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| Product | Description | |
|---|---|---|
| 1H-1,2,4-Triazol-3-amine | 1H-1,2,4-Triazol-3-amine consists of a triazole ring system and an amino group attached to carbon atom 3. The compound has potential applications in various fields such as medicinal chemistry, agrochemicals and material science. In medicinal chemistry, 1H-1,2,4-Triazol-3-amine is used as a starting material for the synthesis of pharmaceutical compounds such as antifungal agents, anticancer agents, and enzyme inhibitors associated with cardiovascular disease. In agrochemicals, it can be used as a raw material for the synthesis of herbicides, fungicides and insecticides. Furthermore, 1H-1,2,4-Triazol-3-amine is used as a ligand in coordination chemistry and as a precursor for the production of new functional materials such as polymers and metal-organic frameworks. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 61-82-5. Pack Sizes: 10 g; 25 g. Product ID: HY-W027592. |  |
| 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase | The enzyme is involved in the detoxification of the benzoxazinoids DIBOA (2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one) and DIMBOA (2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) which are stored as the respective non-toxic glucosides in the vacuoles in some plants, most commonly from the family of Poaceae (grasses). Benzoxazinoids are known to exhibit antimicrobial, antifeedant, and antiinsecticidal effects and are involved in the interaction of plants with other plants, insects, or microorganisms. Group: Enzymes. Synonyms: uridine diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-glucosyltransferase; BX8; BX9; benzoxazinoid glucosyltransferase; DIMBOA glucosyltransferase. Enzyme Commission Number: EC 2.4.1.202. CAS No. 122544-56-3. 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-2430; 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase; EC 2.4.1.202; 122544-56-3; uridine diphosphoglucose-2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-glucosyltransferase; BX8; BX9; benzoxazinoid glucosyltransferase; DIMBOA glucosyltransferase. Cat No: EXWM-2430. |  |
| 5-Lipoxygenase from human, Recombinant | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is an enzyme that in humans is encoded by the ALOX5 gene. Arachidonate 5-lipoxygenase is a member of the lipoxygenase family of enzymes. It transforms EFAs into leukotrienes and is a current target for pharmaceutical intervention in a number of diseases. Group: Enzymes. Synonyms: Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Enzyme Commission Number: EC 1.13.11.34. CAS No. 80619-02-9. Lipoxygenase. Mole weight: 78 kDa. Activity: 1,259.96 U/ml. Stability: As supplied, 6 months from the QC date provided on the Certificate of Analysis, when stored properly. Storage: at -80°C. Form: A solution in 100 mM Tris-HCl, pH 8.0, containing 5 mM EGTA, 1mM CaCl2, and 30% glycerol. Source: S9 insect cells. Species: Human. Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Cat No: NATE-1249. | |
| Active Focal Adhesion Kinase from Human, Recombinant | FAK is a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-le...Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Enzyme Commission Number: EC 2.7.10.2. Purity: Greater than 70% as determined by SDS-PAGE. FAK. Mole weight: 146.7 kDa. Activity: 72 nmole of phosphate transferred to poly [Glu,Tyr] 4:1 substrate/minute/mg of total protein at 30°C. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C to -80°C for longer periods of time. Avoid multiple freeze-thaw cycles. Source: Baculovirus, SF9 insect cells. Species: Human. Focal adhesion kinase 1; EC 2.7.10.2; FADK 1; pp125FAK; Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Cat No: NATE-0800. | |
| Alkaline phosphatase from Mouse, Recombinant | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Group: Enzymes. Synonyms: Alpl; Akp-2; Akp2; ALP; APTNAP; TNAP; TNSALP; HOPS; tissue-nonspecific isozyme. Enzyme Commission Number: EC 3.1.3.1. Purity: > 95% by SDS-PAGE. ALP. Mole weight: 54.5 kDa. Activity: > 46,000 pmol/min/ug. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: Insect cell (Baculovirus) and fused to His-tag at C-terminus. Species: Mouse. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase; Alpl; Akp-2; Akp2; APTNAP; TNAP; TNSALP; HOPS; tissue-nonspecific isozyme. Cat No: NATE-1634. | |
| Amitraz | Amitraz is an antiparasitic used to control red spider mites, leaf miners and scale insects. This compound is active by inhibiting the targets monoaminooxidase enzyme. Group: Biochemicals. Alternative Names: N'- (2, 4-Dimethylphenyl) -N-[[ (2, 4-dimethylphenyl) imino]methyl]-N-methyl-methanimidamide; N-Methyl-N'-2, 4-xylyl-N- (N-2, 4-xylylformimidoyl) formamidine; Acarac; Amigard; Apivar ND; Azaform; BAAM; Ovasyn; Parsec; TCL; Taktic; Triazid; U 36059; Varamit. Grades: Highly Purified. CAS No. 33089-61-1. Pack Sizes: 100mg. US Biological Life Sciences. |  Worldwide |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| Carboxylesterase 1D from Mouse, Recombinant | Ces1d, also known as carboxylesterase 1D, is a member of a large family of carboxylesterases that are responsible for the hydrolysis of ester and amide bonds. It is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity as well as lesser but detectable neutral cholesteryl ester hydrolase activity. The protein shows low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics. Recombinant mouse Ces1d, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Ces1d; Carboxylesterase 3; FAEE synthase; TGH; Ces3. Purity: > 90% by SDS-PAGE. Esterase. Mole weight: 60.9 kDa. Activity: > 80,000 pmol/min/ug. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: Insect cell (Baculovirus) and fused to His-tag at N-terminus. Species: Mouse. Ces1d; Carboxylesterase 3; FAEE synthase; TGH; Ces3; Carboxylesterase 1D. Cat No: NATE-1633. | |
