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| Product | Description | |
|---|---|---|
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. |  |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f...mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| Creatine Kinase MB Isoenzyme Type-1 from Human, Recombinant | The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creat... in elisa. the ckmbiti is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine Kinase MB Isoenzyme Type-I; Creatine Kinase MB Isoenzyme Type-1; CKMBITI; CKMBI; CKMB; CKMBT1. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 500 IU/mg. Stability: CKMBITI although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine Kinase MB Isoenzyme Type-I; Creatine Kinase MB Isoenzyme Type-1; CKMBITI; CKMBI; CKMB; CKMBT1. Cat No: NATE-0818. | |
| Creatine Kinase MB Isoenzyme Type-2 from Human, Recombinant | CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine. This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI. Ckmbitii human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mb isoenzyme in elisa. the ckmbitii is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 892 IU/mg. Stability: CKMBITII although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Cat No: NATE-0819. | |
| Creatine Kinase MM Isoenzyme Type-1 from Human, Recombinant | Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. Ckmt1 human recombinant without c-terminal lysine on both chains produced in pichia pastoris is a glycosylated 47kda polypeptide chain having an identical amino acid sequence compared to t...proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITI; CKMMT1. Enzyme Commission Number: EC 2.7.3.2. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Mole weight: 47kDa. Activity: 537 IU/mg. Stability: CKMT1 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITI; CKMMT1. Cat No: NATE-0820. | |
| Creatine Kinase MM Isoenzyme Type-3 from Human, Recombinant | Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. Ckmt3 human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mm isoenzyme in elisa.the ckmt3 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine kin. Enzyme Commission Number: EC 2.7.3.2. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 500 IU/mg. Stability: CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. lease prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITIII; CKMMT3. Cat No: NATE-0821. | |
| Esterase Isoenzyme 1 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esteras. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 30.0 U/g. Storage: -20°C. Source: E. coli. Species: Porcine liver. 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; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0229. | |
| Esterase Isoenzyme 2 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 2, is from porcine liver and is recombinant and expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 2; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine estera. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 80 U/g. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 2; 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; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0230. | |
| Esterase Isoenzyme 3 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the biochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.8 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 3; 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; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0231. | |
| Esterase Isoenzyme 5 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 5 is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 5; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine e. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.5 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 5; 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; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0232. | |
| Esterase Isoenzyme 6 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 6 is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 6; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine e. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 1.2 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 6; 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; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0233. | |
| Exoenzyme C3 from Clostridium botulinum, Recombinant | Exoenzyme C3 transferase is an ADP ribosyl transferase that selectively ribosylates RhoA, RhoB and RhoC proteins on asparagine residue 41, rendering them inactive. It has extremely low affinity for other members of the Rho family such as Cdc42 and Rac1 and does therefore not affect these GTPases. Hence, C3 transferase is a very potent and useful reagent to specifically block RhoA/B/C signaling. Applications: Inhibition of rho activity in vivo by microinjection or pinocyctic uptake into cells. inhibition of rho activity in vitro. Group: Enzymes. Synonyms: Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Purity: >80% by SDS-P...2, 200 mM NaCl, 5% sucrose and 1% dextran. In order to maintain high biological activity of the protein, it is recommended that the protein solution be supplemented with DTT to 1 mM, aliquoted into "experiment sized" amounts, snap frozen in liquid nitrogen and stored at -70°C. The protein is stable for 6 months if stored at -70° C. Storage: The protein should not be exposed to repeated freeze-thaw cycles. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year. Form: Lyophilized powder. Source: E. coli. Species: Clostridium botulinum. Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Cat No: NATE-0874. | |
