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| Product | Description | |
|---|---|---|
| 7-Methylguanine | Has binding affinity to guanine deaminase, an important metalloenzyme in purine catabolism. Found in urine of patients with malignant cancer. Group: Biochemicals. Alternative Names: 2-Amino-1,7-dihydro-7-methyl-6H-purin-6-one; 2-Amino-7-methylhypoxanthine; N7-Methylguanine; NSC 193444; NSC 19647. Grades: Highly Purified. CAS No. 578-76-7. Pack Sizes: 100mg. US Biological Life Sciences. |  Worldwide |
| aureolysin | A metalloenzyme from S. aureus earlier confused with staphylokinase (a non-enzymic activator of plasminogen). Group: Enzymes. Synonyms: Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease. Enzyme Commission Number: EC 3.4.24.29. CAS No. 39335-13-2. Metalloproteinase. 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-4310; aureolysin; EC 3.4.24.29; 39335-13-2; Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease. Cat No: EXWM-4310. |  |
| Carbonic anhydrase, Bovine erythrocytes | Carbonic anhydrase, Bovine erythrocytes (EC 4.2.1.1) is ubiquitous zinc-containing metalloenzyme present in prokaryotes and eukaryotes. Carbonic anhydrase can catalyze reversible conversion of carbon dioxide to bicarbonate and protons. Carbonic anhydrase can be used for the research of cancer, glaucoma, obesity and epilepsy [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 4.2.1.1. CAS No. 9001-03-0. Pack Sizes: 5 mg; 10 mg. Product ID: HY-P1775. |  |
| Carbonic anhydrase from E. coli, recombinant | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. Group: Enzymes. Synonyms: Carbonate dehydratase; CAN; yadF. Enzyme Commission Number: EC 4.2.1.1. Purity: > 95% by SDS-PAGE. Carbonic Anhydrase. Mole weight: This protein is fused with 6x His tag at N terminus and the protein has a calculated MW of 27 kDa (240aa). Activity: >1,000 pmol/min/ug. 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: E. coli. Species: E. coli. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; CA; CAN; yadF. Cat No: NATE-1669. | |
| Carbonic Anhydrase II from Bovine, Recombinant | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. Carbonic anhydrase is a zinc-containing enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate. one of its main physiological roles is to maintain the acid-base balance in blood and other tissues. lack of carbonic anhydrase results in carbonic anhydrase type ii defi...ns: Carbonic anhydrase is used to create carbon dioxide capture systems and to research various purification techniques. carbonic anhydrase is also used to study acid-base regulation in fish and carbonic anhydrase type ii deficiency syndrome. bovine carbonic anhydrase ii (ca II), has been widely used as a model protein in the investigation of the protein folding process. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Purity: >90% by SDS-PAGE. Carbonic Anhydras | |
| Carbonic Anhydrase II from Human, Recombinant | Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30 kDa Da. The enzyme catalyzes the hydRation of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO2 homeostasis, transport of bicarbonate and CO2, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinsons disease. Applications: Human carbonic anhydrase isozyme ii has been used to assess its gene fusion abilities for efficient expression and recovery of recombinant proteins. human ...viduals. the enzyme has also been used in the study of natural phenolic inhibitors of ca ii. Group: Enzymes. Synonyms: Carbonic Anhydrase II; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; CA-II; CA2; Carbonic Anhydrase 2. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Activity: > 80%, > 3 ,000 W-A units/mg protein. Form: powder. Source: E. coli. Species: Human. Carbonic Anhydrase II; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhyd | |
| Carbonic anhydrase (isoenzyme) | Carbonic anhydrase isoenzyme is the isoenzyme of Carbonic anhydrase (HY-P1775). Carbonic anhydrase isoenzyme is ubiquitous zinc-containing metalloenzyme present in prokaryotes and eukaryotes. Carbonic anhydrase isoenzyme catalyzes reversible conversion of carbon dioxide to bicarbonate and protons, and can be used for the research of cancer, glaucoma, obesity and epilepsy [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-03-0. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-P1775A. | |
