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| Product | Description | |
|---|---|---|
| 1,3-Diphenyl-4,5-dihydro-1H-pyrazole | 1,3-Diphenyl-4,5-dihydro-1H-pyrazole is a heterocyclic compound belonging to the pyrazole family. It is an organic compound composed of two phenyl rings, a nitrogen atom and a hydrogen atom. Pyrazoles are known for their versatile properties, which makes them useful in a wide range of applications. DPDP is of particular interest due to its potential applications in scientific and medical research. Uses: 1,3-diphenyl-4,5-dihydro-1h-pyrazole is a versatile compound that can be used in a variety of scientific research applications. it has been used as a ligand for the binding of metal ions, such as copper, zinc, and iron, in order to study the structure and function of metalloproteins. it has also been used as a fluorescent probe for the study of enzyme kinetics, as well as for the detection of reac. Group: Heterocyclic organic compound. Alternative Names: 1,3-Diphenylpyrazoline, 1,3-Diphenyl-2-pyrazoline, 2-Pyrazoline, 1,3-diphenyl-, MLS000717825, 1,3-Diphenyl-4,5-dihydro-1H-pyrazole, MolPort-001-631-521, NSC186211, NSC625226, AIDS132054, AIDS-132054, 1,3-Diphenyl-.DELTA.2-pyrazoline, CID302304, ZINC04142401, 1H-Pyrazole, 4,5-dihydro-1,3-diphenyl-, BAS 00363868, SMR000279193, AE-848/30721014, A0944/0044214, 2538-52-5. CAS No. 2538-52-5. Molecular formula: C15H14N2. Mole weight: 222.2851. Purity: 0.96. IUPACName: 2,5-diphenyl-3,4-dihydropyrazole. Canonical SMILES: C1CN(N=C1C2=CC=CC=C2)C3=CC=CC=C3. Densit |  |
| 2,4-Pyridinedicarboxylic acid monohydrate | 2,4-Pyridinedicarboxylic acid (2,4-PDCA) is a compound that structurally mimics 2-oxoglutarate (2-OG, also known as α-ketoglutarate) and chelates zinc, thus affecting a range of enzymes. Synonyms: pyridine-2,4-dicarboxylic acid;hydrate. Grades: ≥ 98 %. CAS No. 207671-42-9. Molecular formula: C7H5NO4 · H2O. Mole weight: 185.13. |  |
| 2-deoxy-scyllo-inosamine dehydrogenase | Requires zinc. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, neomycin and ribostamycin. cf. EC 1.1.99.38, 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent). Group: Enzymes. Synonyms: neoA (gene name); kanK (gene name, ambiguous); kanE (gene name, ambiguous). Enzyme Commission Number: EC 1.1.1.329. 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-0242; 2-deoxy-scyllo-inosamine dehydrogenase; EC 1.1.1.329; neoA (gene name); kanK (gene name, ambiguous); kanE (gene name, ambiguous). Cat No: EXWM-0242. |  |
| 2-hydroxypropyl-CoM lyase | Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation ...ission Number: EC 4.4.1.23. CAS No. 244301-07-3. 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-5325; 2-hydroxypropyl-CoM lyase; EC 4.4.1.23; 244301-07-3; epoxyalkane:coenzyme M transferase; epoxyalkane:CoM transferase; epoxyalkane:2-mercaptoethanesulfonate transferase; coenzyme M-epoxyalkane ligase; epoxyalkyl:CoM transferase; epoxypropane:coenzyme M transferase; epoxypropyl:CoM transferase; EaCoMT; 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming); (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing; (R)-1,2-epoxypropane-forming). Cat No: EXWM-5325. | |
| 2-Methoxy-4-morpholinobenzenediazonium chloride zinc chloride double salt | 2-Methoxy-4-morpholinobenzenediazonium chloride zinc chloride double salt (CAS# 67801-08-5) is used in preparation of aryl amino acid and peptide esters as enzyme substrates for leukocyte detection. Synonyms: 2-Methoxy-4-(morpholin-4-yl)benzenediazonium tetrachlorozincate (2:1). Grades: 95 %. CAS No. 67801-08-5. Molecular formula: C22H28Cl4N6O4Zn. Mole weight: 647.7. | |
| 2-Methoxycarbonylphenyl b-D-glucopyranoside | 2-Methoxycarbonylphenyl b-D-glucopyranoside, a versatile compound, occupies a significant position in biomedicine owing to its proficiency in probing carbohydrate metabolism and its implications in diabetes research. This chemical entity emerges as an indispensable tool in scrutinizing glucose transporters and enzymes involved in the intricate glucose-related processes. Synonyms: 2-Methoxycarbonylphenyl b-D-glucopyranoside; 2-Methoxycarbonylphenyl beta-D-glucopyranoside; ZINC05234420; methyl 2-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxybenzoate; DTXSID70428813; CHEBI:168882; methylsalicylate-2-O-beta-D-glucoside; methylsalicylate O-beta-D-glucopyranoside; W-200618; Benzoic acid, 2-(beta-D-glucopyranosyloxy)-, methyl ester. CAS No. 10019-60-0. Molecular formula: C14H18O8. Mole weight: 314.29. | |
