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 | |
|---|---|---|
| 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 | |
| caspase-4 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) 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. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Enzyme Commission Number: EC 3.4.22.57. CAS No. 182762-08-9. 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-4232; caspase-4; EC 3.4.22.57; 182762-08-9; ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Cat No: EXWM-4232. | |
| caspase-5 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) 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. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Enzyme Commission Number: EC 3.4.22.58. CAS No. 192465-11-5. 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-4233; caspase-5; EC 3.4.22.58; 192465-11-5; ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Cat No: EXWM-4233. | |
| caspase-6 | Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) 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. Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to the release of cytochrome c from the mitochondria. The release of cytochrome c is an essential component of the intrinsic apoptosis pathway. The enzyme can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragmentation in the final phases of apoptosis. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-6; apoptotic protease Mch-2; Mch2. Enzyme Commission Number: EC 3.4.22.59. CAS No. 182372-15-2. 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-4234; caspase-6; EC 3.4.22.59; 182372-15-2; CASP-6; apoptotic protease Mch-2; Mch2. Cat No: EXWM-4234. | |
| Caspase-6 (Active) from Human, Recombinant | Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. Group: Enzymes. Synonyms: CASP6; MCH2; Caspase-6 (Active); Caspase-6. Caspase 6. Appearance: Liquid. Storage: -80°C. Form: Liquid. 5μg in 25μl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole. Source: E. coli. Species: Human. CASP6; MCH2; Caspase-6 (Active); Caspase-6. Cat No: NATE-0814. | |
| caspase-7 | Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). 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. Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. Caspase-7 is activated by the initiator caspases [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Enzyme Commission Number: EC 3.4.22.60. CAS No. 189258-14-8. 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-4236; caspase-7; EC 3.4.22.60; 189258-14-8; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Cat No: EXWM-4236. | |
| Caspase-7 from Human, Recombinant | Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. Applications: Used to screen caspase inhibitors, study enzyme regulation, determine caspase substrate specificity, or as positive control in caspase activity assays. Group: Enzymes. Synonyms: CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Enzyme Commission Number: EC 3.4.22.-. Purity: 90% (SDS-PAGE). Caspase 7. Activity: ~25,000U/mg protein. Appearance: Lyophilized. Storage: -80°C. Source: E. coli. Species: Human. CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Cat No: NATE-0815. | |
| caspase-8 | Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Caspase-8 is the apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. It contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. This enzyme is linked to cell surface death receptors such as Fas. When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. The enzyme has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala, at the P1' position. It has very broad P...ORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Enzyme Commission Number: EC 3.4.22.61. CAS No. 179241-78-2. 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-4237; caspase-8; EC 3.4.22.61; 179241-78-2; FLICE, FADD-like ICE; MACH; MORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Cat No: EXWM-4237. | |
| caspase-9 | Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63). Caspase-9 contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. Procaspase-3 is the enzyme's physiological substrate. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Enzyme Commission Number: EC 3.4.22.62. CAS No. 180189-96-2. 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-4238; caspase-9; EC 3.4.22.62; 180189-96-2; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Cat No: EXWM-4238. | |
| Caspase-9 (Active) from Human, Recombinant | The expressed caspase-9 spontaneously undergoes autoprocessing to yield the subunits characteristic of the native enzyme. Active enzyme purified from E. coliThis product is useful in screening caspase inhibitors for pharmaceutical Applications. Group: Enzymes. Synonyms: CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Purity: 90% (SDS-PAGE). Caspase 9. Activity: ~400 units/mg. Appearance: Lyophilized Powder. Storage: -80°C. Source: E. coli. Species: Human. CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Cat No: NATE-0816. | |
| Cassia Nomame Extract (Ratio) | Cassia Nomame Extract (Ratio). Group: Others. Purity: 4:1~20:1. Cassia Nomame Extract (Ratio). Cat No: EXTW-028. | |
| catalase | A hemoprotein. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase. Group: Enzymes. Synonyms: equilase; caperase; optidase; catalase-peroxidase; CAT. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. 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-0508; catalase; EC 1.11.1.6; 9001-05-2; equilase; caperase; optidase; catalase-peroxidase; CAT. Cat No: EXWM-0508. | |
| Catalase (Crude Enzyme) | Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert approximately 5 million molecules of hydrogen peroxide to water and oxygen each minute. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; analysis; biotechnology; industry. Group: Enzymes. Synonyms: hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Pack: 100ml. Cat No: NATE-1795. | |
