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 | |
|---|---|---|
| carbon disulfide lyase | The enzyme contains Zn2+. The hyperthermophilic archaeon Acidianus sp. A1-3 obtains energy by the conversion of carbon disulfide to hydrogen sulfide, with carbonyl sulfide as an intermediate. Group: Enzymes. Synonyms: CS2 hydrolase (misleading); carbon disulfide hydrolase (misleading); CS2-converting enzyme; carbon disulphide-lyase (decarboxylating). Enzyme Commission Number: EC 4.4.1.27. 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-5329; carbon disulfide lyase; EC 4.4.1.27; CS2 hydrolase (misleading); carbon disulfide hydrolase (misleading); CS2-converting enzyme; carbon disulphide-lyase (decarboxylating). Cat No: EXWM-5329. |  |
| 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. | |
| carbon-monoxide dehydrogenase (cytochrome b-561) | Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors. Group: Enzymes. Synonyms: carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase; CO dehydrogenase; carbon-monoxide dehydrogenase. Enzyme Commission Number: EC 1.2.2.4. CAS No. 395639-79-9. 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-1205; carbon-monoxide dehydrogenase (cytochrome b-561); EC 1.2.2.4; 395639-79-9; carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase; CO dehydrogenase; carbon-monoxide dehydrogenase. Cat No: EXWM-1205. | |
| carbonyl reductase (NADPH) | Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Enzyme Commission Number: EC 1.1.1.184. CAS No. 89700-36-7. 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-0086; carbonyl reductase (NADPH); EC 1.1.1.184; 89700-36-7; aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Cat No: EXWM-0086. | |
| carboxybiotin decarboxylase | The integral membrane protein MadBfrom the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 4.1.1.3 (oxaloacetate decarboxylase) and EC 4.1.1.41 (methylmalonyl-CoA decarboxylase). Group: Enzymes. Synonyms: MadB; carboxybiotin protein decarboxylase. Enzyme Commission Number: EC 7.2.4.1 (Formerly EC 4.3.99.2). 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-5309; carboxybiotin decarboxylase; EC 4.3.99.2; MadB; carboxybiotin protein decarboxylase. Cat No: EXWM-5309. | |
| carboxy-cis,cis-muconate cyclase | This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. This enzyme participates in benzoate degradation via hydroxylation. Group: Enzymes. Synonyms: 3-carboxymuconate cyclase; 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). Enzyme Commission Number: EC 5.5.1.5. CAS No. 37318-55-1. 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-5631; carboxy-cis,cis-muconate cyclase; EC 5.5.1.5; 37318-55-1; 3-carboxymuconate cyclase; 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). Cat No: EXWM-5631. | |
| (carboxyethyl)arginine β-lactam-synthase | Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It has been proposed that L-N2-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the β-lactam ring is then formed by the intramolecular attack of the β-nitrogen on the activated carboxy group. Group: Enzymes. Synonyms: L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). Enzyme Commission Number: EC 6.3.3.4. 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-5776; (carboxyethyl)arginine β-lactam-synthase; EC 6.3.3.4; L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). Cat No: EXWM-5776. | |
| carboxylate reductase | A tungsten protein. Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols. Group: Enzymes. Synonyms: aldehyde:(acceptor) oxidoreductase. Enzyme Commission Number: EC 1.2.99.6. CAS No. 125008-36-8. 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-1234; carboxylate reductase; EC 1.2.99.6; 125008-36-8; aldehyde:(acceptor) oxidoreductase. Cat No: EXWM-1234. | |
| carboxylesterase | Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters. Group: Enzymes. Synonyms: ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester h. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. 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-3434; carboxylesterase; EC 3.1.1.1; 9016-18-6; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Cat No: EXWM-3434. | |