| CHR-3996 | CHR-3996 is an orally bioavailable, second-generation hydroxamic acid-based inhibitor of histone deacetylase (HDAC) with potential antineoplastic activity. HDAC inhibitor CHR-3996 inhibits HDAC, resulting in an accumulation of highly acetylated histones, the induction of chromatin remodeling, and the selective transcription of tumor suppressor genes; these events may result in the inhibition of tumor cell division and the induction of tumor cell apoptosis. This agent may upregulate HSP70 and downregulate anti-apoptotic Bcl-2 proteins more substantially than some first-generation HDAC inhibitors. HDACs, upregulated in many tumor cell types, are a family of metalloenzymes responsible for the deacetylation of chromatin histone proteins. Synonyms: CHR3996; CHR 3996; VRx-3996; VRx3996; VRx 3996; Nanatinostat; Tractinostat. CAS No. 1235859-13-8. Molecular formula: C21H20FN5O2. Mole weight: 393.42. |  |
| Galactose Oxidase, Dactylium dendroides | Galactose Oxidase, Dactylium dendroides (GOase) from fungus is often used in biochemical studies. Galactose oxidase is a type II copper metalloenzyme, and it containing a single polypeptide. Galactose oxidase catalyzes two-electron oxidation of primary alcohols to their corresponding aldehydes, coupling with the reduction of dioxygen to hydrogen peroxide [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: GOase. CAS No. 9028-79-9. Pack Sizes: 50 U; 150 U; 450 U. Product ID: HY-P2910. | |
| Leukotriene A4 Hydrolase from Human, Recombinant | Leukotriene A4 Hydrolase human (LTA4H) is a bifunctional zinc metalloenzyme that converts LTA4 into Leukotriene B4, and also demonstrates aminopeptidase activity. Leukotriene B4 is a lipid chemoattractant that plays critical roles in inflammaton, immune responses, host defenses against infections, and lipid homeostasis. Inhibition of LTA4H in a mouse model decreases LTB4 in the airways and attenuates airway inflammation and airway hyperreactivity through modulation of T cell and dendritic cell function. Contains c-terminal his-tag. Applications: Leukotriene a4 hydrolase human (lta4h) is a drug target for anti-inflammation, and for cancer prevention and therapy. it is also suitable for screening inhibitors of leukotriene b4 synthesis. lta4h is used to study allergic asthma and airway hyperresponsiveness. Group: Enzymes. Synonyms: leukotriene-A4 hydrolase; LTA-4 hydrolase; LTA4; LTA4 hydrolase; LTA4H; leukotriene A4 hydrolase; EC 3.3.2.6; 90119-07-6. Enzyme Commission Number: EC 3.3.2.6. CAS No. 90119-07-6. LTA4H. Mole weight: mol wt ~69 kDa. Storage: -70°C. Form: Supplied as a solution in 100mM Tris, pH 8.0, containing 20% glycerol and 100mM potassium chloride. Source: E. coli. Species: Human. leukotriene-A4 hydrolase; LTA-4 hydrolase; LTA4; LTA4 hydrolase; LTA4H; leukotriene A4 hydrolase; EC 3.3.2.6; 90119-07-6. Cat No: NATE-0419. | |
| LY1 | LY1 is a potent, selective and covalent inhibitor against both SARS-CoV-2 PL pro and M pro with K d values of 1.5 μM and 2.3 μM for M pro C145A protein and PL pro C111A protein, respectively. LY1 potent against the viral proteases, with IC 50 s of 0.12 μM and 0.99 μM against M pro and PL pro. LY1 shows high selectivity over other kinases, human proteases and metalloenzyme [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 2883813-32-7. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-152101. | |
| Native Aeromonas proteolytica Aminopeptidase | Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at tempeRatures of 70°C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase. Applications: Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. the enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase. Group: Enzymes. Synonyms: Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. Storage: -20°C. Form: lyophilized powder, 50-150 units/mg protein. Source: Aeromonas proteolytica. Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Cat No: NATE-0071. | |
