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| Product | Description | |
|---|---|---|
| anthocyanin 5-O-glucoside 6'''-O-malonyltransferase | Specific for the penultimate step in salvianin biosynthesis. The enzyme also catalyses the malonylation of shisonin to malonylshisonin [cyanidin 3-O-(6''-O-p-coumaryl-β-D-glucoside)-5-(6'''-O-malonyl-β-D-glucoside)]. The compounds 4'''-demalonylsalvianin, salvianin, pelargonidin 3,5-diglucoside and delphinidin 3,5-diglucoside cannot act as substrates. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.172. CAS No. 380229-66-3. 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-2113; anthocyanin 5-O-glucoside 6'''-O-malonyltransferase; EC 2.3.1.172; 380229-66-3. Cat No: EXWM-2113. |  |
| aralkylamine N-acetyltransferase | Narrow specificity towards 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase). Differs from EC 2.3.1.5 arylamine N-acetyltransferase. Group: Enzymes. Synonyms: serotonin acetyltransferase; serotonin acetylase; arylalkylamine N-acetyltransferase; serotonin N-acetyltransferase; AANAT; melatonin rhythm enzyme. Enzyme Commission Number: EC 2.3.1.87. CAS No. 92941-56-5. 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-2268; aralkylamine N-acetyltransferase; EC 2.3.1.87; 92941-56-5; serotonin acetyltransferase; serotonin acetylase; arylalkylamine N-acetyltransferase; serotonin N-acetyltransferase; AANAT; melatonin rhythm enzyme. Cat No: EXWM-2268. | |
| Cystathionine β-lyase, Recombinant Microorganisms | Cystathionine β-lyase, Recombinant Microorganisms (CBL) is an enzyme that catalyzes the breakdown of cystathionine to homocysteine, the penultimate step in methionine biosynthesis. Cystathionine β-lyase is important for bacterial virulence [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: CBL. CAS No. 9055-5-4. Pack Sizes: 100 U; 500 U. Product ID: HY-E70079. |  |
| lacto-N-biosidase | The enzyme from Streptomyces specifically hydrolyses the terminal lacto-N-biosyl residue (β-D-Gal-(1?3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure β-D-Gal-(1?3)-β-D-GlcNAc-(1?3)-β-D-Gal-(1?R). Lacto-N-hexaose (β-D-Gal-(1?3)-β-D-GlcNAc-(1?3)-β-D-Gal-(1?3)-β-D-GlcNAc-(1?3)-β-D-Gal-(1?4)-D-Glc) is hydrolysed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. Asialo GM1 tetraose (β-D-Gal-(1?3)-β-D-GalNAc-(1?3)-β-D-Gal-(1?4)-D-Glc) is hydrolysed very slowly, but lacto-N-neotetraose (β-D-Gal-(1?4)-β-D-GalNAc-(1?3)-β-D-Gal-(1?4)-D-Glc) is not a substrate. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.140. CAS No. 146359-52-6. 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-3823; lacto-N-biosidase; EC 3.2.1.140; 146359-52-6. Cat No: EXWM-3823. | |
| methionyl aminopeptidase | This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). Group: Enzymes. Synonyms: methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Enzyme Commission Number: EC 3.4.11.18. CAS No. 61229-81-0. MAP. 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-4014; methionyl aminopeptidase; EC 3.4.11.18; 61229-81-0; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP. Cat No: EXWM-4014. | |
| methylecgonone reductase | The enzyme from the plant Erythroxylum coca catalyses the penultimate step in the biosynthesis of cocaine. In vivo the reaction proceeds in the opposite direction. With NADH instead of NADPH the reaction rate is reduced to 14%. The enzyme also reduces tropinone, nortropinone and 6-hydroxytropinone but with lower reaction rates. Group: Enzymes. Synonyms: MecgoR (gene name). Enzyme Commission Number: EC 1.1.1.334. 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-0248; methylecgonone reductase; EC 1.1.1.334; MecgoR (gene name). Cat No: EXWM-0248. | |
| Native Bovine Cathepsin C | Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators. Applications: Cathepsin c has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. catheps...s. Synonyms: CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Enzyme Commission Number: EC 3.4.14.1. CAS No. 9032-68-2. CTSC. Activity: > 5 units/mg protein. Form: Lyophilized from a 1 M sodium chloride solution. Source: Bovine spleen. Species: Bovine. CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Cat No: NATE-0170. | |
| Native Streptomyces griseus Aminopeptidase I | Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070. | |
| oligosaccharide reducing-end xylanase | The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure β-D-xylopyranosyl-(1?4)-β-D-xylopyranosyl-(1?4)-β-D-xylopyranose, leaving the new reducing end in the α configuration. It is specific for the β anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3.The penultimate residue must be β-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly. Group: Enzymes. Synonyms: Rex; reducing end xylose-releasing exo-oligoxylanase. Enzyme Commission Number: EC 3.2.1.156. CAS No. 879497-03-7. Oligosaccharide reducing-end xylanase. 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-3839; oligosaccharide reducing-end xylanase; EC 3.2.1.156; 879497-03-7; Rex; reducing end xylose-releasing exo-oligoxylanase. Cat No: EXWM-3839. | |