| Carboxylesterase 1 isoform b from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥500 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxyl | |
| Carboxylesterase 1 isoform c from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic...er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥1000 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxy | |
| carotenoid isomerooxygenase | The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule. Group: Enzymes. Synonyms: ninaB (gene name). Enzyme Commission Number: EC 1.13.11.65. 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-0585; carotenoid isomerooxygenase; EC 1.13.11.65; ninaB (gene name). Cat No: EXWM-0585. | |
| Catalase from bovine liver | Catalase from bovine liver. Synonyms: H2O2:H2O2 oxidoreductase. CAS No. 9001-5-2. Product ID: CDC10-0039. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; Catalase from bovine liver; CDC10-0039; 9001-05-2; H2O2:H2O2 oxidoreductase; MFCD00081483; 9001-05-2. Physical State: aqueous suspension. Quality Level: 200. Storage: 2-8°C. Application: Catalase from bovine liver has been used for measuring the hydrogen peroxide conetent in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity. Density: 1.06 g/mL at 20 °C. Product Description: Catalase from bovine liver contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region. |  |
| Cedrol | Cedrol is a bioactive sesquiterpene, a potent competitive inhibitor of cytochrome P-450 (CYP) enzymes. Cedrol inhibits CYP2B6-mediated bupropion hydroxylase and CYP3A4-mediated midazolam hydroxylation with Ki of 0.9 μM and 3.4 μM, respectively. Cedrol also has weak inhibitory effect on CYP2C8, CYP2C9, and CYP2C19 enzymes. Cedrol is found in cedar essential oil and poetesses anti-septic, anti-inflammatory, anti-spasmodic, tonic, astringent, diuretic, insecticidal, and anti-fungal activities. Group: Inhibitors. Alternative Names: Cypress camphor. CAS No. 77-53-2. Molecular formula: C15H26O. Mole weight: 222.37. Appearance: Pale yellow to yellow green solid. Purity: 0.99. IUPACName: (1S, 2R, 5S, 7R, 8R)-2, 6, 6, 8-Tetramethyltricyclo[5.3.1.01, 5]undecan-8-ol. Canonical SMILES: CC1CCC2C13CCC(C(C3)C2(C)C)(C)O. Density: 0.9479 g/cm³. Catalog: ACM77532. |  |
| Chlorpyrifos-d10 | Chlorpyrifos-d 10 is the deuterium labeled Chlorpyrifos. Chlorpyrifos is an organophosphate insecticide that is classified as a phosphorothionate. The oxon metabolite of Chlorpyrifos is an inhibitor of acetylcholinesterase (AChE), affecting neurological function in insects, humans, and other animals. The Chlorpyrifos oxon (CPO) metabolite is hydrolyzed by the plasma enzyme paraoxonase 1 (PON1), and susceptibility to neurotoxicity associated with CPO exposure is mitigated by PON1 overexpression. Uses: Scientific research. Group: Isotope-labeled compounds. CAS No. 285138-81-0. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-B0815S. | |
| cholesterol 7-desaturase | The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase. In insects it participates in the the biosythesis of ecdysteroid hormones. The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin. The enzyme differs from regular desaturases, such as EC 1.14.19.20, 7-sterol 5(6)-desaturase, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases. Group: Enzymes. Synonyms: nvd (gene name); daf-36 (gene name). Enzyme Commission Number: EC 1.14.19.21. 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-0984; cholesterol 7-desaturase; EC 1.14.19.21; nvd (gene name); daf-36 (gene name). Cat No: EXWM-0984. | |
| chrysanthemyl diphosphate synthase | Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+. Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums. Group: Enzymes. Synonyms: CPPase. Enzyme Commission Number: EC 2.5.1.67. 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-2804; chrysanthemyl diphosphate synthase; EC 2.5.1.67; CPPase. Cat No: EXWM-2804. | |
| cis-Permethrin | cis-Permethrin is the cis-isomer of Permethrin, which is a medication and an insecticide used to treat scabies and lice. Uses: Enzyme inhibitors. Synonyms: Cyclopropanecarboxylic acid, 3-(2,2-dichloroethenyl)-2,2-dimethyl-, (3-phenoxyphenyl)methyl ester, (1R,3R)-rel-; Cyclopropanecarboxylic acid, 3-(2,2-dichloroethenyl)-2,2-dimethyl-, (3-phenoxyphenyl)methyl ester, cis-; (±)-cis-FMC 33297; (±)-cis-Permethrin; 1RS,cis-Permethrin; Cispermethrin; FMC 35171; NRDC 148. Grades: 98%. CAS No. 61949-76-6. Molecular formula: C21H20Cl2O3. Mole weight: 391.29. |  |
| Cytochrome P450 Reductase from Human, Recombinant | Cytochrome P450 reductase is a membrane bound enzyme required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. The cytochrome P450 enzyme system is mainly involved in the detoxification of xenobiotics in the liver. It also participates in the activation of procarcinogens and the metabolism of endogeneous substrates such as steroids. Applications: Human cytochrome p450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat. human cytochrome p450 reductase has also been u...AD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-3-4. Purity: >90% (SDS-PAGE). CPR. Mole weight: 76.5 kDa. Activity: >30 U/mg. Storage: Store at -70°C. Form: Supplied in a solution containing 10 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.5 mM DTT, 20% (v/v) glycerol. Source: Baculovirus infected insect cells. Species: Human. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-1586. | |
| dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase | The enzyme was isolated from the bacterium Saccharopolyspora spinosa, where it is involved in the biosynthesis of spinosyn A, an active ingredient of several commercial insecticides. Group: Enzymes. Synonyms: SpnS; TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase. Enzyme Commission Number: EC 2.1.1.324. 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-1932; dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase; EC 2.1.1.324; SpnS; TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase. Cat No: EXWM-1932. | |
| (E)-β-ocimene synthase | Widely distributed in plants, which release β-ocimene when attacked by herbivorous insects. Group: Enzymes. Synonyms: β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS. Enzyme Commission Number: EC 4.2.3.106. 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-5117; (E)-β-ocimene synthase; EC 4.2.3.106; β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS. Cat No: EXWM-5117. | |
| ecdysone 20-monooxygenase | An enzyme from insect fat body or malpighian tubules involving a heme-thiolate protein (P-450). NADPH can act as ultimate hydrogen donor. Group: Enzymes. Synonyms: α-ecdysone C-20 hydroxylase; ecdysone 20-hydroxylase. Enzyme Commission Number: EC 1.14.99.22. CAS No. 55071-97-1. 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-1040; ecdysone 20-monooxygenase; EC 1.14.99.22; 55071-97-1; α-ecdysone C-20 hydroxylase; ecdysone 20-hydroxylase. Cat No: EXWM-1040. | |
| Elymoclavine | Elymoclavine is a chemical compound that has been shown to inhibit the enzyme activities of 5-HT2A receptors, which are involved in the transmission of nerve impulses. It also inhibits ergovaline and pergolide mesylate, two amines that are found in perennial ryegrass and have been shown to be toxic to humans. Elymoclavine is a synthetic pathway intermediate and belongs to the class of phytochemicals. It has been shown to have insecticidal activity against insects such as Drosophila melanogaster and Spodoptera littoralis. Elymoclavine has also been shown to have dopamine-like effects on human erythrocytes. Group: Other alkaloids. CAS No. 548-43-6. Molecular formula: C16H18N2O. Mole weight: 254.33 g/mol. Canonical SMILES: CN1CC (=C[C@H]2[C@H]1CC3=CNC4=CC=CC2=C34) CO. Catalog: ACM548436. | |
| endo-1,4-β-Xylanase from Clostridium thermocellum, Recombinant | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-&. Enzyme Commission Number: EC 3.2.1.8. CAS No. 9025-57-4. Purity: > 95 % as judged by SDS-PAGE. Xylanase. Mole weight: 39474.6 Da. Activity: 2500 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium thermocellum. EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Cat No: NATE-1202. | |
| Endotoxin free Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. this product is suitable for cell culture use. Group: Enzymes. Synonyms: transglutaminase; ...rand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is supplied in 10 mM Tris-HCl pH 7.2, 150 mM NaCl, 0.5 mM EDTA, 0.5 mM DTT, 10% Glycerol. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. Cat No: NATE-1729. | |
| farnesal dehydrogenase | Invoved in juvenile hormone production in insects. The enzyme was described from the corpora allata of Drosophila melanogaster (fruit fly), Manduca sexta (tobacco hornworm) and Aedes aegypti (dengue mosquito). Group: Enzymes. Synonyms: AaALDH3. Enzyme Commission Number: EC 1.2.1.94. 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-1198; farnesal dehydrogenase; EC 1.2.1.94; AaALDH3. Cat No: EXWM-1198. | |
| fucosterol-epoxide lyase | The insect enzyme is involved in the conversion of sitosterol into cholesterol. Group: Enzymes. Synonyms: (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase; (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming). Enzyme Commission Number: EC 4.1.2.33. CAS No. 99676-42-3. 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-4870; fucosterol-epoxide lyase; EC 4.1.2.33; 99676-42-3; (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase; (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming). Cat No: EXWM-4870. | |
| Geranylgeranyltransferase from rat, Recombinant | Geranylgeranyltransferase type 1 or simply geranylgeranyltransferase is one of the three enzymes in the prenyltransferase group. In specific terms, Geranylgeranyltransferase (GGTase 1) adds a 20-carbon isoprenoid called a geranylgeranyl group to proteins bearing a CaaX motif:a four-amino acid sequence at the carboxyl terminal of a protein. Geranylgeranyltransferase inhibitors are being investigated as anti-cancer agents. >80% (sds-page), recombinant, expressed in baculovirus infected insect cells, > 200 units/mg protein. Group: Enzymes. Synonyms: geranylgeranyltransferase type I; GGTase-I; GGTase; 160141-09-3; Geranylgeranyltransferase. CAS No. 160141-09-3. Purity: >80% (SDS-PAGE). GGTase. Mole weight: mol wt 43 kDa (β subunit); mol wt 48 kDa (α subunit). Activity: > 200 units/mg protein. Stability: -70°C. Form: Solution. Source: baculovirus infected insect cells. Species: Rat. geranylgeranyltransferase type I; GGTase-I; GGTase; 160141-09-3; Geranylgeranyltransferase. Cat No: NATE-0285. | |