| 3-mercaptopyruvate sulfurtransferase | Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. The bacterial enzyme is a zinc protein. Group: Enzymes. Synonyms: β-mercaptopyruvate sulfurtransferase. Enzyme Commission Number: EC 2.8.1.2. CAS No. 9026-5-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3360; 3-mercaptopyruvate sulfurtransferase; EC 2.8.1.2; 9026-05-5; β-mercaptopyruvate sulfurtransferase. Cat No: EXWM-3360. | |
| 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase | Requires phosphate and contains zinc. The enzyme from Escherichia coli also requires a reducing system. Unlike EC 2.1.1.13, methionine synthase, this enzyme does not contain cobalamin. Group: Enzymes. Synonyms: tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Enzyme Commission Number: EC 2.1.1.14. CAS No. 9068-29-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1735; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase; EC 2.1.1.14; 9068-29-5; tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Cat No: EXWM-1735. | |
| 7-(2-C-Methyl-b-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine | 7-(2-C-Methyl-b-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine, an intricate compound of paramount significance, finds extensive application in the biomedical sector for combating diverse viral infections. It unveils remarkable inhibitory potential against particular viruses through its precise engagement with vital viral enzymes or proteins, thereby impeding the replication and dissemination of the pathogens. Synonyms: (2R,3R,4R,5R)-2-(2-aminopyrrolo[2,3-d]pyrimidin-7-yl)-5-(hydroxymethyl)-3-methyloxolane-3,4-diol;443642-48-6;SCHEMBL731577;ZHRLTTOGZNAIAQ-FWSPBBIJSA-N;ZINC34003523;NU000308. Grades: 95%. CAS No. 443642-48-6. Molecular formula: C12H16N4O4. Mole weight: 280.28. | |
| 7,8-dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase | Contains one zinc atom and one iron atom per subunit of the dodecameric enzyme. It hydrolyses 7,8-dihydroneopterin 2',3'-cyclic phosphate, a step in tetrahydromethanopterin biosynthesis. In vitro the enzyme forms 7,8-dihydroneopterin 2'-phosphate and 7,8-dihydroneopterin 3'-phosphate at a ratio of 4:1. Group: Enzymes. Synonyms: MptB. Enzyme Commission Number: EC 3.1.4.56. 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-3739; 7,8-dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase; EC 3.1.4.56; MptB. Cat No: EXWM-3739. | |
| alcohol dehydrogenase | A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. 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-0001; alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5; aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Cat No: EXWM-0001. | |
| alcohol dehydrogenase (NADP+) | A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH. Group: Enzymes. Synonyms: aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. 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-0103; alcohol dehydrogenase (NADP+); EC 1.1.1.2; 9028-12-0; aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: EXWM-0103. | |
| alkaline phosphatase | Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase). Group: Enzymes. Synonyms: alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum). Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. 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-3607; alkaline phosphatase; EC 3.1.3.1; 9001-78-9; alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum). Cat No: EXWM-3607. | |
| AminoAcylase-1 from Human, Recombinant | Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes. Acy1 recombinant human produced in e. coli is a single, non-... SDS-PAGE. ACY1. Mole weight: 48 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. N-acyl-L-amino-acid amidohydrolase; ACY-1, ACY1D; ACYLASE; ACY1; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short | |
| aminopeptidase Ey | A zinc glycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family), composed of two 150 kDa subunits. From the plasma fraction of hen egg yolk. Group: Enzymes. Enzyme Commission Number: EC 3.4.11.20. CAS No. 9031-94-1. 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-4017; aminopeptidase Ey; EC 3.4.11.20; 9031-94-1. Cat No: EXWM-4017. | |
| aminopeptidase S | Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation. This enzyme contains two zinc molecules in its active site and is activated by Ca2+. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe. Peptides with proline in the P1' position are not substrates. Belongs in peptidase family M28. Group: Enzymes. Synonyms: Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Enzyme Commission Number: EC 3.4.11.24. 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-4021; aminopeptidase S; EC 3.4.11.24; Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Cat No: EXWM-4021. | |