| Carboxylesterase 1D from Mouse, Recombinant | Ces1d, also known as carboxylesterase 1D, is a member of a large family of carboxylesterases that are responsible for the hydrolysis of ester and amide bonds. It is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity as well as lesser but detectable neutral cholesteryl ester hydrolase activity. The protein shows low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics. Recombinant mouse Ces1d, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Ces1d; Carboxylesterase 3; FAEE synthase; TGH; Ces3. Purity: > 90% by SDS-PAGE. Esterase. Mole weight: 60.9 kDa. Activity: > 80,000 pmol/min/ug. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: Insect cell (Baculovirus) and fused to His-tag at N-terminus. Species: Mouse. Ces1d; Carboxylesterase 3; FAEE synthase; TGH; Ces3; Carboxylesterase 1D. Cat No: NATE-1633. | |
| Carboxylesterase 1 isoform b from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic.er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥500 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxyl. | |
| Carboxylesterase 1 isoform c from Human, Recombinant | Carboxylesterase 1 is a member of a large multigene carboxylesterase family. These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolyze long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Applications: Delivers high catalytic activity, ideal for robust high-throughput screening assays including drug-drug interaction studies, and pharmacokinetic.er: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ≥1000 units/mg protein. Storage: at -70°C. Form: Liquid. Source: Baculovirus infected BTI insect cells. Species: Human. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxy. | |
| Carboxylesterase 2 from Human, Recombinant | Member of a serine esterase family that hydrolyze ester and amide bonds. Carboxylesterase 2 is an endoplasmic reticulum-bound hydrolase that plays a critical role in xenobiotic detoxification and activation for ester-containing therapeutics. Carboxylesterase 2 is also involved in the detoxification of drugs such as heroin and cocaine. This enzyme is thought to play a role in lipid metabolism. Human carboxylesterase 2 (hCE-2) recognizes a substrate with a large alcohol group and small acyl group. Its substrate specificity may be restricted by a capability of acyl-hCE-2 conjugate formation due to the presence of conformational interference in the active site pocket. Carboxylesterases catalyze the biotransformation of several ester-containing drugs and prodrugs such as angiotensin-converting enzyme inhibitor (temocarpil, cilazapril), anti-tumor drugs (capecitabin) and narcotics. Group: Enzymes. Synonyms: EC 3.1.1.1; Carboxylesterase 2; CES2; CES2A1; CE-2. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Purity: >95% (SDS-PAGE). Esterase. Mole weight: ~60 kDa. Activity: >30,000 (pmol/min/μg). Storage: Store at -70°C. Form: Supplied as a solution containing sodium chloride, sodium acetate, and 20% glycerol. Source: Mouse NSO cells. Species: Human. EC 3.1.1.1; Carboxylesterase 2; CES2; CES2A1; CE-2; PCE-2; iCE. Cat No: NATE-0812. | |
| carboxylic acid-CoA ligase (GDP-forming) | This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. Group: Enzymes. Synonyms: acyl-CoA synthetase (GDP-forming); acyl coenzyme A synthetase (guanosine diphosphate forming). Enzyme Commission Number: EC 6.2.1.10. CAS No. 37318-59-5. 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-5668; carboxylic acid-CoA ligase (GDP-forming); EC 6.2.1.10; 37318-59-5; acyl-CoA synthetase (GDP-forming); acyl coenzyme A synthetase (guanosine diphosphate forming). Cat No: EXWM-5668. | |
| carboxymethylenebutenolidase | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation. Group: Enzymes. Synonyms: maleylacetate enol-lactonase; dienelactone hydrolase; carboxymethylene butenolide hydrolase. Enzyme Commission Number: EC 3.1.1.45. CAS No. 76689-22-0. 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-3472; carboxymethylenebutenolidase; EC 3.1.1.45; 76689-22-0; maleylacetate enol-lactonase; dienelactone hydrolase; carboxymethylene butenolide hydrolase. Cat No: EXWM-3472. | |
| carboxymethylhydantoinase | This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. Group: Enzymes. Synonyms: hydantoin hydrolase. Enzyme Commission Number: EC 3.5.2.4. CAS No. 9025-14-3. 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-4506; carboxymethylhydantoinase; EC 3.5.2.4; 9025-14-3; hydantoin hydrolase. Cat No: EXWM-4506. | |
| carboxymethyloxysuccinate lyase | This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that cleave carbon-oxygen bonds. Group: Enzymes. Synonyms: carbon-oxygen lyase; carboxymethyloxysuccinate glycolate-lyase. Enzyme Commission Number: EC 4.2.99.12. CAS No. 53167-89-8. 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-5264; carboxymethyloxysuccinate lyase; EC 4.2.99.12; 53167-89-8; carbon-oxygen lyase; carboxymethyloxysuccinate glycolate-lyase. Cat No: EXWM-5264. | |
