Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| acrocylindropepsin | From the imperfect fungus Acrocylindrium sp. Has a very low pH optimum on casein of 2.0. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: Acrocylindrium proteinase; Acrocylindrium acid proteinase. Enzyme Commission Number: EC 3.4.23.28. CAS No. 37288-84-9. 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-4265; acrocylindropepsin; EC 3.4.23.28; 37288-84-9; Acrocylindrium proteinase; Acrocylindrium acid proteinase. Cat No: EXWM-4265. |  |
| acrosin | Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Enzyme Commission Number: EC 3.4.21.10. CAS No. 9068-57-9. 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-4094; acrosin; EC 3.4.21.10; 9068-57-9; acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Cat No: EXWM-4094. | |
| acrylyl-CoA reductase (NADH) | Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate. cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH). Group: Enzymes. Enzyme Commission Number: EC 1.3.1.95. 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-1365; acrylyl-CoA reductase (NADH); EC 1.3.1.95. Cat No: EXWM-1365. | |
| acrylyl-CoA reductase (NADPH) | Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+. Group: Enzymes. Enzyme Commission Number: EC 1.3.1.84. 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-1353; acrylyl-CoA reductase (NADPH); EC 1.3.1.84. Cat No: EXWM-1353. | |
| Acs I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 50°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 500U; 2500U. R↑AATTY YTTAA↓R. Activity: 10000u.a./ml. Appearance: 10 X SE-buffer W, BSA. Storage: -20°C. Form: Liquid. Source: Arthrobacter citreus. Pack: 20 mM Tris-HCl (pH 7.5); 50 mM KCl; 0.1 mM EDTA; 10 mM 2-mercaptoethanol; 50% glycerol. Cat No: RE-1012EN. | |
| actinidain | From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In peptidase family C1 (papain family). Group: Enzymes. Synonyms: actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Enzyme Commission Number: EC 3.4.22.14. CAS No. 39279-27-1. 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-4194; actinidain; EC 3.4.22.14; 39279-27-1; actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Cat No: EXWM-4194. | |
| actinomycin lactonase | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. Group: Enzymes. Enzyme Commission Number: EC 3.1.1.39. CAS No. 37288-09-8. 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-3465; actinomycin lactonase; EC 3.1.1.39; 37288-09-8. Cat No: EXWM-3465. | |
| Active Focal Adhesion Kinase from Human, Recombinant | FAK is a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-le.Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Enzyme Commission Number: EC 2.7.10.2. Purity: Greater than 70% as determined by SDS-PAGE. FAK. Mole weight: 146.7 kDa. Activity: 72 nmole of phosphate transferred to poly [Glu,Tyr] 4:1 substrate/minute/mg of total protein at 30°C. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C to -80°C for longer periods of time. Avoid multiple freeze-thaw cycles. Source: Baculovirus, SF9 insect cells. Species: Human. Focal adhesion kinase 1; EC 2.7.10.2; FADK 1; pp125FAK; Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Cat No: NATE-0800. | |
| Acu I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme about 80% of the dna fragments can be ligated. of these, 80% can be recut. Group: Restriction Enzymes. Purity: 50U; 250U. CTGAAG(N)16↑ GACTTC(N)14&darr. Activity: 1000u.a./ml. Appearance: 10 X SE-buffer Y, BSA, SAM. Storage: -20°C. Form: Liquid. Source: An. E.coli strain that carries the cloned Acu I gene from Acinetobacter calcoaceticus SRW4. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: RE-1013EN. | |
| aculeacin-A deacylase | This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase. Group: Enzymes. Synonyms: aculeacin A acylase. Enzyme Commission Number: EC 3.5.1.70. CAS No. 121479-50-3. 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-4461; aculeacin-A deacylase; EC 3.5.1.70; 121479-50-3; aculeacin A acylase. Cat No: EXWM-4461. | |
| acyl-[acyl-carrier-protein] 4-desaturase | The enzymes from the plants Coriandrum sativum (coriander) and Hedera helix (English ivy) are involved in biosynthesis of petroselinate [(6Z)-octadec-6-enoate], which is formed by elongation of (4Z)-hexadec-4-enoate. The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the corresponding 4,9-diene. Group: Enzymes. Synonyms: Δ4-palmitoyl-[acyl carrier protein] desaturase. Enzyme Commission Number: EC 1.14.19.11. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0973; acyl-[acyl-carrier-protein] 4-desaturase; EC 1.14.19.11; Δ4-palmitoyl-[acyl carrier protein] desaturase. Cat No: EXWM-0973. | |