| Glycogen branching enzyme from Bacillus subtilis, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobil...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 77485.4 Da. Activity: 38.04 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; gluc | |
| Glycogen branching enzyme from Bacteroides fragilis, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobi...1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 81104.6 Da. Activity: 50.88 U/mg (pH 7.0; 3.3 mg/mL starch). Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate, containing 0.5 M imidazole and 0.5 M NaCl, pH ~ 6.8. Source: Bacteroides fragilis NCTC 9343. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzym | |
| Glycogen branching enzyme from Escherichia coli, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobili...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 88157.0 Da. Activity: 15.44 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucos | |
| Insulin Degrading Enzyme (HisoTag) from Rat, Recombinant | Insulin Degrading Enzyme (IDE) is a large zinc-binding protease of the M16A metalloprotease subfamily known to cleave multiple short polypeptides that vary considerably in sequence. IDE was first identified by its ability to degrade the B chain of the hormone insulin. This activity was observed over sixty years ago, though the enzyme specifically responsible for B chain cleavage was identified more recently. This discovery revealed considerable amino acid sequence similarity between IDE and the previously characterized bacterial protease pitrilysin, suggesting a common proteolytic mechanism. Recombinant, rat insulin degrading enzyme fused to a hisotag sequence and expressed in s. frugiperda insect cells. a metalloprotease that degrades insulin and a variety of other peptides including amyloid peptides. Group: Enzymes. Synonyms: IDE; Insulin-degrading enzyme; insulysin; insulin protease. Enzyme Commission Number: EC 3.4.24.56. Purity: >90% by SDS-PAGE. IDE. Mole weight: 110 kDa. Activity: >3 U/mg protein. Storage: < -70°C. Form: Liquid. Source: S. frugiperda. Species: Rat. IDE; Insulin-degrading enzyme; insulysin; insulin protease. Cat No: NATE-0849. | |
| 10-epi-γ-eudesmol synthase | The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% β-eudesmol, 16.8% 10-epi-γ-eudesmol, 10% α-eudesmol, and 5.6% aristolene. cf. EC 4.2.3.68 (β-eudesmol synthase) and EC 4.2.3.85 (α-eudesmol synthase). Group: Enzymes. Enzyme Commission Number: EC 4.2.3.84. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5247; 10-epi-γ-eudesmol synthase; EC 4.2.3.84. Cat No: EXWM-5247. | |
| 1,2-Dioleoyl-sn-glycerol | ALN29882 is a glycerolipid located on the plasma membrane. It consists of two fatty acid chains covalently linked to a single glycerol molecule by means of an ester bond. 18:1 DG has been used as a source of diacylglycerol in the diacylglycerol O-acyltransferase 1 (DGAT1) assay. It is also used as a substrate in the DGAT-1 enzyme assay to evaluate compounds as potential inhibitors of DGAT-1. Suitable for lipoprotein overlay screening assays with the recombinant protein His-AtROP6. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: sn-1,2-Dioleoylglycerol. CAS No. 24529-88-2. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-141572. |  |
| 23S rRNA (adenine1618-N6)-methyltransferase | The recombinant YbiN protein is able to methylate partially deproteinized 50 S ribosomal subunit, but neither the completely assembled 50 S subunits nor completely deproteinized 23 S rRNA. Group: Enzymes. Synonyms: rRNA large subunit methyltransferase F; YbiN protein; rlmF (gene name); m6A1618 methyltransferase. Enzyme Commission Number: EC 2.1.1.181. 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-1780; 23S rRNA (adenine1618-N6)-methyltransferase; EC 2.1.1.181; rRNA large subunit methyltransferase F; YbiN protein; rlmF (gene name); m6A1618 methyltransferase. Cat No: EXWM-1780. | |
| 23S rRNA (adenine2030-N6)-methyltransferase | The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits. Group: Enzymes. Synonyms: YhiR protein; rlmJ (gene name); m6A2030 methyltransferase. Enzyme Commission Number: EC 2.1.1.266. 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-1871; 23S rRNA (adenine2030-N6)-methyltransferase; EC 2.1.1.266; YhiR protein; rlmJ (gene name); m6A2030 methyltransferase. Cat No: EXWM-1871. | |