| Catalase for bio-washing | Catalase is a kind of liquid enzyme preparation fermented by Aspergillus Niger; it can effectively catalyze hydrogen peroxide and decompose hydrogen peroxide into oxygen and water. And catalase only reacts with hydrogen peroxide. Applications: Textile. Group: Enzymes. CAS No. 9001-5-2. CAT. Appearance: liquid. Source: Aspergillus Niger. Catalase; Textile enzyme; Catalase for bio-washing;Catalase for bio-washing; TEXT-1928. Pack: 25kg/barrel or subject to client requirement. Cat No: TEXT-1928. | |
| Catalase from Psychrotolerant Bacteria, recombinant | Catalase is an enzyme that catalyzes the transformation of hydrogen peroxide into water and oxygen. This enzyme functions as a natural antioxidant protecting the cell against oxidative damage. This enzyme finds applications in Research and Clinical Chemistry. It also finds diverse industrial applications in textiles, waste treatment, cosmetics and as a disinfectant agent. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Mole weight: ~220 kDa. Activity: > 65000 U/mL (Specific activity: > 7500 U/mg). Storage: At -20°C, it keeps activity for at least 18 months. Form: Liquid. Source: E. coli. Species: Psychrotolerant Bacteria. EC 1.11.1.6; Catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Cat No: NATE-1699. | |
| Catalase from Psychrotolerant Bacteria, recombinant (Lyophilized Powder) | Catalase is an enzyme that catalyzes the transformation of hydrogen peroxide into water and oxygen. This enzyme functions as a natural antioxidant protecting the cell against oxidative damage. This enzyme finds applications in Research and Clinical Chemistry. It also finds diverse industrial applications in textiles, waste treatment, cosmetics and as a disinfectant agent. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Mole weight: ~220 kDa. Activity: > 8000 U/mg protein. Storage: At -20°C, it keeps 100% of its activity for more than two years. Form: Lyophilized Powder. Source: E. coli. Species: Psychrotolerant Bacteria. EC 1.11.1.6; Catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Cat No: NATE-1700. | |
| catalase-peroxidase | Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid. Group: Enzymes. Synonyms: katG (gene name). Enzyme Commission Number: EC 1.11.1.21. 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-0503; catalase-peroxidase; EC 1.11.1.21; katG (gene name). Cat No: EXWM-0503. | |
| catechol 1,2-dioxygenase | Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida. Group: Enzymes. Synonyms: catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II. Enzyme Commission Number: EC 1.13.11.1. CAS No. 9027-16-1. 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-0529; catechol 1,2-dioxygenase; EC 1.13.11.1; 9027-16-1; catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II. Cat No: EXWM-0529. | |
| catechol 2,3-dioxygenase | Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation. Group: Enzymes. Synonyms: 2,3-pyrocatechase; catechol 2,3-oxygenase; catechol oxygenase; metapyrocatechase; pyrocatechol 2,3-dioxygenase; xylE (gene name); catechol:oxygen 2,3-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.2. CAS No. 9029-46-3. 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-0539; catechol 2,3-dioxygenase; EC 1.13.11.2; 9029-46-3; 2,3-pyrocatechase; catechol 2,3-oxygenase; catechol oxygenase; metapyrocatechase; pyrocatechol 2,3-dioxygenase; xylE (gene name); catechol:oxygen 2,3-oxidoreductase (decyclizing). Cat No: EXWM-0539. | |
| catechol O-methyltransferase | The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols. Group: Enzymes. Synonyms: COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. 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-1961; catechol O-methyltransferase; EC 2.1.1.6; 9012-25-3; COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Cat No: EXWM-1961. | |
| catechol oxidase | A type 3 copper protein that catalyses exclusively the oxidation of catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols.It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols. Group: Enzymes. Synonyms: diphenol oxidase; o-diphenolase; polyphenol oxidase; pyrocatechol oxidase; dopa oxidase; catecholase; o-diphenol:oxygen oxidoreductase; o-diphenol oxidoreductase. Enzyme Commission Number: EC 1.10.3.1. CAS No. 9002-10-2. 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-0475; catechol oxidase; EC 1.10.3.1; 9002-10-2; diphenol oxidase; o-diphenolase; polyphenol oxidase; pyrocatechol oxidase; dopa oxidase; catecholase; o-diphenol:oxygen oxidoreductase; o-diphenol oxidoreductase. Cat No: EXWM-0475. | |
| catechol oxidase (dimerizing) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is catechol:oxygen oxidoreductase (dimerizing). Group: Enzymes. Enzyme Commission Number: EC 1.1.3.14. CAS No. 37250-83-2. 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-0396; catechol oxidase (dimerizing); EC 1.1.3.14; 37250-83-2. Cat No: EXWM-0396. | |
| cathepsin B | An intracellular (lysosomal) enzyme in peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin B1 (obsolete); cathepsin II. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Cathepsin B. 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-4192; cathepsin B; EC 3.4.22.1; 9047-22-7; cathepsin B1 (obsolete); cathepsin II. Cat No: EXWM-4192. | |
| Cathepsin B from Human, recombinant | Cathepsin B is a lysosomal cysteine protease. It is implicated in playing a role in protein degradation, arthritis, apoptosis, and cancer. Group: Enzymes. Synonyms: CTSB; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Purity: > 90% by SDS-PAGE. Cathepsin B. Mole weight: 27.8 kDa (80-333 aa). Activity: >7500 mU/mg. Storage: Stable for at least 1 year as supplied. Dilute in de-ionized water to 0.1 mg/ml and store at -80°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II; EC 3.4.22.1. Cat No: NATE-1706. | |