| acyl-[acyl-carrier-protein] 6-desaturase | The enzyme, characterized from the endosperm of the plant Thunbergia alata (black-eyed Susan vine), introduces a cis double bond at carbon 6 of several saturated acyl-[acp]s. It is most active with palmitoyl-[acp] (16:0), but can also act on myristoyl-[acp] (14:0) and stearoyl-[acp] (18:0). The position of the double bond is determined by its distance from the carboxyl end of the fatty acid. Group: Enzymes. Synonyms: DELTA6 palmitoyl-ACP desaturase; DELTA6 16:0-ACP desaturase. Enzyme Commission Number: EC 1.14.19.26. 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-0989; acyl-[acyl-carrier-protein] 6-desaturase; EC 1.14.19.26; DELTA6 palmitoyl-ACP desaturase; DELTA6 16:0-ACP desaturase. Cat No: EXWM-0989. | |
| acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase | This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in glycerophospholipid metabolism. Group: Enzymes. Synonyms: acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase. Enzyme Commission Number: EC 2.3.1.40. CAS No. 37257-18-4. 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-2219; acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase; EC 2.3.1.40; 37257-18-4; acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase. Cat No: EXWM-2219. | |
| acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase | Involved with EC 2.4.1.182 (lipid-A-disaccharide synthase) and EC 2.7.1.130 (tetraacyldisaccharide 4'-kinase) in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Escherichia coli. Group: Enzymes. Synonyms: UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase. Enzyme Commission Number: EC 2.3.1.129. CAS No. 105843-69-4. 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-2066; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; EC 2.3.1.129; 105843-69-4; UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase. Cat No: EXWM-2066. | |
| acylagmatine amidase | Also acts on acetylagmatine, propanoylagmatine and bleomycin B2. Group: Enzymes. Synonyms: acylagmatine amidohydrolase; acylagmatine deacylase. Enzyme Commission Number: EC 3.5.1.40. CAS No. 39419-74-4. 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-4429; acylagmatine amidase; EC 3.5.1.40; 39419-74-4; acylagmatine amidohydrolase; acylagmatine deacylase. Cat No: EXWM-4429. | |
| acylaminoacyl-peptidase | Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Group: Enzymes. Synonyms: acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Enzyme Commission Number: EC 3.4.19.1. CAS No. 73562-30-8. 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-4082; acylaminoacyl-peptidase; EC 3.4.19.1; 73562-30-8; acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Cat No: EXWM-4082. | |
| Acylase I from Aspergillus sp., Immobilized on Eupergit C | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; &alpha. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 50 U/g moist material. Storage: 2-8°C. Source: Aspergillus sp. 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 acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0030. | |
| acylcarnitine hydrolase | Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine. Group: Enzymes. Synonyms: high activity acylcarnitine hydrolase; HACH; carnitine ester hydrolase; palmitoylcarnitine hydrolase; palmitoyl-L-carnitine hydrolase; long-chain acyl-L-carnitine hydrolase; palmitoyl carnitine hydrolase. Enzyme Commission Number: EC 3.1.1.28. CAS No. 37278-42-5. 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-3453; acylcarnitine hydrolase; EC 3.1.1.28; 37278-42-5; high activity acylcarnitine hydrolase; HACH; carnitine ester hydrolase; palmitoylcarnitine hydrolase; palmitoyl-L-carnitine hydrolase; long-chain acyl-L-carnitine hydrolase; palmitoyl carnitine hydrolase. Cat No: EXWM-3453. | |
| [acyl-carrier-protein] phosphodiesterase | The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species. Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo. Activation of apo-ACP to form the holoenzyme is carried out byEC 2.7.8.7, holo-[acyl-carrier-protein] synthase. Group: Enzymes. Synonyms: ACP hydrolyase; ACP phosphodiesterase; AcpH; [acyl-carrier-protein] 4'-pantetheine-phosphohydrolase; holo-[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase. Enzyme Commission Number: EC 3.1.4.14. CAS No. 37288-21-4. 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-3714; [acyl-carrier-protein] phosphodiesterase; EC 3.1.4.14; 37288-21-4; ACP hydrolyase; ACP phosphodiesterase; AcpH; [acyl-carrier-protein] 4'-pantetheine-phosphohydrolase; holo-[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase. Cat No: EXWM-3714. | |