| glycerol-3-phosphate dehydrogenase | This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain.This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9. The enzyme is activated by calcium. Group: Enzymes. Synonyms: α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenas | |
| glycoprotein 3-α-L-fucosyltransferase | Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-α-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-β-L-fucose to form an α1,3-linkage rather than an α1,6-linkage. The N-glycan products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea). Group: Enzymes. Synonyms: GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1?6GlcNAc)-Asn-peptide) α1?3-fucosyltransferase; GDP-L-fucose:glycoprotein (L-fucose to asparagine-. Enzyme Commission Number: EC 2.4.1.214. CAS No. 68247-53-0. α-fucosyltransferase. 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-2442; glycoprotein 3-α-L-fucosyltransferase; EC 2.4.1.214; 68247-53-0; GDP-L-Fuc:N-acetyl-β-D-glucosaminide α1,3-fucosyltransferase; GDP-L-Fuc:Asn-linked GlcNAc α1,3-fucosyltransferase; GDP-fucose:β-N-acetylglucosamin | |
| Hck from Human, Recombinant | Hck is a member of the Src family of non-receptor associated protein tyrosine kinases (PTK). Hck has been shown to associate with and be activated by Bcr-Abl, which is a protein-tyrosine kinase that is expressed in chronic myelogenous leukemia. Group: Enzymes. Synonyms: Hck; HCK; tyrosine-protein kinase HCK; JTK9; p59Hck; p61Hck. Hck. Mole weight: mol wt 58 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris pH 7.5, containing 0.05 mM EDTA, 1mM DTT, 100 mM NaCl, 0.05% NP-40, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. Hck; HCK; tyrosine-protein kinase HCK; JTK9; p59Hck; p61Hck. Cat No: NATE-0334. | |
| Immobilized human urokinase | Immobilized human two-chain HMW urokinase is ideal for the controlled activation of plasminogen to plasmin. After the activation is complete, the resin is simply removed and the reaction is quenched. May be used to immunopurify monoclonal and polyclonal antibodies directed against human urokinase. May be used repeatedly. Group: Enzymes. Synonyms: Urokinase; EC 3. 4. 21. 73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Enzyme Commission Number: EC 3. 4. 21. 73. Purity: >95% by SDS-PAGE analysis. Mole weight: 54000. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Insect cell culture. Species: Human. Urokinase; EC 3. 4. 21. 73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator; Immobilized uPA; Immobilized urokinase. Cat No: NATE-1759. | |
| indole-3-glycerol-phosphate lyase | Forms part of the defence mechanism against insects and microbial pathogens in the grass family, Gramineae, where it catalyses the first committed step in the formation of the cyclic hydroxamic acids 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA) and 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one (DIMBOA). This enzyme resembles the α-subunit of EC 4.2.1.20, tryptophan synthase, for which, (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate is also a substrate, but, unlike tryptophan synthase, its activity is independent of the β-subunit and free indole is released. Group: Enzymes. Synonyms: tryptophan synthase α; TSA; indoleglycerolphosphate aldolase; indole glycerol phosphate hydrolase; indole synthase; indole-3-glycerolphosphate D-glyceraldehyde-3-pho. Enzyme Commission Number: EC 4.1.2.8. CAS No. 9014-52-2. 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-4896; indole-3-glycerol-phosphate lyase; EC 4.1.2.8; 9014-52-2; tryptophan synthase α; TSA; indoleglycerolphosphate aldolase; indole glycerol phosphate hydrolase; indole synthase; indole-3-glycerolphosphate D-glyceraldehyde-3-phosphate-lyase; indole-3-glycerol phosphate lyase; IGL; BX1; (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate D-glyceraldehyde-3-phosphate-lyase. Cat No: EXWM-4896. | |
| Insulin Degrading Enzyme (HisoTag) from Rat, Recombinant | Insulin Degrading Enzyme (IDE) is a large zinc-binding protease of the M16A metalloprotease subfamily known to cleave multiple short polypeptides that vary considerably in sequence. IDE was first identified by its ability to degrade the B chain of the hormone insulin. This activity was observed over sixty years ago, though the enzyme specifically responsible for B chain cleavage was identified more recently. This discovery revealed considerable amino acid sequence similarity between IDE and the previously characterized bacterial protease pitrilysin, suggesting a common proteolytic mechanism. Recombinant, rat insulin degrading enzyme fused to a hisotag sequence and expressed in s. frugiperda insect cells. a metalloprotease that degrades insulin and a variety of other peptides including amyloid peptides. Group: Enzymes. Synonyms: IDE; Insulin-degrading enzyme; insulysin; insulin protease. Enzyme Commission Number: EC 3.4.24.56. Purity: >90% by SDS-PAGE. IDE. Mole weight: 110 kDa. Activity: >3 U/mg protein. Storage: < -70°C. Form: Liquid. Source: S. frugiperda. Species: Rat. IDE; Insulin-degrading enzyme; insulysin; insulin protease. Cat No: NATE-0849. | |