| cathepsin D | Occurs intracellularly, in lysosomes. A zymogen form is known. In peptidase family A1 (pepsin A family). Group: Enzymes. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. 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-4287; cathepsin D; EC 3.4.23.5; 9025-26-7. Cat No: EXWM-4287. | |
| Cathepsin D from Human, recombinant | Cathepsin D is a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is an estrogen-regulated protein associated with tissue breakdown. Levels of cathepsin D have been positively correlated with recurring breast cancers of both node negative and node positive types. Additionally cathepsin D has been associated with amyloid formation in Alzheimer's plaques. Cathepsin D is produced initially as a pre-pro-enzyme which gets transported to lysosomes via endosomes in most cell types. In endosomes, it gets proteolyzed by unidentified proteases by removal of the pro-peptide to generate...e cathepsins B and L generates mature, active double-chain Cathepsin D. Group: Enzymes. Synonyms: CTSD; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. Purity: > 80% by SDS-PAGE. CTSD. Mole weight: 45.1 kDa. Activity: >100 pmol/min/mg. Storage: Store at -20°C. Stable for at least 6 months as supplied. Reconstitute to 1 mg/ml in sterile water, store at -80°C in aliquots and use within 6 months after reconstitution. Avoid repeated freeze-thaw cycles. Form: Freeze-Dried. Source: E. coli. Species: Human. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Cat No: NATE-1707. | |
| cathepsin E | Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Enzyme Commission Number: EC 3.4.23.34. CAS No. 110910-42-4. 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-4271; cathepsin E; EC 3.4.23.34; 110910-42-4; slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Cat No: EXWM-4271. | |
| cathepsin F | Cathepsin F is a lysosomal cysteine endopeptidase of family C1 (papain family), most active at pH 5.9. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Cathepsin F is expressed in most tissues of human, mouse and rat. Human gene locus: 11q13.1-13.3. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.41. CAS No. 65997-74-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4216; cathepsin F; EC 3.4.22.41; 65997-74-2. Cat No: EXWM-4216. | |
| Cathepsin F from Human, Recombinant | Cathepsin F, also known as CTSF, belongs to the cathepsin family. Cathepsins are papain familycysteine proteinases that represent a major component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF isthought to play a role in normal protein catabolism, and because it is highly expressed in some cancer cell lines, itmay be involved in degradative processes occurring during tumor progression. Recombinant human CTSF protein,fused to His-tag at N-terminus, was expressed in E.coli. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.41. Mole weight: This protein is fused with a 6× His tag at N-terminus and has a calculated MW of 26 kDa. Form: Liquid. Source: E. coli. Species: Human. Cat No: NATE-1666. | |
| cathepsin G | From azurophil granules of polymorphonuclear leukocytes. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: chymotrypsin-like proteinase; neutral proteinase. Enzyme Commission Number: EC 3.4.21.20. CAS No. 56645-49-9. CTSG. 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-4120; cathepsin G; EC 3.4.21.20; 56645-49-9; chymotrypsin-like proteinase; neutral proteinase. Cat No: EXWM-4120. | |
| cathepsin H | Present in lysosomes of mammalian cells. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin B3; benzoylarginine-naphthylamide (BANA) hydrolase (obsolete); cathepsin Ba, aleurain; N-benzoylarginine-β-naphthylamide hydrolase. Enzyme Commission Number: EC 3.4.22.16. CAS No. 60748-73-4. 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-4196; cathepsin H; EC 3.4.22.16; 60748-73-4; cathepsin B3; benzoylarginine-naphthylamide (BANA) hydrolase (obsolete); cathepsin Ba, aleurain; N-benzoylarginine-β-naphthylamide hydrolase. Cat No: EXWM-4196. | |
| cathepsin K | Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin O and cathepsin X (both misleading, having been used for other enzymes); cathepsin O2. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. 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-4213; cathepsin K; EC 3.4.22.38; 94716-09-3; cathepsin O and cathepsin X (both misleading, having been used for other enzymes); cathepsin O2. Cat No: EXWM-4213. | |
| Cathepsin K from Human, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 95% by SDS-PAGE. Activity: >900 mU/mg protein. Storage: at -80°C. Avoid freeze/thaw. Form: Liquid. Source: E. coli. Species: Human. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1705. | |
| Cathepsin K from Mouse, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 90% by SDS-PAGE. Mole weight: 23.4 kDa (115-329 aa). Activity: >1000 mU/mg. Storage: Stable for 6 months at -80°C. Use as provided or dilute to 0.1 mg/ml with 50% glycerol. Aliquot and store at -80°C. Avoid repeated freezing and thawing cycles, as this may lead to the loss in its activity over time. Form: Liquid. Source: E. coli. Species: Mouse. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1704. | |
| Cathepsin K from Rat, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 90% by SDS-PAGE. Mole weight: 23.5 kDa (115-329 aa). Activity: >500 mU/mg. Storage: Stable for 6 months at -80°C. Use as provided or dilute to 0.1 mg/ml with 50% glycerol. Aliquot and store at -80°C. Avoid repeated freezing and thawing cycles, as this may lead to the loss in its activity over time. Form: Liquid. Source: E. coli. Species: Rat. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1703. | |
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