| carboxymethylproline synthase | The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. Group: Enzymes. Synonyms: CarB (ambiguous). Enzyme Commission Number: EC 2.3.1.226. 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-2173; carboxymethylproline synthase; EC 2.3.1.226; CarB (ambiguous). Cat No: EXWM-2173. | |
| carboxynorspermidine decarboxylase | A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro. Group: Enzymes. Synonyms: carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name). Enzyme Commission Number: EC 4.1.1.96. 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-4846; carboxynorspermidine decarboxylase; EC 4.1.1.96; carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name). Cat No: EXWM-4846. | |
| carboxynorspermidine synthase | The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine / carboxyspermidine, respectively. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro. Group: Enzymes. Synonyms: carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name). Enzyme Commission Number: EC 1.5.1.43. 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-1524; carboxynorspermidine synthase; EC 1.5.1.43; carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name). Cat No: EXWM-1524. | |
| 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 A2 | Isolated from rat pancreas but not present in cattle pancreas. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: CPA2. Enzyme Commission Number: EC 3.4.17.15. CAS No. 181186-98-1. 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-4067; carboxypeptidase A2; EC 3.4.17.15; 181186-98-1; CPA2. Cat No: EXWM-4067. | |
| 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 B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb). mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C. | |
| Carboxypeptidase-B from rat, Recombinant | Carboxypeptidase B, recombinant, is intended to use in highly regulated production processes at pharmaceutical companies. Carboxypeptidase B is a widely used metalloprotease, typically isolated from pancreas of different animals, that specifically releases arginine and lysine from the C-terminus of peptides and proteins. Roche has chemically synthesized a gene encoding for the amino acid sequence of the rat Carboxypeptidase B and has transformed the gene into the expression host Pichia pastoris, which expresses the recombinant Carboxypeptidase B as active protease with identical properties compared to the native Carboxypeptidase B. The product is manufactured according to.terial for the production of active pharmaceutical ingredients (api), i.e., insulin. Group: Enzymes. Synonyms: protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine] hydrolase. Purity: >85%. CPB1. Activity: >210 U/mg. Stability: At -15 to -25°C within specification range for 24 months. Appearance: Clear, colorless to slightly yellowish solution. Storage: Tris/HCl, 33 mmol/l; ZnCl2, 0.1 mmol/l; pH 7.5-8.5 at +25°C. Source: Pichia pastoris. Species: Rat pancreas. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat N. | |
| Carboxypeptidase-B rat, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit.sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| carboxypeptidase C | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in). Widely distributed in eukaryotes. Type example of peptidase family S10. Group: Enzymes. Synonyms: carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin. Enzyme Commission Number: EC 3.4.16.5. CAS No. 9046-67-7. Carboxypeptidase Y. 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-4059; carboxypeptidase C; EC 3.4.16.5; 9046-67-7; carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin. Cat No: EXWM-4059. | |
| carboxypeptidase D | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in). In peptidase family S10 (carboxypeptidase C family). Group: Enzymes. Synonyms: cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Enzyme Commission Number: EC 3.4.16.6. CAS No. 153967-26-1. CPDW-II. 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-4060; carboxypeptidase D; EC 3.4.16.6; 153967-26-1; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: EXWM-4060. | |