| [acyl-carrier-protein] S-acetyltransferase | This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide. This is one of the activities associated with β-ketoacyl-ACP synthase III (EC 2.3.1.180). Group: Enzymes. Synonyms: acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]acetyltransferase; [ACP]acetyltransferase; ACAT; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. Enzyme Commission Number: EC 2.3.1.38. CAS No. 37257-16-2. 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-2216; [acyl-carrier-protein] S-acetyltransferase; EC 2.3.1.38; 37257-16-2; acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]acetyltransferase; [ACP]acetyltransferase; ACAT; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. Cat No: EXWM-2216. | |
| [acyl-carrier-protein] S-malonyltransferase | This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 (biotin-independent malonate decarboxylase) and EC 4.1.1.89 (biotin-dependent malonate decarboxylase). Malonylation of ACP is immediately followed by d. malonyl coenzyme A-acyl carrier protein transacylase; malonyl transacylase; malonyl transferase; malonyl-CoA-acyl carrier protein transacylase; malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase; malonyl-CoA:ACP transacylase; malonyl-CoA:ACP-SH transacylase; malonyl-CoA:AcpM transacylase; malonyl-CoA:acyl carrier protein transacylase; malonyl-CoA:acyl-carrier-protein transacylase; malonyl-CoA/dephospho-CoA acyltransferase; MAT; MCAT; MdcH. Enzyme Commission Number: EC 2.3.1.39. CAS No. 37257-17-3. 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-2217; [acyl-carrier-protein] S-malon. | |
| acyl-CoA 11-(E)-desaturase | Involved in sex pheromone synthesis in the Lepidoptera (moths). The enzyme from the moth Spodoptera littoralis prefers 13:0 and 14:0 substrates. The product is formed by the stereospecific removal of the pro-R H at C-11 and the pro-S H at C-12. cf. EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase. Group: Enzymes. Enzyme Commission Number: EC 1.14.19.24. CAS No. 199543-17-4. 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-0987; acyl-CoA 11-(E)-desaturase; EC 1.14.19.24; 199543-17-4. Cat No: EXWM-0987. | |
| acyl-CoA 11-(Z)-desaturase | The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0), that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0), while that from the moth Spodoptera littoralis accepts both substrates. The enzyme contains three histidine boxes that are conserved in all desaturases. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase. Group: Enzymes. Synonyms: Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11. Enzyme Commission Number: EC 1.14.19.5. 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-1013; acyl-CoA 11-(Z)-desaturase; EC 1.14.19.5; Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase; Δ11-fatty-acid desaturase. Cat No: EXWM-1013. | |
| acyl-CoA 15-desaturase | The enzyme, characterized from the the plant Sorghum bicolor, is involved in the biosynthesis of sorgoleone, an allelopathic compound produced in root hair cells. The enzyme inserts a cis double bond at carbon 15. When acting on its natural substrate, (9Z,12Z)-hexadeca-9,12-dienoyl-CoA, it produces a product with a terminal double bond. Group: Enzymes. Synonyms: DES3 (gene name). Enzyme Commission Number: EC 1.14.19.13. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0975; acyl-CoA 15-desaturase; EC 1.14.19.13; DES3 (gene name). Cat No: EXWM-0975. | |
| acyl-CoA 5-desaturase | The enzyme, characterized from the plant Anemone leveillei, introduces a cis double bond at carbon 5 of acyl-CoAs that do not contain a double bond at position 8. In vivo it forms non-methylene-interrupted polyunsaturated fatty acids such as sciadonate and juniperonate. When expressed in Arabidopsis thaliana the enzyme could also act on unsaturated substrates such as palmitoyl-CoA. cf. EC 1.14.19.44, acyl-CoA (8-3)-desaturase. Group: Enzymes. Synonyms: acyl-CoA 5-desaturase (non-methylene-interrupted). Enzyme Commission Number: EC 1.14.19.37. 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-1001; acyl-CoA 5-desaturase; EC 1.14.19.37; acyl-CoA 5-desaturase (non-methylene-interrupted). Cat No: EXWM-1001. | |