| Native Baker's yeast (S. cerevisiae) D-Ribulose-5-phosphate 3-Epimerase | RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis. Applications: D-ribulose-5-phosphate 3-epimerase is an enzyme that converts the reversible conversion of d-ribulose 5-phosphate into d-xylulose 5-phosphate, which is important for the cellular response against oxidative stress. d-ribulose-5-phosphate 3-epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. this product is from bakers yeast and is provided as a lyophilized powder. it is useful in enzyme syste...EC 5.1.3.1. CAS No. 9024-20-8. RPE. Activity: 50-100 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder. Lyophilized and essentially sulfate-free; contains approx. 35% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). EC 5.1.3.1; RPE; phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase; 9024-20-8. Cat No: NATE-0659. | |
| Native Baker's yeast (S. cerevisiae) Enolase | Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from bakers yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+. Applications: Enolase from baker?s yeast has been used in a st...d spectroscopy. it has also been used along with other proteins to study gradient chromatof ocusing-mass spectrometry; a new technique for protein analysis. Group: Enzymes. Synonyms: EC 4.2.1.11; enolase; 2-phosphoglyceRate dehydRatase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydRatase; 2-phosphoglyceRate dehydRatase; 2-phosphoglyceric dehydRatase; 2-phosphoglyceRate enolase; γ-enolase; 2-phospho-D-glyceRate hydro-lyase; 9014-08-8. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Baker's yeast (S. cerevisiae) | |
| Native Bovine Carbonic Anhydrase | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. It was from bovine erythrocytes. a dialyzed, lyophilized powder. Applications: Co2 determination in blood; elimination of co2 in reagents for acidity testing; carboxy group transfers; reduction reactions. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Mole weight: 29.0 kDa (Theoretical) 30 kDa (Lindskog et al. 1971). Activity: > 3,000 units per mg dry weight. Storage: 2-8°C. Form: lyophilized powder. Source: Bovine Erythrocytes. Species: Bovine. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: NATE-0101. | |
| Native Bovine Carboxypeptidase A | Carboxypeptidase as isolated from Bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate. Protein determined by e1%/278. Applications: Carboxypeptidase a from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase a in escherichia coli. carboxypeptidase a fr...dase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Enzyme Commission Number: EC 3.4.17.1. CAS No. 11075-17-5. CPA1. Mole weight: mol wt ~35 kDa. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: aqueous suspension. Source: Bovine pancreas. Species: Bovine. EC 3.4.17.1; CPA1; CPA; carboxypeptidase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Cat No: NATE-0150 | |
| Native Human Carbonic Anhydrase I | Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30 kDa Da. The enzyme catalyzes the hydRation of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO2 homeostasis, transport of bicarbonate and CO2, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinsons disease. Applications: Carbonic anhydrase from human erythrocytes (hca) has been used to study the molten-globule state of carbonic anhydrase (ca). chaperone-like α-crystallin bi...on-small cell lung cancer. Group: Enzymes. Synonyms: Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Activity: 100-500 W-A units/mg protein. Form: powder. Source: Human erythrocytes. Species: Human. Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Cat No: NATE-0097. | |
| Native Porcine Superoxide Dismutase | Superoxide dismutase (SOD) is one kind of metalloenzyme, it can be used in antioxidization, fight against senium and improve the immunologic function. Superoxide dismutase(SOD) can be used in health care food, cosmetics and beer, etc. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: 32KD. Activity: 4500 U/mg. Storage: 2 years in dry and low temperature. Form: light blue green powder. Source: Porcine. Species: Porcine. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein; hepatocuprein; 9054-89-1. Cat No: NATE-1925. | |
| Native Pseudomonas fragi mutant strain Endoproteinase Asp-N | Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Cleavage of Xaa-Asp, Xaa-Glu and Xaa-cysteic acid bonds. This metalloenzyme is isolated from Pseudomonas fragi. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 9001-92-7. Endoproteinase Asp-N. Storage: 2-8°C. Form: lyophilized powder. Source: Pseudomonas fragi mutant strain. endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Pack: vial of 2 μg. Cat No: NATE-0222. | |