| ammonia monooxygenase | The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper, iron and possibly zinc. The enzymes require two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor. Group: Enzymes. Synonyms: AMO. Enzyme Commission Number: EC 1.14.99.39. 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-1050; ammonia monooxygenase; EC 1.14.99.39; AMO. Cat No: EXWM-1050. | |
| aspartoacylase | Aspartoacylase (EC 3.5.1.15, aminoacylase II, N-acetylaspartate amidohydrolase, acetyl-aspartic deaminase, acylase II, ASPA) is a hydrolase enzyme responsible for catalyzing the deacylation of N-acetyl-l-aspartate (N-acetylaspartate,NAA) into aspartate and acetate. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the brain, where it controls the levels of N-actetyl-l-aspartate. Group: Enzymes. Synonyms: aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Enzyme Commission Number: EC 3.5.1.15. CAS No. 9031-86-1. 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-4404; aspartoacylase; EC 3.5.1.15; 9031-86-1; aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Cat No: EXWM-4404. | |
| bacterial leucyl aminopeptidase | A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Streptococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively). Group: Enzymes. Synonyms: Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. 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-4008; bacterial leucyl aminopeptidase; EC 3.4.11.10; 37288-67-8; Aeromonas proteolytica aminopeptidase. Cat No: EXWM-4008. | |
| barbiturase | Contains zinc and is specific for barbiturate as substrate. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase. Group: Enzymes. Enzyme Commission Number: EC 3.5.2.1. CAS No. 9025-16-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4492; barbiturase; EC 3.5.2.1; 9025-16-5. Cat No: EXWM-4492. | |
| Benzamide, N-[4-methyl-3-[[4-(6-methyl-3-pyridinyl)-2-pyrimidinyl]amino]phenyl]-4-[(4-methyl-1-piperazinyl)methyl]- | This product is a kinase inhibitor used in the treatment of certain types of cancer, including non-small cell lung cancer and pancreatic cancer. It works by inhibiting specific enzymes involved in cell growth and proliferation, ultimately leading to tumor regression. Synonyms: N-[4-methyl-3-[[4-(6-methylpyridin-3-yl)pyrimidin-2-yl]amino]phenyl]-4-[(4-methylpiperazin-1-yl)methyl]benzamide; CHEMBL1079113; 1032314-85-4; SCHEMBL11939618; BDBM50313640; ZINC49018631. Grades: 95%. CAS No. 1032314-85-4. Molecular formula: C30H33N7O. Mole weight: 507.63. | |
| betaine-homocysteine S-methyltransferase | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively. Group: Enzymes. Synonyms: betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase. Enzyme Commission Number: EC 2.1.1.5. CAS No. 9029-78-1. 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-1953; betaine-homocysteine S-methyltransferase; EC 2.1.1.5; 9029-78-1; betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase. Cat No: EXWM-1953. | |
| Betaine Homocysteine S-methyltransferase, Recombinant | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) ? dimethylglycine (hydrogen receiver) + methionine (methyl receiver). Group: Enzymes. Synonyms: Betaine-homocysteine S-methyltransferase; Betaine homocysteine S-methyltransferase; Betaine-homocysteine S methyltransferase; Betaine homocysteine S methyltransferase; betaine-homocysteine methyltransferase; BHMT; 9029-78-1; EC 2.1.1.5. Enzyme Commission Number: EC 2.1.1.5. CAS No. 9029-78-1. Purity: 90% (SDS-PAGE test). Mole weight: About 47 kDa ?SDS-PAGE?. Storage: 4°C,store at -20°C for long-term preservation. Form: White powder, lyophilized. Betaine-homocysteine S-methyltransferase; Betaine homocysteine S-methyltransferase; Betaine-homocysteine S methyltransferase; Betaine homocysteine S methyltransferase; betaine-homocysteine methyltransferase; BHMT; 9029-78-1; EC 2.1.1.5. Cat No: NATE-1684. | |
| bontoxilysin | This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: botulinum neurotoxin; BoNT. Enzyme Commission Number: EC 3.4.24.69. CAS No. 107231-12-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4352; bontoxilysin; EC 3.4.24.69; 107231-12-9; botulinum neurotoxin; BoNT. Cat No: EXWM-4352. | |
| carbonate dehydratase | A zinc protein. Group: Enzymes. Synonyms: carbonic anhydrase; 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. 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-4938; carbonate dehydratase; EC 4.2.1.1; 9001-03-0; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: EXWM-4938. | |