| acyl-CoA 6-desaturase | An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA, and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase. Group: Enzymes. Synonyms: Δ6-desatu. Enzyme Commission Number: EC 1.14.19.3. CAS No. 9082-66-0. 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-0993; acyl-CoA 6-desaturase; EC 1.14.19.3; 9082-66-0; Δ6-desaturase; Δ6-fatty acyl-CoA desaturase; Δ6-acyl CoA desaturase; fatty acid Δ6-desaturase; fatty acid 6-desaturase; linoleate desaturase; linoleic desaturase; linoleic acid desaturase; linoleoyl CoA desaturase; linoleoyl-coenzyme A desaturase; long-chain fatty acid Δ6-desaturase; linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase; linoleoyl-CoA desaturase; FADS2 (gene name). Cat No: EXWM-0993. | |
| acyl-CoA (8-3)-desaturase | The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8. The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyse the desaturation of dihomo-γ-linoleate [(8Z,11Z,14Z)-icosa-8,11,14-trienoate] and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37, acyl-CoA 5-desaturase. Group: Enzymes. Synonyms: FADS1 (gene name); acyl-CoA 5-desaturase (methylene-interrupted). Enzyme Commission Number: EC 1.14.19.44. 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-1009; acyl-CoA (8-3)-desaturase; EC 1.14.19.44; FADS1 (gene name); acyl-CoA 5-desaturase (methylene-interrupted). Cat No: EXWM-1009. | |
| acyl-CoA (9+3)-desaturase | This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Δ10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor. Group: Enzymes. Synonyms: oleoyl-CoA 12-desaturase; Δ12 fatty acid desaturase; Δ12(ω6)-desaturase; oleoyl-CoA Δ12 desaturase; Δ12 desaturase; Δ12-desaturase; Δ12-fatty-acid desaturase; acyl-CoA,hydrogen donor:oxygen Δ12-oxidoreductase. Enzyme Commission Number: EC 1.14.19.6. 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-1014; acyl-CoA (9+3)-desaturase; EC 1.14.19.6; oleoyl-CoA 12-desaturase; Δ12 fatty acid desaturase; Δ12(ω6)-desaturase; oleoyl-CoA Δ12 desaturase; Δ12 desaturase; Δ12-desaturase; Δ12-fatty-acid desaturase; acyl-CoA,hydrogen donor:oxygen Δ12-oxidoreductase. Cat No: EXWM-1014. | |
| acyl-CoA dehydrogenase (NADP+) | The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)]. Group: Enzymes. Synonyms: 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP+). Enzyme Commission Number: EC 1.3.1.8. CAS No. 37251-07-3. 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-1349; acyl-CoA dehydrogenase (NADP+); EC 1.3.1.8; 37251-07-3; 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP+). Cat No: EXWM-1349. | |
| acyl-CoA hydrolase | Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase). Group: Enzymes. Synonyms: acyl coenzyme A thioesterase; acyl-CoA thioesterase; acyl coenzyme A hydrolase; thioesterase B; thioesterase II; acyl-CoA thioesterase. Enzyme Commission Number: EC 3.1.2.20. CAS No. 37270-64-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3555; acyl-CoA hydrolase; EC 3.1.2.20; 37270-64-7; acyl coenzyme A thioesterase; acyl-CoA thioesterase; acyl coenzyme A hydrolase; thioesterase B; thioesterase II; acyl-CoA thioesterase. Cat No: EXWM-3555. | |
| acyl-CoA oxidase | A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. Group: Enzymes. Synonyms: fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Acyl-CoA oxidase. 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-1380; acyl-CoA oxidase; EC 1.3.3.6; 61116-22-1; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase. Cat No: EXWM-1380. | |
| Acyl-CoA oxidase from Microorganism | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2? trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Mole weight: 78 kDa (SDS-PAGE). Activity: >30U/mg protein. Storage: Store at -20°C. Form: Yellow powder, lyophilized. Source: Microorganism. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Cat No: NATE-1711. | |
| Acyl-CoA oxidase, Recombinant | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Purity: 90% (SDS-PAGE test). Acyl-CoA oxidase. Mole weight: About 90KDa (SDS-PAGE detection). Activity: 40U/mg protein. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preservation. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-292. | |
| Acyl-CoA synthetase from Microorganism | Acetylcoenzyme A synthetase (ACS, EC 6.2.1.3)catalyzes the formation of acetyl coenzyme A with free fatty acids and coenzyme A. The ACS provided by our company is gene recombinant protein. It is of high purity and good activity. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetas. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. Mole weight: 63 kDa (SDS-PAGE). Activity: >20U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: NATE-1712. | |