| ipsdienol synthase | A cytochrome P-450 heme-thiolate protein. Involved in the insect aggregation pheromone production. Isolated from the pine engraver beetle, Ips pini. A small amount of (S)-ipsdienol is also formed. In vitro it also hydroxylated (+)- and (-)-α-pinene, 3-carene, and (+)-limonene, but not α-phellandrene, (-)-β-pinene, γ-terpinene, or terpinolene. Group: Enzymes. Synonyms: myrcene hydroxylase; CYP9T2; CYP9T3. Enzyme Commission Number: EC 1.14.14.31. 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-0929; ipsdienol synthase; EC 1.14.14.31; myrcene hydroxylase; CYP9T2; CYP9T3. Cat No: EXWM-0929. | |
| Isoprocarb | Isoprocarb is a non-systematic carbamate insecticide. Isoprocarb functions by reversibly inactivating the enzyme acetylcholinesterase in insects. Group: Biochemicals. Alternative Names: 2-(1-Methylethyl)phenol 1-(N-methylcarbamate); 2-Isopropylphenyl N-Methylcarbamate; 2-Isopropylphenyl Methylcarbamate; BAY 39731; ENT 25670; Etrofolan; MIPC; Mipcin; Mipcine; NSC 191479; OMS 32; PPC 3; Ro 7-5050; o-Cumenyl N-Methylcarbamate; o-Cumenyl Methylcarbamate; o-Isopropylphenol Methylcarbamate. Grades: Highly Purified. CAS No. 2631-40-5. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| juvenile-hormone esterase | Demethylates the insect juvenile hormones JH1 and JH3, but does not hydrolyse the analogous ethyl or isopropyl esters. Group: Enzymes. Synonyms: JH-esterase; juvenile hormone analog esterase; juvenile hormone carboxyesterase; methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase. Enzyme Commission Number: EC 3.1.1.59. CAS No. 50812-15-2. 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-3487; juvenile-hormone esterase; EC 3.1.1.59; 50812-15-2; JH-esterase; juvenile hormone analog esterase; juvenile hormone carboxyesterase; methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase. Cat No: EXWM-3487. | |
| juvenile hormone-III synthase | The enzyme, found in insects, is involved in the synthesis of juvenile hormone III, a sesquiterpenoid that regulates several processes including embryonic development, metamorphosis, and reproduction, in many insect species. Group: Enzymes. Synonyms: farnesoic acid methyltransferase; juvenile hormone acid methyltransferase; JHAMT. Enzyme Commission Number: EC 2.1.1.325. 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-1933; juvenile hormone-III synthase; EC 2.1.1.325; farnesoic acid methyltransferase; juvenile hormone acid methyltransferase; JHAMT. Cat No: EXWM-1933. | |
| methyl farnesoate epoxidase | A heme-thiolate protein (cytochrome P-450). The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.13.203, farnesoate epoxidase). Group: Enzymes. Synonyms: CYP15A1. Enzyme Commission Number: EC 1.14.13.202. 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-0804; methyl farnesoate epoxidase; EC 1.14.13.202; CYP15A1. Cat No: EXWM-0804. | |
| methyltransferase cap1 | This enzyme catalyses the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules, which may be either guanosine or adenosine. This methylation event is known as cap1, and occurrs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine. Group: Enzymes. Synonyms: messenger ribonucleate nucleoside 2'-methyltransferase; messenger RNA (nucleoside-2'-)-methyltransferase; MTR1; cap1-MTase; mRNA (nucleoside-2'-O)-methyltransferase (ambiguous); S-adenosyl-L-methionine:mRNA (nucleoside-2'-O)-methyltransferase. Enzyme Commission Number: EC 2.1.1.57. CAS No. 61970-02-3. 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-1959; methyltransferase cap1; EC 2.1.1.57; 61970-02-3; messenger ribonucleate nucleoside 2'-methyltransferase; messenger RNA (nucleoside-2'-)-methyltransferase; MTR1; cap1-MTase; mRNA (nucleoside-2'-O)-methyltransferase (ambiguous); S-adenosyl-L-methionine:mRNA (nucleoside-2'-O)-methyltransferase. Cat No: EXWM-1959. | |
| methyltransferase cap2 | The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream purine ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency. Group: Enzymes. Synonyms: MTR2; cap2-MTase; mRNA (nucleoside-2'-O)-methyltransferase (ambiguous). Enzyme Commission Number: EC 2.1.1.296. 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-1903; methyltransferase cap2; EC 2.1.1.296; MTR2; cap2-MTase; mRNA (nucleoside-2'-O)-methyltransferase (ambiguous). Cat No: EXWM-1903. | |
| Monoamine Oxidase A from Human, Recombinant | MAO's are proteins of the mitochondrial membrane. These enzymes are responsible for catalyzing oxidative deamination of endo-and xenobiotic amines. Substrate specificity differs for each isozyme. Monoamine oxidase a contains binding sites for 8α-s-cysteinyl-fad. Applications: Monoamine oxidase a has been used in a study to assess abnormal behavior in a large kindred of males where a deficiency of enzymatic activity of monamine oxidase a was found. it has also been used in a study to investigate an ass ociation between smoking and the inhibition of maoa. Group: Enzymes. Synonyms: MAO-A; MAOA; EC 1.4.3.4; Monoamine Oxidase A; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreducta. Enzyme Commission Number: EC 1.4.3.4. CAS No. 231-791-2. Monoamine Oxidase. Storage: -70°C. Source: Baculovirus infected BTI insect cells. Species: Human. MAO-A; MAOA; EC 1.4.3.4; Monoamine Oxidase A; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase. Cat No: NATE-0440. | |