| 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 | |
| carboxypeptidase A | A zinc enzyme formed from procarboxypeptidase A. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells and skeletal muscle. Type example of peptidase family M14. Group: Enzymes. Synonyms: carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Enzyme Commission Number: EC 3.4.17.1. CAS No. 11075-17-5. CPA1. 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-4061; carboxypeptidase A; EC 3.4.17.1; 11075-17-5; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Cat No: EXWM-4061. | |
| carboxypeptidase B | A zinc enzyme formed from procarboxypeptidase B. Isolated from cattle, pig and dogfish pancreas and other sources, including skin fibroblasts and adrenal medulla. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. 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-4072; carboxypeptidase B; EC 3.4.17.2; 9025-24-5; protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase. Cat No: EXWM-4072. | |
| carboxypeptidase E | A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Enzyme Commission Number: EC 3.4.17.10. CAS No. 81876-95-1. 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-4062; carboxypeptidase E; EC 3.4.17.10; 81876-95-1; carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Cat No: EXWM-4062. | |
| carboxypeptidase U | Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Enzyme Commission Number: EC 3.4.17.20. CAS No. 156621-18-0. 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-4073; carboxypeptidase U; EC 3.4.17.20; 156621-18-0; arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Cat No: EXWM-4073. | |
| Creatininase from E. coli, Recombinant | Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site. Group: Enzymes. Synonyms: EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Enzyme Commission Number: EC 3.5.2.10. Mole weight: ca. 170 kDa. Activity: > 100 U/mg. Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Cat No: NATE-1242. | |
| Cu/Zn Superoxide Dismutase, Recombinant | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Superoxide dismutase (sod?ec 1.15.1.1) deal with the superoxide radical byalternately adding or removing an electron from t...c arthritis, myocardial infarction, angiocardiopathy, cancer patients. 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. Purity: >90% (SDS-PAGE test). Mole weight: About 20kDa (SDS-PAGE detection). Activity: 21,186U/mg protein. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preserva | |
| cystinyl aminopeptidase | A zinc-containing sialoglycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: cystyl-aminopeptidase; oxytocinase; cystine aminopeptidase; L-cystine aminopeptidase; oxytocin peptidase; vasopresssinase. Enzyme Commission Number: EC 3.4.11.3. CAS No. 9031-41-8. 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-4024; cystinyl aminopeptidase; EC 3.4.11.3; 9031-41-8; cystyl-aminopeptidase; oxytocinase; cystine aminopeptidase; L-cystine aminopeptidase; oxytocin peptidase; vasopresssinase. Cat No: EXWM-4024. | |
| cytidine deaminase | Contains zinc. Catalyses the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. The enzyme, which is widely distributed among organisms, is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Group: Enzymes. Synonyms: cytosine nucleoside deaminase; (deoxy)cytidine deaminase; cdd (gene name); CDA (gene name). Enzyme Commission Number: EC 3.5.4.5. CAS No. 9025-6-3. 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-4573; cytidine deaminase; EC 3.5.4.5; 9025-06-3; cytosine nucleoside deaminase; (deoxy)cytidine deaminase; cdd (gene name); CDA (gene name). Cat No: EXWM-4573. | |
| cytosol alanyl aminopeptidase | A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Enzyme Commission Number: EC 3.4.11.14. CAS No. 243859-94-1. 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-4010; cytosol alanyl aminopeptidase; EC 3.4.11.14; 243859-94-1; arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Cat No: EXWM-4010. | |
| cytosol nonspecific dipeptidase | A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine. Group: Enzymes. Synonyms: N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipe. Enzyme Commission Number: EC 3.4.13.18. CAS No. 9025-31-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4032; cytosol nonspecific dipeptidase; EC 3.4.13.18; 9025-31-4; N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipeptidase; prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase; glycyl-L-leucine hydrolase; glycyl-glycine dipeptidase. Cat No: EXWM-4032. | |
