Synonyms: tissue plasminogen activator; plasminogen activator, tissue-type; tissue-type plasminogen activator; tPA; t-PA. Enzyme Commission Number: EC 3.4.21.68. CAS No. 139639-23-9. tPA. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4159; t-plasminogen activator; EC 3.4.21.68; 139639-23-9; tissue plasminogen activator; plasminogen activator, tissue-type; tissue-type plasminogen activator; tPA; t-PA. Cat No: EXWM-4159. | |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| xanthine oxidase | An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: hypoxanthine o. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1088; xanthine oxidase; EC 1.17.3.2; 9002-17-9; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: EXWM-1088. | |
| 17β-estradiol 17-dehydrogenase | The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+. Group: Enzymes. Synonyms: 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Enzyme Commission Number: EC 1.1.1.62. CAS No. 9028-61-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0348; 17β-estradiol 17-dehydrogenase; EC 1.1.1.62; 9028-61-9; 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Cat No: EXWM-0348. | |
| 1,8-cineole 2-exo-monooxygenase | A heme-thiolate protein (P-450). The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. cf. EC 1.14.13.97 (taurochenodeoxycholate 6-hydroxylase), EC 1.14.13.67 (quinine 3-monooxygenase) and EC 1.14.13.32 (albendazole monooxygenase). Group: Enzymes. Synonyms: CYP3A4. Enzyme Commission Number: EC 1.14.13.157. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0757; 1,8-cineole 2-exo-monooxygenase; EC 1.14.13.157; CYP3A4. Cat No: EXWM-0757. | |
| 3α-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3α-hydroxysteroids, such as androsterone and 5 α-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific)]. Group: Enzymes. Synonyms: 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Enzyme Commission Number: EC 1.1.1.357. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0273; 3α-hydroxysteroid 3-dehydrogenase; EC 1.1.1.357; 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Cat No: EXWM-0273. | |
| 3β-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase. Group: Enzymes. Synonyms: 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Enzyme Commission Number: EC 1.1.1.270. CAS No. 42616-29-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0177; 3β-hydroxysteroid 3-dehydrogenase; EC 1.1.1.270; 42616-29-5; 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Cat No: EXWM-0177. | |
| 3-oxo-5α-steroid 4-dehydrogenase (NADP+) | The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor). Group: Enzymes. Synonyms: cholestenone 5α-reductase; testosterone Δ4-5&. Enzyme Commission Number: EC 1.3.1.22. CAS No. 37255-34-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1297; 3-oxo-5α-steroid 4-dehydrogenase (NADP+); EC 1.3.1.22; 37255-34-8; cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase. Cat No: EXWM-1297. | |
| 4-α-glucanotransferase | This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase). Group: Enzymes. Synonyms: disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Amylomaltase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2479; 4-α-glucanotransferase; EC 2.4.1.25; 9032-09-1; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Cat No: EXWM-2479. | |
| 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside | 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside is a compound widely used in the biomedical industry as an artificial chromogenic substrate. It is primarily employed in the detection and visualization of β-D-glucosidase enzyme activity. This compound finds applications in various biochemical assays, including determination of bacterial and mammalian β-D-glucosidase levels, providing valuable insights into drug discovery and disease research. Synonyms: X-Mannose. CAS No. 129787-67-3. Molecular formula: C14H15BrClNO6. Mole weight: 408.63. | |
| 5-Hydroxymethylcytosine | 5-Hydroxymethylcytosine (5hmC) is an oxidized forms of 5-methylcytosine (5mC) in mammalian DNA. 5-Hydroxymethylcytosine is produced from 5mC in an enzymatic pathway involving three 5mC oxidases, Ten-eleven translocation (TET)1, TET2, and TET3. The conversion of 5mC into 5hmC can be the first step in a pathway leading towards DNA demethylation. 5-Hydroxymethylcytosine is associated with gene transcription and frequently used as a mark to investigate dynamic DNA methylation conversion during mammalian development [1]. Uses: Scientific research. Group: Natural products. Alternative Names: 5hmC. CAS No. 1123-95-1. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-W018324. |  |
| 6-Chloro-5-(2,3-dichlorophenoxy)-2-methylthio-benzimidazole (Triclabendazole) | Triclabendazole is a member of the benzimidazole family of anthelmintics. It is effective against F. hepatica helminths that cause fascioliasis, reducing secreted protease enzyme activities that are critical for the invasion, migration, nutrition, and survival of the parasite.1 In yeast and mammalian cells, triclabendazole was shown to inhibit adenylyl cyclase in the Ras-adenylyl cyclase-protein kinase A nutrient-sensing pathway and to prevent apoptosis induced by the Parkinsons disease-related protein α-synuclein, demonstrating a protective role during various cellular stresses.2,3. Group: Biochemicals. Alternative Names: 5-Chloro-6- (2, 3-dichlorophenoxy) -2- methyl thiobenzimidazole; CGA-89317, egaten; Fasinex; Triclabendazole. Grades: Highly Purified. CAS No. 68786-66-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C14H9Cl3N2OS, Molecular Weight: 359.66. US Biological Life Sciences. | Worldwide |
| 7, 12-Dimethylbenz [a]anthracene | A highly potent carcinogen that is activated by microsomal enzymes to a diol epoxide metabolite that binds covalently to DNA in mammalian cells, leading ultimately to tumor induction. Group: Biochemicals. Grades: Highly Purified. CAS No. 57-97-6. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| 8R-Brassicasterol | 8R-Brassicasterol is a by-product in the synthesis of Brassicasterol (B676850). Brassicasterol is a phytosterol found in canola oil, rapeseed oil, marine algae and shellfish. This compound has been shown to inhibit sterol Δ24-reductase, an enzyme involved in the mammalian cholesterol biosynthesis pathway. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C28H46O. US Biological Life Sciences. | Worldwide |
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