| Monoamine Oxidase B from Human, Recombinant | MAO's are proteins of the mitochondrial membrane. These enzymes are responsible for catalyzing oxidative deamination of endo-and xenobiotic amines. Substrate specificity differs for each isozyme. Monoamine oxidase b is a mit ochondrial outermembrane flavoenzyme that is a target for antidepressant and neuroprotective drugs. Applications: Drugs that inhibit monoamine oxidase b activity are used for the treatment of various neurological disorders including depression. monoamine oxidase b has been used in a study to assess the effect of age in 23 different regions of the human brain. it has also been used in a study to determine the specific l ocations of monoamine oxidase in the human brain. Group: Enzymes. Synonyms: MAO-B; MAOB; EC 1.4.3.4; Monoamine Oxida. Enzyme Commission Number: EC 1.4.3.4. CAS No. 231-791-2. Monoamine Oxidase. Storage: -70°C. Source: Baculovirus infected BTI insect cells. Species: Human. MAO-B; MAOB; EC 1.4.3.4; Monoamine Oxidase B; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase. Cat No: NATE-0441. | |
| Native Aspergillus niger Glucose Oxidase | The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. Glucose oxidase from aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kda each. each subunit contains one flavin adenine dinulceotide moiety and one iron. the enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. the enzyme also contains 3 cysteine residues and 8 potential sites for n-linked ...xidase oxidizes β-d-glucose to d-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. although glucose oxidase is specific for β-d-glucose, solutions of d-glucose can be quantified as α-d-glucose will mutorotate to β-d-glucose as the β-d-glucose is consumed by the enzymatic reaction. Applications: Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxi | |
| Native Aspergillus sp. Glucose Oxidase | The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. Applications: This enzyme is useful for enzymatic determination of glucose, and for amylase-activity assay when coupled with α-glucosidase in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; 9001-37-0; glucose oxidas. Enzyme Commission Number: EC 1.1.3.4. CAS No. 9001-37-0. Mole weight: approx. 153 kDa. Activity: 100U/mg-solid or more (containing approx. 50% of stabilizers). Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Aspergillus sp. EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; 9001-37-0; glucose oxidase enzyme; GOx; notatin; glucose oxidase. Cat No: DIA-193. | |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711. | |
| Native Cucumis melo α-Galactosidase I, Alkaline | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Applications: Alkaline α-galactosidase i was used to assay enzyme activity with 2 mmp-nitrophenyl-α-d-galactoside as substrate at ph 6.5 to compare with the enzyme activity of α-gal a isolated and purified from sf-9 insect cells infected with a recombinant baculovirus encoding normal α-gal a gene. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Mole weight: apparent mol wt ~84 kDa by SDS-PAGE. Storage: -20°C. Form: The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl. Source: Cucumis melo. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0291. | |
| Native Rabbit Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase from rabbit liver has been used in a study to investigate a toxic effect of carbamate insecticides. esterase from rabbit liver has also been used in a study to investigate the effect of simvastatin on expression and activity of a lipoprotein-ass ociated phospholipase a. the enzyme from creative enzymes has been used to study the effect of divalent metal ions on the activity of esterase. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; ca. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rabbit liver. Species: Rabbit. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0238. | |
| Native Rabbit Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess molecular characterizations of cryptosporidium, giardia, and enter ...e phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: Type I, > 4,000 units/mg protein; Type II, > 3,500 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0; Type II, lyophilized powder, Sulfate-free, contains EDTA and borate buffer salts. Source: Rabbit muscle. Species: Rabbit. Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0712. | |
| Native Trichoderma longibrachiatum endo-1,4-β-Xylanase | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4. Enzyme Commission Number: EC 3.2.1.8. CAS No. 9025-57-4. Xylanase. Activity: > 1.0 units/mg solid. Storage: Room temp. Source: Trichoderma longibrachiatum. EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Cat No: NATE-0735. | |
| nepenthesin | From the insectivorous plants Nepenthes spp. (secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, including Lotus and sorghum. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: Nepenthes aspartic proteinase; Nepenthes acid proteinase; nepenthacin; nepenthasin; aspartyl endopeptidase. Enzyme Commission Number: EC 3.4.23.12. CAS No. 9073-80-7. 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-4251; nepenthesin; EC 3.4.23.12; 9073-80-7; Nepenthes aspartic proteinase; Nepenthes acid proteinase; nepenthacin; nepenthasin; aspartyl endopeptidase. Cat No: EXWM-4251. | |
| nitrite dismutase | Contains ferriheme b. The enzyme is one of the nitrophorins from the salivary gland of the blood-feeding insect Rhodnius prolixus. Nitric oxide produced induces vasodilation after injection. Nitrophorins 2 and 4 can also catalyse this reaction. Group: Enzymes. Synonyms: Prolixin S; Nitrophorin 7. Enzyme Commission Number: EC 1.7.6.1. 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-1631; nitrite dismutase; EC 1.7.6.1; Prolixin S; Nitrophorin 7. Cat No: EXWM-1631. | |