| Acyl-CoA synthetase, recombinant | Acetylcoenzyme A synthetase (ACS, EC 6.2.1.3)catalyzes the formation of acetyl coenzyme A with free fatty acids and coenzyme A. The ACS provided by our company is gene recombinant protein. It is of high purity and good activity. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. Purity: 90% (SDS-PAGE test). ACS3. Mole weight: About 70kDa (SDS-PAGE detection). Activity: 30U/mg protein. Storage: 4°C,store at -20°C for long-term preservation. Form: White powder, lyophilized. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: NATE-1682. | |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f.mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| acylglycerol kinase | Acts on both 1- and 2-acylglycerols. Group: Enzymes. Synonyms: monoacylglycerol kinase; monoacylglycerol kinase (phosphorylating); sn-2-monoacylglycerol kinase; MGK; monoglyceride kinase; monoglyceride phosphokinase. Enzyme Commission Number: EC 2.7.1.94. CAS No. 62213-37-0. 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-3124; acylglycerol kinase; EC 2.7.1.94; 62213-37-0; monoacylglycerol kinase; monoacylglycerol kinase (phosphorylating); sn-2-monoacylglycerol kinase; MGK; monoglyceride kinase; monoglyceride phosphokinase. Cat No: EXWM-3124. | |
| acylglycerol lipase | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism. Group: Enzymes. Synonyms: monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Enzyme Commission Number: EC 3.1.1.23. CAS No. 9040-75-9. Monoglyceride lipase. 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-3448; acylglycerol lipase; EC 3.1.1.23; 9040-75-9; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Cat No: EXWM-3448. | |
| acylglycerone-phosphate reductase | Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate. Group: Enzymes. Synonyms: palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase. Enzyme Commission Number: EC 1.1.1.101. CAS No. 37250-35-4. 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-0004; acylglycerone-phosphate reductase; EC 1.1.1.101; 37250-35-4; palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase. Cat No: EXWM-0004. | |
| acyl-homoserine-lactone acylase | Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine l.ion, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity. Group: Enzymes. Synonyms: acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Enzyme Commission Number: EC 3.5.1.97. 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-4489; acyl-homoserine-lactone acylase; EC 3.5.1.97; acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Cat No: EXWM-4489. | |
| acyl-homoserine-lactone synthase | Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. N-(3-Oxohexanoyl)-[acyl-carrier protein] and hexanoyl-[acyl-carrier protein] are the best substrates. The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier protein] rather than from fatty-acid degradation through acyl-CoA. S-Adenosyl-L-methionine cannot be rep.No. 176023-66-8. 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-2126; acyl-homoserine-lactone synthase; EC 2.3.1.184; 176023-66-8; acyl-homoserine lactone synthase; acyl homoserine lactone synthase; acyl-homoserinelactone synthase; acylhomoserine lactone synthase; AHL synthase; AHS; AHSL synthase; AhyI; AinS; AinS protein; autoinducer synthase; autoinducer synthesis protein rhlI; EsaI; ExpISCC1; ExpISCC3065; LasI; LasR; LuxI; LuxI protein; LuxM; N-acyl homoserine lactone synthase; RhlI; YspI acyl-[acyl carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadeno. | |
| acyl-lipid (11-3)-desaturase | The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina, introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Δ11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate. Group: Enzymes. Synonyms: acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen &Delta. Enzyme Commission Number: EC 1.14.19.4. 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-1004; acyl-lipid (11-3)-desaturase; EC 1.14.19.4; acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase (incorrect); SLD. Cat No: EXWM-1004. | |
| acyl-lipid (7-3)-desaturase | The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Δ7 double bond. The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate. The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Group: Enzymes. Synonyms: D4Des (gene name); des1 (gene name); CrΔ4FAD (gene name); acyl-lipid 4-desaturase. Enzyme Commission Number: EC 1.14.19.31. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0995; acyl-lipid (7-3)-desaturase; EC 1.14.19.31; D4Des (gene name); des1 (gene name); CrΔ4FAD (gene name); acyl-lipid 4-desaturase. Cat No: EXWM-0995. | |