| D-aminoacyl-tRNA deacylase | The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp. Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc. Group: Enzymes. Synonyms: Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Enzyme Commission Number: EC 3.1.1.96. 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-3525; D-aminoacyl-tRNA deacylase; EC 3.1.1.96; Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Cat No: EXWM-3525. | |
| diacylglycerol diphosphate phosphatase | The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase).The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase. Group: Enzymes. Synonyms: DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Enzyme Commission Number: EC 3.1.3.81. 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-3687; diacylglycerol diphosphate phosphatase; EC 3.1.3.81; DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Cat No: EXWM-3687. | |
| Dispase II | Dispase II is a neutral protease that hydrolyzes the N-terminal peptide bonds of non-polar amino acid residues. It may be used for separating many tissues and cells grown in vitro. The enzyme is very gentle and does not damage cell membranes. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin.[3] Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Ca2+, Mg2+, Mn2+, Fe2+, Fe3+ and Al3+ activate the enzyme. EDTA, EGTA, Hg2+ and other heavy metals inhibit the enzyme activity.[6] The enzyme contains 1g-atom of zinc per g-mol of purified enzyme. If this zinc component is removed by chelating agents such as EDTA or EGTA, an inactive apoenzyme is obtained. The enzyme is not inhibited by serum. Group: Biochemicals. Grades: Highly Purified. CAS No. 42613-33-2. Pack Sizes: 50mg, 100mg, 250mg, 500mg, 1g. US Biological Life Sciences. |  Worldwide |
| D-lactate dehydrogenase (acceptor) | The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known. Group: Enzymes. Synonyms: D-2-hydroxy acid dehydrogenase; D-2-hydroxy-acid dehydrogenase; (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. Enzyme Commission Number: EC 1.1.99.6. CAS No. 9028-83-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0469; D-lactate dehydrogenase (acceptor); EC 1.1.99.6; 9028-83-5; D-2-hydroxy acid dehydrogenase; D-2-hydroxy-acid dehydrogenase; (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. Cat No: EXWM-0469. | |
| flavastacin | A zinc metalloendopeptidase in peptidase family M12 (astacin family), secreted by the bacterium Flavobacterium meningosepticum. The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp metalloendopeptidase from Pseudomonas fragi but the two are reported to be structurally dissimilar. Group: Enzymes. Enzyme Commission Number: EC 3.4.24.76. CAS No. 167973-66-2. 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-4360; flavastacin; EC 3.4.24.76; 167973-66-2. Cat No: EXWM-4360. | |
| Fpg Protein from Escherichia coli, Recombinant | Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). ... Protein. Mole weight: mol wt 30.2 kDa (269 amino acids, predicted from the nucleotide sequence). Activity: >20 ,000 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl. Source: E. coli. Species: Escherichia coli. Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5 (N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein; DNA-formamidopyrimidine glycosylase; EC 3.2.2.23; 78783-53-6; | |
| fructose-bisphosphate aldolase | Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; fructose diphosphate aldolase; diphosphofructose aldolase; fructose 1,6-diphosphate aldolase; ketose 1-phosphate aldolase; phosphofructoaldolase; zymohexase; fructoaldolase; fructose 1-phosphate aldolase; fructose 1-monophosphate aldolase; 1,6-diphosphofructose aldolase; SMALDO; D-fructose-1,6-bisph. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. 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-4853; fructose-bisphosphate aldolase; EC 4.1.2.13; 9024-52-6; aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; fructose diphosphate aldolase; diphosphofructose aldolase; fructose 1,6-diphosphate aldolase; ketose 1-phosphate aldolase; phosphofructoaldolase; zymohexase; fructoaldolase; fructose 1-phosphate aldolase; fructose 1-monophosphate aldolase; 1,6-diphosphofructose aldolase; SMALDO; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase. Cat No: EXWM-4853. | |
| galactitol-1-phosphate 5-dehydrogenase | Contains zinc. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.251. CAS No. 60120-43-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0157; galactitol-1-phosphate 5-dehydrogenase; EC 1.1.1.251; 60120-43-6. Cat No: EXWM-0157. | |