| 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 M | A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: CPM. Enzyme Commission Number: EC 3.4.17.12. CAS No. 120038-28-0. 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-4064; carboxypeptidase M; EC 3.4.17.12; 120038-28-0; CPM. Cat No: EXWM-4064. | |
| carboxypeptidase T | Known from Thermoactinomyces vulgaris. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: CPT. Enzyme Commission Number: EC 3.4.17.18. CAS No. 89623-65-4. 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-4070; carboxypeptidase T; EC 3.4.17.18; 89623-65-4; CPT. Cat No: EXWM-4070. | |
| carboxypeptidase Taq | A 56-kDa enzyme from Thermus aquaticus. Most active at 80° C. Type example of peptidase family M32. Group: Enzymes. Enzyme Commission Number: EC 3.4.17.19. CAS No. 9031-98-5. 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-4071; carboxypeptidase Taq; EC 3.4.17.19; 9031-98-5. Cat No: EXWM-4071. | |
| 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. | |
| carboxyvinyl-carboxyphosphonate phosphorylmutase | Catalyses the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos. Group: Enzymes. Enzyme Commission Number: EC 2.7.8.23. CAS No. 122799-57-9. 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-3323; carboxyvinyl-carboxyphosphonate phosphorylmutase; EC 2.7.8.23; 122799-57-9. Cat No: EXWM-3323. | |
| Cardiolipin | Cardiolipin. Group: Others. Synonyms: 1,3-bis[1,2-dioleoyl-sn-glycero-3-phospho]-2-[4-(dipyrrometheneboron difluoride)butanoyl]-sn-glycerol (ammonium salt). Purity: >99%. Mole weight: 1808.209. Stability: 6 Months. Storage: -20°C. Avanti Polar Lipids; lipid products; bioactive lipids; fluorescent lipids; singnal transduction; cell pathways; 1,3-bis[1,2-dioleoyl-sn-glycero-3-phospho]-2-[4-(dipyrrometheneboron difluoride)butanoyl]-sn-glycerol (ammonium salt); Cardiolipin; 1,1,2,2-tetraoleoyl cardiolipin[4-(dipyrrometheneboron Difluoride)butanoyl] (ammonium salt) Cardiolipin. Cat No: FLBZ-130. | |
| cardiolipin synthase (CMP-forming) | The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin. It requires divalent cations for activity. Group: Enzymes. Enzyme Commission Number: EC 2.7.8.41. 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-3341; cardiolipin synthase (CMP-forming); EC 2.7.8.41. Cat No: EXWM-3341. | |
| caricain | From papaya plant, Carica papaya. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: papaya peptidase A; papaya peptidase II; papaya proteinase papaya proteinase III; papaya proteinase 3; proteinase ω; papaya proteinase A; chymopapain S; Pp. Enzyme Commission Number: EC 3.4.22.30. CAS No. 39307-22-7. 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-4205; caricain; EC 3.4.22.30; 39307-22-7; papaya peptidase A; papaya peptidase II; papaya proteinase papaya proteinase III; papaya proteinase 3; proteinase ω; papaya proteinase A; chymopapain S; Pp. Cat No: EXWM-4205. | |
| carlactone synthase | Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase, but 10-fold slower. Group: Enzymes. Synonyms: CCD8 (gene name); MAX4 (gene name); NCED8 (gene name). Enzyme Commission Number: EC 1.13.11.69. 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-0589; carlactone synthase; EC 1.13.11.69; CCD8 (gene name); MAX4 (gene name); NCED8 (gene name). Cat No: EXWM-0589. | |
| carminomycin 4-O-methyltransferase | The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin. In vitro the enzyme from Streptomyces sp. C5 also catalyses the 4-O-methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy-13-deoxycarminomycin. Group: Enzymes. Synonyms: DnrK; DauK. Enzyme Commission Number: EC 2.1.1.292. 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-1899; carminomycin 4-O-methyltransferase; EC 2.1.1.292; DnrK; DauK. Cat No: EXWM-1899. | |
| carnitinamidase | Does not act on D-carnitinamide. Group: Enzymes. Synonyms: L-carnitinamidase; carnitine amidase; L-carnitine amidase. Enzyme Commission Number: EC 3.5.1.73. CAS No. 117444-04-9. 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-4464; carnitinamidase; EC 3.5.1.73; 117444-04-9; L-carnitinamidase; carnitine amidase; L-carnitine amidase. Cat No: EXWM-4464. | |
| carnitine 3-dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.108. CAS No. 9045-45-8. 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-0011; carnitine 3-dehydrogenase; EC 1.1.1.108; 9045-45-8. Cat No: EXWM-0011. | |
| carnitine decarboxylase | Requires ATP. Group: Enzymes. Synonyms: carnitine carboxy-lyase. Enzyme Commission Number: EC 4.1.1.42. CAS No. 37237-38-0. 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-4787; carnitine decarboxylase; EC 4.1.1.42; 37237-38-0; carnitine carboxy-lyase. Cat No: EXWM-4787. | |