| nodavirus endopeptidase | A single aspartic residue is critical for activity, and inhibition by EDTA indicates that a metal ion is also important. The enzyme is known from several nodaviruses that are pathogens of insects. Type example of peptidase family A6, and structurally related to the tetravirus endopeptidase in family A21, although in that family, the catalytic residue is thought to be Glu. Group: Enzymes. Synonyms: Black Beetle virus endopeptidase; Flock House virus endopeptidase. Enzyme Commission Number: EC 3.4.23.44. CAS No. 852954-38-2. 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-4281; nodavirus endopeptidase; EC 3.4.23.44; 852954-38-2; Black Beetle virus endopeptidase; Flock House virus endopeptidase. Cat No: EXWM-4281. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) | The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reacti... dPGM. Enzyme Commission Number: EC 5.4.2.11. 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-5522; phosphoglycerate mutase (2,3-diphosphoglycerate-dependent); EC 5.4.2.11; glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM. Cat No: EXWM-5522. | |
| Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) | Photinus (firefly) is a bioluminescent insect. The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate. The enzyme may be assayed by measurement of light emission. Group: Enzymes. Synonyms: firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase. Enzyme Commission Number: EC 1.13.12.7. CAS No. 61970-00-1. Luciferase. 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-0620; Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); EC 1.13.12.7; 61970-00-1; firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase. Cat No: EXWM-0620. | |
| Piperonylbutoxide | Piperonyl butoxide works as an insecticide synergist. It is useful in inhibitng the insect microsomal enzyme detoxification activity and is always under the combination usage with other ingredients like pyrethroid, rotenone, pyrethrin and etc. Uses: Piperonyl butoxide works as an insecticide synergist mainly for pyrethroids and rotenone. Synonyms: 5-[2-(2-butoxyethoxy)ethoxymethyl]-6-propyl-1,3-benzodioxole. Grades: > 90 %. CAS No. 51-03-6. Molecular formula: C19H30O5. Mole weight: 338.44. | |
| PNGase A from Oryza sativa (rice), Recombinant | PNGase A cleaves N-linked glycans from high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.PNGase A is a recombinant amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues. Group: Enzymes. Synonyms: N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Enzyme Commission Number: EC 3.5.1.52. Purity: > 95% pure as determined by SDS-PAGE. PNGase F. Mole weight: 63.8 kDa. Activity: 5,000 units/ml. Storage: 4°C. Form: Storage Conditions: 50 mM NaCl, 20 mM Tris-HCl, 5 mM EDTA, (pH 7.5 @ 25°C). Source: Pichia pastoris. Species: Oryza sativa (rice). N-Glycosidase A; PNGase A; Glycopeptidase A; N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase; PNGase. Cat No: NATE-1941. | |
| Propoxur | Propoxur is a non-systematic carbamate insecticide. Propoxur is used against a wide range of insects such as fleas, mosquitoes, ants, gypsy moths, and other agricultural pests. Propoxur functions by reversibly inactivating the enzyme acetylcholinesterase in insects. Group: Biochemicals. Alternative Names: 2-(1-Methylethoxy)phenol 1-(N-Methylcarbamate); 2-(1-Methylethoxy)phenyl N-Methylcarbamate; 2-Isopropoxyphenyl N-Methylcarbamate; Arprocarb; Bayer 39007; Bayer B 5122; Baygon G; Blattanex; Blattosep; Bolfo; Boruho; Boruho 50; Brygou; Dalf Dust; ENT 25,671; IPMC; Invisi-Gard; Mrowkozol; NSC 379584; O-(2-Isopropoxyphenyl) N-methylcarbamate; OMS 33; PHC 7; Propotox; Propoxylor; Sendran; Suncide; Tendex; Unden. Grades: Highly Purified. CAS No. 114-26-1. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| Prostatic acid phosphatase from Human, recombinant | ACPP, also known as prostatic acid phosphatase isoform PAP, is a type I integral membrane protein of the plasma membrane and lysosomes, and a secreted form also exists. The concentration of ACPP is elevated in the circulation of prostate cancer patients, making the enzyme a marker for the progression of prostate cancer. Recombinant human ACPP, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39; ACPP; ACP-3, ACP3. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Purity: > 95% by SDS-PAGE. Apase. Mole weight: 41.8 kDa. Activity: >100,000 units/mg. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: Baculovirus. Species: Human. Prostatic acid phosphatase; PAP; prostatic specific acid phosphatase; PSAP; EC 3.1.3.2; ACP; Acid Phos; 5'-nucleotidase; 5'-NT; Ecto-5'-nucleotidase; Thiamine monophosphatase; TMPase; PAPf39; ACPP; ACP-3, ACP3. Cat No: NATE-1673. | |
| Protein kinase Cα isozyme human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second...third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. > 70% (sds-page), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution. Group: Enzymes. Synonyms: PRKCA; protein kinase C, alpha; PKCA; protein kinase C alpha type; PKC-A; PKCα; AAG6; PKC-alpha; PRKACA. Purity: > 70% (SDS-PAGE). PKC. Mole weight: mol wt 80-81 kDa by SDS-PAGE. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected insect cells. Species: Human. PRKCA; protein kinase C, alpha; PKCA; protein kinase C alpha type; PKC-A; PKCα; AAG6; PKC-alpha; PRKACA. Cat No: NATE-0574. | |
| Protein Kinase CβII isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec... esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: calculated mol wt 76.9 kDa; mol wt 80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0622. | |