| acyl-lipid (8-3)-desaturase | The enzyme, which has been characterized from multiple organisms including the moss Physcomitrella patens, the marine microalga Rebecca salina, and the filamentous fungus Mortierella alpina, introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Δ8 double bond. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Group: Enzymes. Synonyms: acyl-lipid 5-desaturase; Δ5-fatty-acid desaturase; DES5 (gene name); D5des (gene name); FADS1. Enzyme Commission Number: EC 1.14.19.30. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0994; acyl-lipid (8-3)-desaturase; EC 1.14.19.30; acyl-lipid 5-desaturase; Δ5-fatty-acid desaturase; DES5 (gene name); D5des (gene name); FADS1. Cat No: EXWM-0994. | |
| acyl-lipid (9-3)-desaturase | The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Δ9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase. Group: Enzymes. Synonyms: acyl-lipid 6-desaturase; Δ6-desaturase; DES6 (gene name). Enzyme Commission Number: EC 1.14.19.47. 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-1012; acyl-lipid (9-3)-desaturase; EC 1.14.19.47; acyl-lipid 6-desaturase; Δ6-desaturase; DES6 (gene name). Cat No: EXWM-1012. | |
| acyl-lipid (9+3)-(E)-desaturase | The enzymes from the plants Dimorphotheca sinuata (African daisy) and Vernicia fordii (tung oil tree) insert a trans double bond in position C-12 of oleate and palmitoleate incorporated into glycerolipids. The enzyme introduces the new double bond at a position three carbons away from an existing double bond at position 9, towards the methyl end of the fatty acid. The enzyme from tung oil tree also possesses the activity of EC 1.14.19.33, Δ12 acyl-lipid conjugase. Group: Enzymes. Synonyms: acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX. Enzyme Commission Number: EC 1.14.19.34. 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-0998; acyl-lipid (9+3)-(E)-desaturase; EC 1.14.19.34; acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX. Cat No: EXWM-0998. | |
| acyl-lipid Δ12-acetylenase | The enzyme, characterized from the plant Crepis alpina, converts the double bond at position 12 of linoleate into a triple bond. The product is the main fatty acid found in triacylglycerols in the seed oil of Crepis alpina. Group: Enzymes. Enzyme Commission Number: EC 1.14.19.39. 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-1003; acyl-lipid Δ12-acetylenase; EC 1.14.19.39. Cat No: EXWM-1003. | |
| acyl-lipid Δ6-acetylenase | The enzyme, characterized from the moss Ceratodon purpureus, converts the double bond at position 6 of γ-linolenate and stearidonate into a triple bond. The product of the latter, dicranin, is the main fatty acid found in C. purpureus. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The enzyme also has the activity of EC 1.14.19.47, acyl-lipid (9-3)-desaturase. Group: Enzymes. Enzyme Commission Number: EC 1.14.19.38. 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-1002; acyl-lipid Δ6-acetylenase; EC 1.14.19.38. Cat No: EXWM-1002. | |
| acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) | This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids. The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, towards the methyl end of the fatty acid. The native substrates are oleoyl (18:1 Δ9) and (Z)-hexadec-7-enoyl (16:1 Δ7) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an ω6 desaturase. However, when acting on palmitoleoyl groups(16:1 Δ9), the enzyme introduces the second double bond at position 12 (ω4), indicating it is an (n+3) desaturase. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase. Group: Enzymes. Synonyms: acyl-. Enzyme Commission Number: EC 1.14.19.23. 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-0986; acyl-lipid (n+3)-(Z)-desaturase (ferredoxin); EC 1.14.19.23; acyl-lipid ω6-desaturase (ferredoxin); oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (ambiguous); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); FAD6 (gene name). Cat No: EXWM-0986. | |
| acyl-lipid ω-3 desaturase (cytochrome b5) | This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid. The distance from the carboxylic acid end of the molecule does not have an effect. The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into α-linolenoyl groups. The enzyme from the fungus Mortierella alpina acts on γ-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively. cf. EC 1.14.19.35, acyl-lipid ω-3 desaturase (ferredoxin). Group: Enzymes. Synonyms: FAD3. Enzyme Commission Number: EC 1.14.19.25. 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-0988; acyl-lipid ω-3 desaturase (cytochrome b5); EC 1.14.19.25; FAD3. Cat No: EXWM-0988. | |