| gametolysin | A glycoprotein found in the periplasmic space of Chlamydomonas reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa upon activation. A zinc enzyme, inhibited by phosphoramidon, but also thiol activated. Type example of peptidase family M11. Group: Enzymes. Synonyms: autolysin, Chlamydomonas cell wall degrading protease; lysin; Chlamydomonas reinhardtii metalloproteinase; gamete lytic enzyme; gamete autolysin. Enzyme Commission Number: EC 3.4.24.38. CAS No. 97089-74-2. 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-4320; gametolysin; EC 3.4.24.38; 97089-74-2; autolysin, Chlamydomonas cell wall degrading protease; lysin; Chlamydomonas reinhardtii metalloproteinase; gamete lytic enzyme; gamete autolysin. Cat No: EXWM-4320. | |
| γ-resorcylate decarboxylase | The enzyme, characterized from several bacterial strains, is involved in the degradation of γ-resorcylate. It contains a zinc ion and a water molecule at the active site. The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction. Group: Enzymes. Synonyms: graF (gene name); tsdA (gene name). Enzyme Commission Number: EC 4.1.1.103. 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-4756; γ-resorcylate decarboxylase; EC 4.1.1.103; graF (gene name); tsdA (gene name). Cat No: EXWM-4756. | |
| glucose/galactose 1-dehydrogenase | A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)). Group: Enzymes. Synonyms: GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase. Enzyme Commission Number: EC 1.1.1.360. 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-0277; glucose/galactose 1-dehydrogenase; EC 1.1.1.360; GdhA; dual-specific glucose/galactose dehydrogenase; glucose (galactose) dehydrogenase; glucose/galactose dehydrogenase. Cat No: EXWM-0277. | |
| glutamate carboxypeptidase | A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20. Group: Enzymes. Synonyms: carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase. Enzyme Commission Number: EC 3.4.17.11. CAS No. 9074-87-7. Carboxypeptidase G. 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-4063; glutamate carboxypeptidase; EC 3.4.17.11; 9074-87-7; carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase. Cat No: EXWM-4063. | |
| glutamyl aminopeptidase | Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Enzyme Commission Number: EC 3.4.11.7. CAS No. 9074-83-3. 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-4028; glutamyl aminopeptidase; EC 3.4.11.7; 9074-83-3; aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Cat No: EXWM-4028. | |
| GTP cyclohydrolase IV | Requires Fe2+. A zinc protein. The enzyme is involved in methanopterin biosynthesis in methanogenic archaea. cf. GTP cyclohydrolase I (EC 3.5.4.16), GTP cyclohydrolase II (EC 3.5.4.25) and GTP cyclohydrolase IIa (EC 3.5.4.29). Group: Enzymes. Synonyms: MptA; GTP cyclohydrolase MptA. Enzyme Commission Number: EC 3.5.4.39. 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-4567; GTP cyclohydrolase IV; EC 3.5.4.39; MptA; GTP cyclohydrolase MptA. Cat No: EXWM-4567. | |
| Ilomastat | Ilomastat is a broad-spectrum matrix metalloproteinase inhibitor, displaying potential anticancer activity. Ilomastat is a member of the hydroxamic acid class of reversible metallopeptidase inhibitors. The anionic state of the hydroxamic acid group forms a bidentate complex with the active site zinc. Ilomastat inhibits enzymes including thermolysin, peptide deformylase, and anthrax lethal factor endopeptidase (LF) produced by the bacterium Bacillus anthracis. Synonyms: GM6001; GM-6001; GM 6001; Ilomastat; galardin; (2R)-N'-hydroxy-N-[(2S)-3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanedia. Grades: 98%. CAS No. 142880-36-2. Molecular formula: C20H28N4O4. Mole weight: 388.468. | |
| 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. | |
| Isopropyl-a-D-thiomannopyranoside | Isopropyl-α-D-thiomannopyranoside is a widely employed synthetic compound in the biomedical industry, exhibiting significant utility as a molecular probe for the inhibition of specific enzymes and subsequent investigation of their functionalities. Synonyms: IPTG (dioxane free); 2-(hydroxymethyl)-6-propan-2-ylsulfanyloxane-3,4,5-triol; Isopropyl-a-D-thiomannopyranoside; beta-D-Galactopyranoside, 1-methylethyl 1-thio-; 936550-10-6; Maybridge3_000466; SCHEMBL12291669; SCHEMBL20341170; DTXSID60859354; Propan-2-yl 1-thiohexopyranoside; Isopropyl.beta.- thiogalactoside; 2-(hydroxymethyl)-6-(propan-2-ylsulfanyl)oxane-3,4,5-triol; HMS1432F04; HMS3604O21; ZINC00134320; IDI1_011853; FT-0627483; FT-0772631; EN300-114826. CAS No. 936550-10-6. Molecular formula: C9H18O5S. Mole weight: 238.30. | |