| Native Saccharomyces cerevisiae Glyoxalase I | Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Glyoxalase detoxification system consists of glyoxalase (glo)-i and glo-ii. glo-i is a cytosolic, 42 kda, dimeric zn2+ metalloenzyme. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. CAS No. 9033-12-9. Glyoxalase I. Mole weight: 42 kDa. Activity: > 400 units/mg protein. Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol, 0.4 M (NH4)2SO4 and 0.002 M KH2PO4 pH 6.5. Source: Saccharomyces cerevisiae. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-0308. | |
| peptidoglycan-N-acetylglucosamine deacetylase | Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori,Listeria monocytogenes and Streptococcus suis. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively. Group: Enzymes. Synonyms: HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase. Enzyme Commission Number: EC 3.5.1.104. 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-4383; peptidoglycan-N-acetylglucosamine deacetylase; EC 3.5.1.104; HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase. Cat No: EXWM-4383. | |
| peptidyl-Asp metalloendopeptidase | A metalloenzyme isolated from Pseudomonas fragi. Useful in protein sequencing applications because of its limited specificity. In peptidase family M72. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 55576-49-3. Endoproteinase Asp-N. 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-4315; peptidyl-Asp metalloendopeptidase; EC 3.4.24.33; 55576-49-3; endoproteinase Asp-N; peptidyl-Asp metalloproteinase. Cat No: EXWM-4315. | |
| protein farnesyltransferase | This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, γ-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity. Group: Enzymes. Synonyms: FTase. Enzyme Commission Number: EC 2.5.1.58. CAS No. 131384-38-8. 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-2795; protein farnesyltransferase; EC 2.5.1.58; 131384-38-8; FTase. Cat No: EXWM-2795. | |
| protein geranylgeranyltransferase type I | This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most γ-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding. Group: Enzymes. Synonyms: GGTase-I; GGTaseI. Enzyme Commission Number: EC 2.5.1.59. CAS No. 135371-29-8. 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-2796; protein geranylgeranyltransferase type I; EC 2.5.1.59; 135371-29-8; GGTase-I; GGTaseI. Cat No: EXWM-2796. | |
| PSM P2 (711-719) | PSM P2 (711-719) is a 9-aa peptide. PSM P2 is a zinc metalloenzyme that resides in membranes. It is mainly expressed in four tissues of the body, including prostate epithelium, the proximal tubules of the kidney, the jejunal brush border of the small intestine and ganglia of the nervous system. Synonyms: Glutamate carboxypeptidase 2 (711-719); N-acetyl-L-aspartyl-L-glutamate peptidase I (711-719); NAAG peptidase (711-719); prostate-specific membrane antigen (PSMA) (711-719). | |
| sn-glycerol-1-phosphate dehydrogenase | This enzyme is found primarily as a Zn2+-dependent form in archaea but a Ni2+-dependent form has been found in Gram-positive bacteria. The Zn2+-dependent metalloenzyme is responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of gl...oval of CMP, leading to the production of unsaturated archaetidylserine. Activity of the enzyme is stimulated by K+. Group: Enzymes. Synonyms: glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM. Enzyme Commission Number: EC 1.1.1.261. CAS No. 204594-18-3. 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-0167; sn-glycerol-1-phosphate dehydrogenase; EC 1.1.1.261; 204594-18-3; glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM. Cat No: EXWM-0167. | |
| Tioxolone | Tioxolone is a metalloenzyme carbonic anhydrase I inhibitor with a Ki of 91 nM. Synonyms: 6-Hydroxy-1,3-benzoxathiol-2-one. Grades: >98%. CAS No. 4991-65-5. Molecular formula: C7H4O3S. Mole weight: 168.17. | |
| Tioxolone | Tioxolone is an inhibitor of the metalloenzyme carbonic anhydrase I and has anti-acne activity. Uses: Scientific research. Group: Signaling pathways. CAS No. 4991-65-5. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g. Product ID: HY-B0483. | |
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