| acyl-lipid ω-6 desaturase (cytochrome b5) | This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid ω-6 desaturase (ferredoxin). Group: Enzymes. Synonyms: oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name). Enzyme Commission Number: EC 1.14.19.22. CAS No. 72536-70-0. 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-0985; acyl-lipid ω-6 desaturase (cytochrome b5); EC 1.14.19.22; 72536-70-0; oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name). Cat No: EXWM-0985. | |
| acyl-lipid ω-(9-4) desaturase | The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in ω9 unsaturated C18 or C20 fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing ω9 bond, towards the carboxy end of the fatty acid (at the ω13 position). When acting on 20:2Δ(11,14) and 20:3Δ(11,14,17) substrates it introduces the new double bond between carbons 7 and 8. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor for the active site of the desaturase. Group: Enzymes. Synonyms: acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.12. 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-0974; acyl-lipid ω-(9-4) desaturase; EC 1.14.19.12; acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous). Cat No: EXWM-0974. | |
| acyl-lysine deacylase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acyl-L-lysine amidohydrolase. Other names in common use include epsilon-lysine acylase, and 6-N-acyl-L-lysine amidohydrolase. This enzyme participates in lysine degradation. Group: Enzymes. Synonyms: ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Enzyme Commission Number: EC 3.5.1.17. CAS No. 9025-11-0. 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-4406; acyl-lysine deacylase; EC 3.5.1.17; 9025-11-0; ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Cat No: EXWM-4406. | |
| acyloxyacyl hydrolase | The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, β-D-GlcN-(1? 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups. Group: Enzymes. Enzyme Commission Number: EC 3.1.1.77. CAS No. 110277-64-0. 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-3505; acyloxyacyl hydrolase; EC 3.1.1.77; 110277-64-0. Cat No: EXWM-3505. | |
| acylphosphatase | This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides.This enzyme participates in 3 metabolic pathways: glycolysis/gluconeogenesis, pyruvate metabolism, and benzoate degradation via coa ligation. Group: Enzymes. Synonyms: acetylphosphatase; 1,3-diphosphoglycerate phosphatase; acetic phosphatase; Ho 1-3; GP 1-3. Enzyme Commission Number: EC 3.6.1.7. CAS No. 9012-34-4. 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-4641; acylphosphatase; EC 3.6.1.7; 9012-34-4; acetylphosphatase; 1,3-diphosphoglycerate phosphatase; acetic phosphatase; Ho 1-3; GP 1-3. Cat No: EXWM-4641. | |
| acyl-phosphate-hexose phosphotransferase | Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6. Group: Enzymes. Synonyms: hexose phosphate:hexose phosphotransferase. Enzyme Commission Number: EC 2.7.1.61. CAS No. 37278-06-1. 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-3092; acyl-phosphate-hexose phosphotransferase; EC 2.7.1.61; 37278-06-1; hexose phosphate:hexose phosphotransferase. Cat No: EXWM-3092. | |
| acylpyruvate hydrolase | Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate. Group: Enzymes. Enzyme Commission Number: EC 3.7.1.5. CAS No. 54004-67-0. 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-4734; acylpyruvate hydrolase; EC 3.7.1.5; 54004-67-0. Cat No: EXWM-4734. | |
| ADAM10 endopeptidase | In peptidase family M12. Partially responsible for the "α-secretase" activity in brain that degrades the potentially harmful β-amyloid peptide. Work with ADAM10-deficient mice supports a role in Notch signalling. Group: Enzymes. Synonyms: Kuzbanian protein; myelin-associated disintegrin metalloproteinase. Enzyme Commission Number: EC 3.4.24.81. CAS No. 193099-09-1. 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-4365; ADAM10 endopeptidase; EC 3.4.24.81; 193099-09-1; Kuzbanian protein; myelin-associated disintegrin metalloproteinase. Cat No: EXWM-4365. | |
| ADAM 17 endopeptidase | In peptidase family M12. In vivo, the cleavage of tumour necrosis factor α precursor releases the soluble, 17-kDa TNFα, which induces inflammation. Group: Enzymes. Synonyms: tumor necrosis factor α-converting enzyme; TACE. Enzyme Commission Number: EC 3.4.24.86. CAS No. 151769-16-3. 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-4370; ADAM 17 endopeptidase; EC 3.4.24.86; 151769-16-3; tumor necrosis factor α-converting enzyme; TACE. Cat No: EXWM-4370. | |
| adamalysin | From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Enzyme Commission Number: EC 3.4.24.46. CAS No. 74812-51-4. 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-4328; adamalysin; EC 3.4.24.46; 74812-51-4; Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Cat No: EXWM-4328. | |