| carnitine O-acetyltransferase | Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase). Group: Enzymes. Synonyms: acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC. Enzyme Commission Number: EC 2.3.1.7. CAS No. 9029-90-7. CRAT. 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-2250; carnitine O-acetyltransferase; EC 2.3.1.7; 9029-90-7; acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC. Cat No: EXWM-2250. | |
| carnitine O-octanoyltransferase | Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase). Group: Enzymes. Synonyms: medium-chain/long-chain carnitine acyltransferase; carnitine medium-chain acyltransferase; easily solubilized mitochondrial carnitine palmitoyltransferase; overt mitochondrial carnitine palmitoyltransferase. Enzyme Commission Number: EC 2.3.1.137. CAS No. 39369-19-2. 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-2075; carnitine O-octanoyltransferase; EC 2.3.1.137; 39369-19-2; medium-chain/long-chain carnitine acyltransferase; carnitine medium-chain acyltransferase; easily solubilized mitochondrial carnitine palmitoyltransferase; overt mitochondrial carnitine palmitoyltransferase. Cat No: EXWM-2075. | |
| carnitine O-palmitoyltransferase | Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase. Group: Enzymes. Synonyms: CPT; CPTo; outer malonyl-CoA inhibitable carnitine palmitoyltransferase; CPTi; CPT I (outer membrane carnitine palmitoyl transferase); carnitine palmitoyltransferase I; carnitine palmitoyltransferase II; CPT-A; CPT-B; acylcarnitine transferase; carnitine palmitoyltransferase; carnitine palmitoyltransferase-A; L-carnitine palmitoyltransferase; palmitoylcarnitine transferase. Enzyme Commission Number: EC 2.3.1.21. CAS No. 9068-41-1. 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-2155; carnitine O-palmitoyltransferase; EC 2.3.1.21; 9068-41-1; CPT; CPTo; outer malonyl-CoA inhibitable carnitine palmitoyltransferase; CPTi; CPT I (outer membrane carnitine palmitoyl transferase); carnitine palmitoyltransferase I; carnitine palmitoyltransferase II; CPT-A; CPT-B; acylcarnitine transferase; carnitine palmitoyltransferase; carnitine palmitoyltransferase-A; L-carnitine palmitoyltransferase; palmitoylcarnitine transferase. Cat No: EXWM-2155. | |
| carnosine N-methyltransferase | This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:carnosine N-methyltransferase. This enzyme participates in histidine metabolism. Group: Enzymes. Enzyme Commission Number: EC 2.1.1.22. CAS No. 37256-93-2. 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-1822; carnosine N-methyltransferase; EC 2.1.1.22; 37256-93-2. Cat No: EXWM-1822. | |
| carnosine synthase | This enzyme was thought to form AMP, but studies with highly purified enzyme proved that it forms ADP. Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates. It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity. Group: Enzymes. Synonyms: carnosine synthetase; carnosine-anserine synthetase; homocarnosine-carnosine synthetase; carnosine-homocarnosine synthetase;L-histidine:β-alanine ligase (AMP-forming) (incorrect). Enzyme Commission Number: EC 6.3.2.11. CAS No. 9023-61-4. 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-5732; carnosine synthase; EC 6.3.2.11; 9023-61-4; carnosine synthetase; carnosine-anserine synthetase; homocarnosine-carnosine synthetase; carnosine-homocarnosine synthetase;L-histidine:β-alanine ligase (AMP-forming) (incorrect). Cat No: EXWM-5732. | |
| carotene ε-monooxygenase | A heme-thiolate protein (P-450). Also acts on zeinoxanthin to give lutein. Group: Enzymes. Synonyms: CYP97C1; LUT1. Enzyme Commission Number: EC 1.14.99.45. 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-1055; carotene ε-monooxygenase; EC 1.14.99.45; CYP97C1; LUT1. Cat No: EXWM-1055. | |
| carotenoid 1,2-hydratase | In Rubrivivax gelatinosus and Thiocapsa roseopersicina both products are formed, whereas Rhodobacter capsulatus only gives 1-hydroxy-1,2-dihydrolycopene. Also acts on neurosporene giving 1-hydroxy-1,2-dihydroneurosporene with both organism but 1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene only with Rubrivivax gelatinosus. Group: Enzymes. Synonyms: CrtC. Enzyme Commission Number: EC 4.2.1.131. 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-4972; carotenoid 1,2-hydratase; EC 4.2.1.131; CrtC. Cat No: EXWM-4972. | |