| L-dopachrome isomerase | A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84, D-dopachrome decarboxylase). Group: Enzymes. Synonyms: dopachrome tautomerase; tyrosinase-related protein 2; TRP-1; TRP2; TRP-2; tyrosinase-related protein-2; dopachrome Δ7,Δ2-isomerase; dopachrome Δ-isomerase; dopachrome conversion factor; dopachrome isomerase; dopachrome oxidoreductase; dopachrome-rearranging enzyme; DCF; DCT; dopachrome keto-enol isomerase; L-dopachrome-methyl ester tautomerase. Enzyme Commission Number: EC 5.3.3.12. CAS No. 130122-81-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5492; L-dopachrome isomerase; EC 5.3.3.12; 130122-81-5; dopachrome tautomerase; tyrosinase-related protein 2; TRP-1; TRP2; TRP-2; tyrosinase-related protein-2; dopachrome Δ7,Δ2-isomerase; dopachrome Δ-isomerase; dopachrome conversion factor; dopachrome isomerase; dopachrome oxidoreductase; dopachrome-rearranging enzyme; DCF; DCT; dopachrome keto-enol isomerase; L-dopachrome-methyl ester tautomerase. Cat No: EXWM-5492. | |
| leishmanolysin | A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100?Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8. Group: Enzymes. Synonyms: promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Enzyme Commission Number: EC 3.4.24.36. CAS No. 161052-06-8. 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-4318; leishmanolysin; EC 3.4.24.36; 161052-06-8; promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Cat No: EXWM-4318. | |
| leucyl aminopeptidase | A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Group: Enzymes. Synonyms: leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9001-61-0. LAP. 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-4007; leucyl aminopeptidase; EC 3.4.11.1; 9001-61-0; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Cat No: EXWM-4007. | |
| leukotriene-A4 hydrolase | This is a bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities. It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates (see EC 3.4.11.6, aminopeptidase B). It also converts leukotriene A4 into leukotriene B4, unlike EC 3.3.2.10, soluble epoxide hydrolase, which converts leukotriene A4 into 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol-5,6-oxide hydrolase). Group: Enzymes. Synonyms: LTA4 hydrolase; LTA4H; leukotriene A4 hydrolase. Enzyme Commission Number: EC 3.3.2.6. CAS No. 90119-07-6. LTA4H. 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-4003; leukotriene-A4 hydrolase; EC 3.3.2.6; 90119-07-6; LTA4 hydrolase; LTA4H; leukotriene A4 hydrolase. Cat No: EXWM-4003. | |
| 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. | |
| lysine carboxypeptidase | A zinc enzyme found in plasma. Inactivates bradykinin and anaphylatoxins in blood plasma. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: carboxypeptidase N; arginine carboxypeptidase; kininase I; anaphylatoxin inactivator; plasma carboxypeptidase B; creatine kinase conversion factor; bradykinase; kininase Ia; hippuryllysine hydrolase; bradykinin-decomposing enzyme; protaminase; CPase N; creatinine kinase convertase; peptidyl-L-lysine(-L-arginine) hydrolase; CPN. Enzyme Commission Number: EC 3.4.17.3. CAS No. 9013-89-2. 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-4077; lysine carboxypeptidase; EC 3.4.17.3; 9013-89-2; carboxypeptidase N; arginine carboxypeptidase; kininase I; anaphylatoxin inactivator; plasma carboxypeptidase B; creatine kinase conversion factor; bradykinase; kininase Ia; hippuryllysine hydrolase; bradykinin-decomposing enzyme; protaminase; CPase N; creatinine kinase convertase; peptidyl-L-lysine(-L-arginine) hydrolase; CPN. Cat No: EXWM-4077. | |
| lysostaphin | A zinc-dependent, 25-kDa endopeptidase from Staphylococcus simulans. Lyses cells of S. aureus, in particular, by its action on the cross-bridges of the cell wall. Type example of peptidase family M23. Group: Enzymes. Synonyms: glycyl-glycine endopeptidase. Enzyme Commission Number: EC 3.4.24.75. CAS No. 9011-93-2. Lysostaphin. 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-4359; lysostaphin; EC 3.4.24.75; 9011-93-2; glycyl-glycine endopeptidase. Cat No: EXWM-4359. | |
| mannose-6-phosphate isomerase | A zinc protein. Group: Enzymes. Synonyms: phosphomannose isomerase; phosphohexomutase; phosphohexoisomerase; mannose phosphate isomerase; phosphomannoisomerase; D-mannose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.8. CAS No. 9023-88-5. PMI. 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-5479; mannose-6-phosphate isomerase; EC 5.3.1.8; 9023-88-5; phosphomannose isomerase; phosphohexomutase; phosphohexoisomerase; mannose phosphate isomerase; phosphomannoisomerase; D-mannose-6-phosphate ketol-isomerase. Cat No: EXWM-5479. | |