| peptidylglycine monooxygenase | A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. Involved in the final step of biosynthesis of α-melanotropin and related biologically active peptides. Group: Enzymes. Synonyms: peptidylglycine 2-hydroxylase; peptidyl α-amidating enzyme; peptide-α-amide synthetase; synthase, peptide α-amide; peptide α-amidating enzyme; peptide α-amide synthase; peptidylglycine α-hydroxylase; peptidylglycine α-amidating monooxygenase; PAM-A; PAM-B; PAM. Enzyme Commission Number: EC 1.14.17.3. CAS No. 90597-47-0. 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-0961; peptidylglycine monooxygenase; EC 1.14.17.3; 90597-47-0; peptidylglycine 2-hydroxylase; peptidyl α-amidating enzyme; peptide-α-amide synthetase; synthase, peptide α-amide; peptide α-amidating enzyme; peptide α-amide synthase; peptidylglycine α-hydroxylase; peptidylglycine α-amidating monooxygenase; PAM-A; PAM-B; PAM. Cat No: EXWM-0961. | |
| propanoyl-CoA C-acyltransferase | Also acts on dihydroxy-5β-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase. Group: Enzymes. Synonyms: SCP2 (gene name); peroxisomal thiolase 2; sterol carrier protein-χ; SCPχ; PTE-2 (ambiguous); propionyl-CoA C2-trimethyltridecanoyltransferase; 3-oxopristanoyl-CoA hydrolase; 3-oxopristanoyl-CoA thiolase; peroxisome sterol carrier protein thiolase; sterol carrier protein; oxopristanoyl-CoA thiolase; . Enzyme Commission Number: EC 2.3.1.176. 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-2117; propanoyl-CoA C-acyltransferase; EC 2.3.1.176; SCP2 (gene name); peroxisomal thiolase 2; sterol carrier protein-χ; SCPχ; PTE-2 (ambiguous); propionyl-CoA C2-trimethyltridecanoyltransferase; 3-oxopristanoyl-CoA hydrolase; 3-oxopristanoyl-CoA thiolase; peroxisome sterol carrier protein thiolase; sterol carrier protein; oxopristanoyl-CoA thiolase; peroxisomal 3-oxoacyl coenzyme A thiolase; SCPx; 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA 2-C-4,8,12-trimethyltridecanoyltransferase. Cat No: EXWM-2117. | |
| thiamine phosphate synthase | The enzyme catalyses the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. The enzyme is thought to accept the product of EC 2.8.1.10, thiazole synthase, as its substrate. However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, thiazole tautomerase (EC 5.3.99.10) converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiami...-diphosphate:4-methyl-5-(2-phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Enzyme Commission Number: EC 2.5.1.3. CAS No. 9030-30-2. 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-2767; thiamine phosphate synthase; EC 2.5.1.3; 9030-30-2; thiamine phosphate pyrophosphorylase; thiamine monophosphate pyrophosphorylase; TMP-PPase; thiamine-phosphate diphosphorylase; thiE (gene name); TH1 (gene name); THI6 (gene name); 2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2-phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Cat No: EXWM-2767. | |
| UDP-glucose-glycoprotein glucose phosphotransferase | Penultimate mannose residues on oligo-mannose type glycoproteins can act as acceptors. Group: Enzymes. Synonyms: UDP-glucose:glycoprotein glucose-1-phosphotransferase; GlcPTase; Glc-phosphotransferase; uridine diphosphoglucose-glycoprotein glucose-1-phosphotransferase. Enzyme Commission Number: EC 2.7.8.19. CAS No. 84861-40-5. 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-3318; UDP-glucose-glycoprotein glucose phosphotransferase; EC 2.7.8.19; 84861-40-5; UDP-glucose:glycoprotein glucose-1-phosphotransferase; GlcPTase; Glc-phosphotransferase; uridine diphosphoglucose-glycoprotein glucose-1-phosphotransferase. Cat No: EXWM-3318. | |
| vestitone reductase | This plant enzyme catalyses the penultimate step in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. This activity was previously classified as part of EC 1.1.1.246, pterocarpin synthase, which is now known to be catalysed by two enzymes, vestitone reductase and EC 4.2.1.139, medicarpin synthase. Group: Enzymes. Synonyms: pterocarpin synthase (incorrect); pterocarpan synthase (incorrect). Enzyme Commission Number: EC 1.1.1.348. CAS No. 118477-70-6. 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-0263; vestitone reductase; EC 1.1.1.348; 118477-70-6; pterocarpin synthase (incorrect); pterocarpan synthase (incorrect). Cat No: EXWM-0263. | |
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