| carotenoid-9',10'-cleaving dioxygenase | Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene. Group: Enzymes. Synonyms: BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving). Enzyme Commission Number: EC 1.13.11.71. 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-0591; carotenoid-9',10'-cleaving dioxygenase; EC 1.13.11.71; BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving). Cat No: EXWM-0591. | |
| carotenoid isomerooxygenase | The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule. Group: Enzymes. Synonyms: ninaB (gene name). Enzyme Commission Number: EC 1.13.11.65. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0585; carotenoid isomerooxygenase; EC 1.13.11.65; ninaB (gene name). Cat No: EXWM-0585. | |
| Carrot Powder | Yesherb carrot powder is made from fresh carrot, using the advanced spray drying technology processing. Carrot powder maintain the maximum flavor of carrot itself, the extract contains a variety of vitamins and acids. Carrot powder have good taste, easy to dissolve, easy to save. Group: Others. Carrot Powder; Daucus Carota Subsp. Sativus. Cat No: EXTC-109. | |
| carveol dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-carveol:NADP+ oxidoreductase. This enzyme is also called (-)-trans-carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. Group: Enzymes. Synonyms: (-)-trans-carveol dehydrogenase. Enzyme Commission Number: EC 1.1.1.243. CAS No. 122653-66-1. 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-0150; carveol dehydrogenase; EC 1.1.1.243; 122653-66-1; (-)-trans-carveol dehydrogenase. Cat No: EXWM-0150. | |
| carvone reductase | This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin. Group: Enzymes. Enzyme Commission Number: EC 1.3.99.25. 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-1427; carvone reductase; EC 1.3.99.25. Cat No: EXWM-1427. | |
| (+)-caryolan-1-ol synthase | A multifunctional enzyme which also forms (+)-β-caryophyllene from farnesyl diphosphate [EC 4.2.3.89, (+)-β-caryophyllene synthase]. Group: Enzymes. Synonyms: GcoA. Enzyme Commission Number: EC 4.2.1.138. 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-4979; (+)-caryolan-1-ol synthase; EC 4.2.1.138; GcoA. Cat No: EXWM-4979. | |
| Cas9-C-NLS Nuclease | Cas9-C-NLS Nuclease. Cas9-c-nls nuclease is the recombinant streptococcus pyogenes cas9 (wt) protein with a c-terminal nucleic localization signal (nls). it can be used for genome editing by inducing site-specific dna double stranded breaks. cas9 protein forms a very stable ribonucleoprotein (rnp) complex with the guide rna (grna) component of the crispr/cas9 system, which can localize to the nucleus immediately once entering the cell with the guide of the nls. compared with the mrna or plasmid systems, transcription and translation processes are not required. this dna-free system avoids the risk of inserting foreign dna into the genome, which can be quite useful for gene editing-based disease therapy. our highly pure and active cas9 nuclease meets all of the researchers requirements (e.g. in vitro cleavage assay, rnp complex transfection, micro injection). Group: Cloning Enzymes. Purity: 50μg; 100μg. Storage: Store at -20 ?. Source: E.coli. Pack: 10 mM Tris, 300 mM NaCl, 0.1 mM EDTA, 1 mM DTT, 50% Glycerol PH 7.4 at 25°C. Cat No: CE-3502. | |
| Cas9-N-NLS Nuclease | Cas9-N-NLS Nuclease. Cas9-n-nls nuclease is the recombinant streptococcus pyogenes cas9 (wt) protein with a n-terminal nucleic localization signal (nls) that can be used for genome editing by inducing site-specific dna double stranded breaks. cas9 protein forms a very stable ribonucleoprotein (rnp) complex with the guide rna (grna) component of the crispr/cas9 system, which can localize to the nucleus immediately once entering the cell with the guide of the nls. compared with the mrna or plasmid systems, transcription and translation processes are not required. this dna-free system avoids the risk of inserting foreign dna into the genome, which can be quite useful for gene editing-based disease therapy. our highly pure and active cas9 nuclease meets all of the researcher´s requirements (e.g. in vitro cleavage assay, rnp complex transfection, micro injection). Group: Cloning Enzymes. Purity: 50μg; 100μg. Storage: Store all components at -20 ?. Source: E.coli. Cat No: CE-3503. | |