| Protein Kinase CβI isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...ted by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 95% (SDS-PAGE). PKC. Mole weight: apparent mol wt 79-80 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCB; PKCB; PRKCB1; PRKCB2; protein kinase C, beta 1; protein kinase C beta type; PKC-beta; EC 2.7.1.37. Cat No: NATE-0621. | |
| Protein Kinase Cδ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 74-79 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCD; protein kinase C, delta; protein kinase C delta type; ALPS3; CVID9; MAY1; PKCD; nPKC-delta; EC 2.7.1.37. Cat No: NATE-0623. | |
| Protein Kinase Cε isozyme human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the secon...tein kinase C, epsilon; protein kinase C epsilon type; PKCE; nPKC-epsilon; Ca2+-activated phospholipid-dependent serine-threonine kinase, ε isozyme human; PKCε human; PKCε; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: apparent mol wt 89-96 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected insect cells. Species: Human. PRKCE; protein kinase C, epsilon; protein kinase C epsilon type; PKCE; nPKC-epsilon; Ca2+-activated phospholipid-dependent serine-threonine kinase, ε isozyme human; PKCε human; PKCε; EC 2.7.1.37. Cat No: NATE-0575. | |
| Protein Kinase Cη isozyme human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second ...nd include PKCξ, μ, and &Iota. > 90% (sds-page), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution. Group: Enzymes. Synonyms: PRKCH; Ca2+-activated phospholipid-dependent serine-threonine kinase η isozyme human; PKCη human; PKCH; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 90% (SDS-PAGE). PKC. Mole weight: mol wt 82-84 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected insect cells. Species: Human. PRKCH; Ca2+-activated phospholipid-dependent serine-threonine kinase η isozyme human; PKCη human; PKCH; EC 2.7.1.37. Cat No: NATE-0576. | |
| Protein kinase Cγ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the sec...vated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 77-84 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCG; protein kinase C, gamma; protein kinase C gamma type; PKC-gamma; PKCC; PKCG; SCA14; EC 2.7.1.37. Cat No: NATE-0624. | |
| Protein Kinase Cζ isozyme from human, Recombinant | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the seco...Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Group: Enzymes. Synonyms: PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Enzyme Commission Number: EC 2.7.1.37. Purity: > 75% (SDS-PAGE). PKC. Mole weight: mol wt 76-80 kDa by SDS-PAGE. Storage: -70°C. Form: buffered aqueous solution; Solution in 20 mM HEPES, pH 7.5; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol. Source: Baculovirus infected insect cells. Species: Human. PRKCZ; protein kinase C, zeta; protein kinase C zeta type; PKC2; PKC-ZETA; EC 2.7.1.37. Cat No: NATE-0625. | |
| Protein Kinase G Iβ human, Recombinant | Protein Kinase G Iβ induces apoptosis in certain cell lines such as human breast cancer cell lines MCF-7 and MDA-MB-468. It inhibits cell proliferation and induces apoptosis in colon cancer cell lines. > 95% (sds-page), recombinant, expressed in baculovirus infected sf9 cells, buffered aqueous glycerol solution. Applications: Protein kinase g is a serine/threonine-specific protein kinase that is activated by cgmp. protein kinase g iβ is used to induce apoptosis and inhibit cell proliferation. Group: Enzymes. Synonyms: Protein Kinase G Iβ; PRKG1B; PRKGR1B; PKG1B; cGMP-dependent protein kinase 1; cGKI-BETA. Purity: >95% (SDS-PAGE). PKG. Mole weight: mol wt 76 kDa (monomer). Activity: > 1.5 units/mg protein (20-fold stimulation by cGMP (5 μM)). Stability: -20°C. Form: buffered aqueous glycerol solution. Source: baculovirus infected insect cells. Species: Human. Protein Kinase G Iβ; PRKG1B; PRKGR1B; PKG1B; cGMP-dependent protein kinase 1; cGKI-BETA. Cat No: NATE-0580. | |
| Protein Phosphatase 2Ac from Human, Recombinant | Divalent cation-independent catalytic subunit of protein phosphatase 2A. Useful for functional studies of the A and B subunit of the phosphatase. Human recombinant pp2a catalytic subunit expressed in insect cells with an n-terminal octahistidine-tag followed by a streptactin-tag. the c-terminal leucine 309 was deleted. Applications: Useful for the study of enzyme kinetics and regulation, to dephosphorylate target substrates and to evaluate the effects of test substances on the activity of the phosphatase. Group: Enzymes. Synonyms: Protein Phosphatase 2Ac; PP2Ac. Purity: >90% estimated by SDS-PAGE. Protein Phosphatase. Mole weight: 38.6 kDa. Stability: As supplied, 6 months from the QC date provided on the Certificate of Analysis, when stored properly. Storage: at -80°C. Source: Insect cells. Species: Human. Protein Phosphatase 2Ac; PP2Ac. Cat No: NATE-1398. | |
| senecionine N-oxygenase | A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates. Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores. Group: Enzymes. Synonyms: senecionine monooxygenase (N-oxide-forming); SNO. Enzyme Commission Number: EC 1.14.13.101. CAS No. 220581-68-0. 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-0700; senecionine N-oxygenase; EC 1.14.13.101; 220581-68-0; senecionine monooxygenase (N-oxide-forming); SNO. Cat No: EXWM-0700. | |
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