| Adamantanyl Galactosyl(ss) Ceramide | Adamantanyl Galactosyl(ss) Ceramide. Group: Others. Synonyms: AdaGalCer. Purity: >99%. Mole weight: 637.887. Stability: 1 Year. Storage: -20°C. AdaGalCer; Adamantanyl Galactosyl(ss) Ceramide; N-(1-Adamantaneacetyl)-galactosylceramide. Cat No: SPHZ-005. | |
| ADAMTS13 endopeptidase | In peptidase family M12. Group: Enzymes. Synonyms: ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Enzyme Commission Number: EC 3.4.24.87. 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-4371; ADAMTS13 endopeptidase; EC 3.4.24.87; ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Cat No: EXWM-4371. | |
| ADAMTS-4 endopeptidase | In peptidase family M12. Thought to be biologically significant for the degradation of the aggrecan component of cartilage matrix. Group: Enzymes. Synonyms: aggrecanase-1. Enzyme Commission Number: EC 3.4.24.82. CAS No. 147172-61-0. 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-4366; ADAMTS-4 endopeptidase; EC 3.4.24.82; 147172-61-0; aggrecanase-1. Cat No: EXWM-4366. | |
| Ademetionine | Ademetionine is a common co-substrate involved in methyl group transfers. Applications: A common co-substrate involved in methyl group transfers. Group: Coenzymes. Synonyms: S-Adenosyl-L-methionine; SAMe; AdoMet. CAS No. 29908-03-0. Purity: ≥95%. Mole weight: 398.44. Form: Solid. S-Adenosyl-L-methionine; SAMe; AdoMet; Ademetionine; 29908-03-0. Cat No: COEC-097. | |
| adenain | A cysteine endopeptidase from adenoviruses, the type example of peptidase family C5, with a protein fold unlike that known for any other peptidase. Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.39. CAS No. 369652-03-9. 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-4214; adenain; EC 3.4.22.39; 369652-03-9. Cat No: EXWM-4214. | |
| adenine deaminase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase, and ADase. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: adenase; adenine aminase; ADase. Enzyme Commission Number: EC 3.5.4.2. CAS No. 9027-68-3. 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-4546; adenine deaminase; EC 3.5.4.2; 9027-68-3; adenase; adenine aminase; ADase. Cat No: EXWM-4546. | |
| adenine phosphoribosyltransferase | 5-Amino-4-imidazolecarboxamide can replace adenine. Group: Enzymes. Synonyms: AMP pyrophosphorylase; transphosphoribosidase; APRT; AMP-pyrophosphate phosphoribosyltransferase; adenine phosphoribosylpyrophosphate transferase; adenosine phosphoribosyltransferase; adenylate pyrophosphorylase; adenylic pyrophosphorylase. Enzyme Commission Number: EC 2.4.2.7. CAS No. 9027-80-9. APRT. 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-2690; adenine phosphoribosyltransferase; EC 2.4.2.7; 9027-80-9; AMP pyrophosphorylase; transphosphoribosidase; APRT; AMP-pyrophosphate phosphoribosyltransferase; adenine phosphoribosylpyrophosphate transferase; adenosine phosphoribosyltransferase; adenylate pyrophosphorylase; adenylic pyrophosphorylase. Cat No: EXWM-2690. | |
| Adenosine 3',5'-cyclic monophosphate Monosodium salt | Adenosine-3',5'-cyclic monophosphate (cAMP) is an activator of cyclic-AMP-dependent protein kinase A (PKA). The cAMP/PKA signaling pathway has been shown to inhibit cell proliferation, induce differentiation and lead to apoptosis. Exogneous cAMP plays a role in the spontaneous activity and contraction of the heart muscle. Group: Coenzymes. Synonyms: Adenosine 3',5'-cyclic monophosphate; cAMP; cAMP Monosodium salt; Adenosine 3',5'-cyclic monophosphate Monosodium salt; cAMP-Na. Mole weight: 351.19. Storage: Store at -20° C. Form: Crystalline powder. Adenosine 3',5'-cyclic monophosphate; cAMP; cAMP Monosodium salt; Adenosine 3',5'-cyclic monophosphate Monosodium salt; cAMP-Na. Cat No: COEC-119. | |
| Adenosine 5'-diphosphate Disodium salt | Adenosine 5'-diphosphate (ADP) is used in the determination of creatine kinase, glutamate dehydrogenase, urea and ammonia. Group: Coenzymes. Synonyms: Adenosine 5'-diphosphate; ADP; Adenosine 5'-diphosphate Disodium salt; ADP Disodium salt; ADP-Na2. Mole weight: 507.2. Storage: Store at -20° C. Form: Crystalline powder. Adenosine 5'-diphosphate; ADP; Adenosine 5'-diphosphate Disodium salt; ADP Disodium salt; ADP-Na2. Cat No: COEC-120. | |
| Adenosine-5'-diphosphate?Na2-salt | Adenosine-5'-diphosphate?Na2-salt. Group: Coenzymes. Synonyms: ADP; Adenosine-5'-diphosphate?Na2-salt. CAS No. 16178-48-6. Purity: 0.94. Mole weight: 471.2. Appearance: White powder. Storage: -15 °C to -25 °C. coenzyme; Adenosine-5'-diphosphate?Na2-salt; ADP; 16178-48-6. Cat No: COEZ-001. | |
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