| Cas9 Nuclease | Cas9 Nuclease. Recombinant streptococcus pyogenes cas9 (wt) nuclease is purified from e. coli.it can be used for genome editing by inducing site-specific double stranded breaks in double stranded dna. cas9 protein forms a very stable ribonucleoprotein (rnp) complex with the guide rna (grna) component of the crispr/cas9 system. the rnp complex recognizes the target site by matching grna with the genomic dna sequence and leads to dna breaks within 3 bases from the ngg pam (protospacer adjacent motif). with gencrispr cas9 nuclease, customers can screen highly efficient grna using in vitro dna cleavage assays. it could be a powerful tool for gene editing. Group: Cloning Enzymes. Purity: 10μg; 50μg. Storage: Store at -20 ?. Source: E.coli. Cat No: CE-3501. | |
| casbene synthase | The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene. Group: Enzymes. Synonyms: casbene synthetase; geranylgeranyl-diphosphate diphosphate-lyase (cyclizing). Enzyme Commission Number: EC 4.2.3.8. CAS No. 69106-45-2. 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-5242; casbene synthase; EC 4.2.3.8; 69106-45-2; casbene synthetase; geranylgeranyl-diphosphate diphosphate-lyase (cyclizing). Cat No: EXWM-5242. | |
| Casein Kinase Iδ rat, Recombinant | The Casein kinase 1 family of protein kinases are serine/threonine-selective enzymes that function as regulators of signal transduction pathways in most eukaryotic cell types. CK1 isoforms are involved in Wnt signaling, circadian rhythms, nucleo-cytoplasmic shuttling of transcription factors, DNA repair, and DNA transcription. C-terminal truncated, n-terminal his-tag/s-tag, > 90% (sds-page), recombinant, expressed in e. coli, solution. Group: Enzymes. Synonyms: Casein Kinase Iδ; Casein Kinase I; CK-Iδ; CK-I; Non-specific serine/threonine protein kinase; Protein phosphokinase; Protein serine kinase; Protein serine-threonine kinase; Protein-serine kinase; Serine kinase; Serine protein kinase; Serine (threonine) protein kinase; Serine-specific protein kinase; Serine/t. Purity: > 90% (SDS-PAGE). CK-I&delta. Mole weight: mol wt 41.8 kDa. Activity: 1,000-3,000 units/mg protein. Stability: -20°C. Form: solution. Source: E. coli. Species: Rat. Casein Kinase Iδ; Casein Kinase I; CK-Iδ; CK-I; Non-specific serine/threonine protein kinase; Protein phosphokinase; Protein serine kinase; Protein serine-threonine kinase; Protein-serine kinase; Serine kinase; Serine protein kinase; Serine (threonine) protein kinase; Serine-specific protein kinase; Serine/threonine protein kinase; Threonine-specific protein kinase. Cat No: NATE-0140. | |
| Casein Kinase II from Human, Recombinant | The Casein kinase 2 (EC 2.7.11.1) is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes. Casein kinase ii (ck2) is a constitutively active serine/threonine protein kinase composed of two 44 kda catalytic α-subunits and two 26 kda regulatory β-subunits in an α2β2 configuration to form stable heterotetramers. ck2 holoenzyme undergoes autophosphorylation at two serine residues (s2/s3) of its β-subunit. recen. ck2 is able to phosphorylate, under special circumstances, tyrosyl residues in proteins. ck2 is implicated in a variety of cellular functions. Group: Enzymes. Synonyms: EC 2.7.11.1; Casein Kinase II; CK2; CK II; Casein Kinase 2. CAS No. 9026-43-1. CK. Mole weight: a-subunit (45 kDa), b-subunit (25 kDa). The apparent molecular weight of the a-subunit estimated by SDS-PAGE is about 42 kDa. Activity: 859,000 units/mg. Storage: at -80°C. Avoid repeated freeze/thaw cycles. Form: 350 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), 1 mM Na2EDTA, 2 mM DTT and 0.1% Triton X-100. Source: E. coli. Species: Human. EC 2.7.11.1; Casein Kinase II; CK2; CK II; Casein Kinase 2. Cat No: NATE-1271. | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi.proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. 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-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| caspase-10 | Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62). Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-κB survival signalling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation). Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp?.u-Thr-Asp? to yield a p13 fragment that is not N-myristoylated. Belongs in peptidase family C14. Group: Enzymes. Synonyms: FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Enzyme Commission Number: EC 3.4.22.63. CAS No. 189088-85-5. 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-4239; caspase-10; EC 3.4.22.63; 189088-85-5; FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Cat No: EXWM-4239. | |