| Matrix Metalloproteinase-13 (HisoTag) from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular pr..., a ca2+- and zn2+- binding catalytic domain, a hinge region, and a c-terminal hemopexin domain. hydrolyzes collagen type ii 5-6 times faster than collagens type i and iii. exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2. Group: Enzymes. Synonyms: Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 60 kDa. Activity: >50 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: S. frugiperda. Species: Human. Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Cat No: NATE-0859. | |
| Matrix Metalloproteinase-1 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...may also undergo autocatalysis to yield a 27 kda/22 kda active enzyme. expressed by a large number of cell types. cleaves fibrillar type i collagen. must be activated just prior to use. Group: Enzymes. Synonyms: Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase-1; EC 3.4.24.7; vertebrate collagenase. Enzyme Commission Number: EC 3.4.24.7. CAS No. 9001-12-1. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 56 kDa/52 kDa. Activity: >15 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: Human Rheumatoid Synovial Fibroblast. Species: Human. Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase | |
| Matrix Metalloproteinase-2 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe... does not interfere with activation. may contain up to 10% timp proteins. during storage, a small portion (less than 10%) of the enzyme may also become activated. Group: Enzymes. Synonyms: 72 kDa Gelatinase; Matrix Metalloproteinase 2; Gelatinase A; EC 3.4.24.24; type IV collagenase; 3/4 collagenase; matrix metalloproteinase 5; 72 kDa gelatinase type A; collagenase IV; collagenase type IV; MMP 2; type IV collagen metalloproteinase; type IV collagenase/gelatinase. Enzyme Commission Number: EC 3.4.24.24. CAS No. 146480-35-5. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 72 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: CHO Cells. Spe | |
| Matrix Metalloproteinase-9 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...(less than 10%) of the enzyme may also become activated. requires activation prior to use. a simple activation protocol is included. Applications: Immunoblotting (1 ug protein/lane) substrate cleavage assay (1 ug protein/lane) zymography (1 ug protein/lane). Group: Enzymes. Synonyms: Gelatinase B; EC 3.4.24.35; 92-kDa gelatinase; matrix metalloproteinase 9; type V collagenase; 92-kDa type IV collagenase; macrophage gelatinase; 95 kDa type IV collagenase/gelatinase; collagenase IV; collagenase type IV; gelatinase MMP 9; MMP 9; type IV collagen metalloproteinase. Enzyme Commission Number: EC 3.4.24.35. CAS No. 146480-36-6. Purity: >90% by SDS-PAGE. Matrix Metalloprotei | |
| Meldola Blue | A biosensor for the measurement of lactate in serum has been developed, which is based on a screen-printed carbon electrode, modified with Meldola's Blue-Reinecke Salt (MBRS-SPCE), coated with the enzyme lactate dehydrogenase NAD+ dependent (from Porcine heart), and NAD+. A cellulose acetate layer was deposited on the top of the device to act as a permselective membrane. Group: Biochemicals. Alternative Names: 9- (Dimethylamino) benzo[a]phenoxazin-7-ium Chloride Zinc Chloride; Meldola's Blue; Zinc Chloride 9- (Dimethylamino) benzo[a]phenoxazin-7-ium Chloride; Basic Leather Blue D; Meldola Blue. CAS No. 7057-57-0. Pack Sizes: 2.5mg. Molecular Formula: C??H??ClN?O xZnCl?. US Biological Life Sciences. | Worldwide |
| membrane alanyl aminopeptidase | A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1. Group: Enzymes. Synonyms: microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. 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-4016; membrane alanyl aminopeptidase; EC 3.4.11.2; 9054-63-1; microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Cat No: EXWM-4016. | |
| membrane dipeptidase | A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19. Group: Enzymes. Synonyms: renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Enzyme Commission Number: EC 3.4.13.19. CAS No. 9031-99-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4033; membrane dipeptidase; EC 3.4.13.19; 9031-99-6; renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP. Cat No: EXWM-4033. | |
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