| caspase-11 | This murine enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Like caspase-5, but unlike caspase-4, this enzyme can be induced by lipopolysaccharide. This enzyme not only activates caspase-1, which is required for the maturation of proinflammatory cytokines such as interleukin-1β (IL-1β) and IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads to cellular apoptosis under pathological conditions. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-11. Enzyme Commission Number: EC 3.4.22.64. 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-4240; caspase-11; EC 3.4.22.64; CASP-11. Cat No: EXWM-4240. | |
| Caspase-1 from Human, Recombinant | Caspase 1/Interleukin-1 converting enzyme is an enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory cytokines interleukin 1β and interleukin 18, into active mature peptides. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington's disease. Alternative splicing of the gene results in five transcript variants encoding distinct isoforms. Recent studies implicated caspase 1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS. Recombinant, human caspase-1 fused at the n-terminus to a hisotag sequence and expressed in e. coli useful for the study of enzyme regulation, cleavage of target substrates, and inhibitor screening. Group: Enzymes. Synonyms: CASP1; ICE; IL1BC; P45; Caspase 1; Interleukin-1; IL-1β Converting Enzyme. Purity: >90% by SDS-PAGE. Caspase-1. Mole weight: 10 kDa and 20 kDa. Activity: >25,000 units/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: E. coli. Species: Human. CASP1; ICE; IL1BC; P45; Caspase 1; Interleukin-1; IL-1β Converting Enzyme. Cat No: NATE-0813. | |
| caspase-2 | Caspase-2 is an initiator caspase, as are caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Two forms of caspase-2 with antagonistic effects exist: caspase-2L induces programmed cell death and caspase-2S suppresses cell death. Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease. Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments. Proteolysis occurs at Asp residues and the.s a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Enzyme Commission Number: EC 3.4.22.55. CAS No. 182372-14-1. 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-4230; caspase-2; EC 3.4.22.55; 182372-14-1; ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Cat No: EXWM-4230. | |
| caspase-3 | Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. Caspase-3 can activate procaspase-2 (EC 3.4.22.55). Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. Although Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp? is a better substrate than Asp-Val-Ala-Asp?. This is not the case for caspase-7. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CPP32; apopain; yama protein. Enzyme Commission Number: EC 3.4.22.56. CAS No. 169592-56-7. 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-4231; caspase-3; EC 3.4.22.56; 169592-56-7; CPP32; apopain; yama protein. Cat No: EXWM-4231. | |
| Caspase 3 Human, Recombinant | Caspase 3 is a member of the CED-3 subfamily of caspases and is responsible for the cleavage of many key proteins such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP), the inhibitor of caspase-activated deoxyribonuclease (ICAD), and gelsolin, a protein involved in apoptosis regulation. Caspase 3 is considered to be an effector caspase, activating pro-caspase 6 and pro-caspase 9 in vitro. Caspase 3 can be activated by caspase 8, caspase 6, and granzyme B. Human recombinant c-terminal histidine tagged caspase 3 is a fully active protein consisting of 17 kda and 13.5 kda subunits; the 13.5 kda subunit contains the histidine tag. Applications: Caspase-3 is a caspase prote.ve enzyme. this protein cleaves and activates caspases 6 and 7; and the protein itself is processed and activated by caspases 8, 9, and 10. it is the predominant caspase involved in the cleavage of amyloid-beta 4a precursor protein, which is associated with neuronal death in alzheimer's disease. alternative splicing of this gene results in two transcript variants that encode the same protein. caspase-3 shares many of the typical characteristics common to all currently-known caspases. for example, its active site contains a cysteine residue (cys-163) and histidine residue (his-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an. | |
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