| (4S)-limonene synthase | A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor. Group: Enzymes. Synonyms: (-)-(4S)-limonene synthase; 4S-(-)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming); geranyldiphosphate diphosphate lyase [cyclizing, (4S)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing; (-)-(4S)-limonene-forming]. Enzyme Commission Number: EC 4.2.3.16. CAS No. 110639-20-8. 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-5172; (4S)-limonene synthase; EC 4.2.3.16; 110639-20-8; (-)-(4S)-limonene synthase; 4S-(-)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming); geranyldiphosphate diphosphate lyase [cyclizing, (4S)-limonene-forming]; geranyl-diphosphate diphosphate-lyase [cyclizing; (-)-(4S)-limonene-forming]. Cat No: EXWM-5172. | |
| 5-Bromo-4-chloro-3-indolyl-α-D-N-acetylneuraminic Acid, Methyl Ester | Used as a substrate for the detection of sialidase-like enzyme in screening of enzymes, studying physiological activities of gangliosides, and recombinant technologies. Synonyms: N-Acetyl-2-O-(5-bromo-4-chloro-1H-indol-3-yl)-α-neuraminic acid methyl ester; D-glycero-α-D-galacto-2-Nonulopyranosidonic acid, 5-bromo-4-chloro-1H-indol-3-yl 5-(acetylamino)-3,5-dideoxy-, methyl ester; α-Neuraminic acid, N-acetyl-2-O-(5-bromo-4-chloro-1H-indol-3-yl)-, methyl ester; Methyl N-acetyl-2-O-(5-bromo-4-chloro-1H-indol-3-yl)-α-neuraminate. Grade: 95%. CAS No. 1447125-47-4. Molecular formula: C20H24BrClN2O9. Mole weight: 551.77. |  |
| 7-epi-α-selinene synthase | The recombinant enzyme from Vitis vinifera forms 49.5% (+)-valencene (cf. EC 4.2.3.73, valencene synthase) and 35.5% (-)-7-epi-α-selinene. Initial cyclization gives (+)-germacrene A in an enzyme bound form which is not released to the medium. Group: Enzymes. Enzyme Commission Number: EC 4.2.3.86. 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-5249; 7-epi-α-selinene synthase; EC 4.2.3.86. Cat No: EXWM-5249. | |
| abieta-7,13-dien-18-ol hydroxylase | A heme-thiolate protein (P-450). This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine), and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine). The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene. Group: Enzymes. Synonyms: CYP720B1; PtAO; abietadienol hydroxylase (ambiguous). Enzyme Commission Number: EC 1.14.13.109. 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-0708; abieta-7,13-dien-18-ol hydroxylase; EC 1.14.13.109; CYP720B1; PtAO; abietadienol hydroxylase (ambiguous). Cat No: EXWM-0708. | |
| Acyl-CoA synthetase from Microorganism | Acetylcoenzyme A synthetase (ACS, EC 6.2.1.3)catalyzes the formation of acetyl coenzyme A with free fatty acids and coenzyme A. The ACS provided by our company is gene recombinant protein. It is of high purity and good activity. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetas. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. Mole weight: 63 kDa (SDS-PAGE). Activity: >20U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: NATE-1712. | |
| Acyl-CoA synthetase, recombinant | Acetylcoenzyme A synthetase (ACS, EC 6.2.1.3)catalyzes the formation of acetyl coenzyme A with free fatty acids and coenzyme A. The ACS provided by our company is gene recombinant protein. It is of high purity and good activity. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; . Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. Purity: 90% (SDS-PAGE test). ACS3. Mole weight: About 70kDa (SDS-PAGE detection). Activity: 30U/mg protein. Storage: 4°C,store at -20°C for long-term preservation. Form: White powder, lyophilized. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: NATE-1682. | |
| Alanine Aminotransferase from Human, Recombinant | Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine aminotransferase human recombinant produced in e. coli is a homodimer, nonglycosylated, polypeptide chain containing 495a.a...inotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. CAS No. 9000-86-6. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. ALT. Mole weight: 54,479 Da. Activity: 1,000 U/mg. Stability: AAT1 although stable at 10°C for 5 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile liquid formulation. Source: E. coli. Species: Human. ALT1; Glutamic-pyruvic transaminase 1; GPT 1; Glutamic-alanine transaminase 1; AAT1; ALT; ALAT; SGPT; Alanine transaminase; alanine aminotransferase; GPT; β-alanine aminotransferase; alanine-α | |
| Alcohol dehydrogenase from E. coli, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0803. | |
| alcohol-forming fatty acyl-CoA reductase | The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons. Group: Enzymes. Synonyms: FAR (gene name); long-chain acyl-CoA:NADPH reductase. Enzyme Commission Number: EC 1.2.1.84. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1187; alcohol-forming fatty acyl-CoA reductase; EC 1.2.1.84; FAR (gene name); long-chain acyl-CoA:NADPH reductase. Cat No: EXWM-1187. | |
| Aldolase A from Human, Recombinant | Fructose bisphosphate aldolase A, also known as Aldolase A is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Deficiency has been associated with myopathy and hemolytic anemia. Recombinant human Aldolase A, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Fructose bisphosphate Aldolase A; ALDOA; ALDA; GSD12. Enzyme Commission Number: EC 4.1.2.13. Purity: > 95% by SDS-PAGE. Aldolase. Mole weight: 41.5 kDa (384 aa, 1-364 aa + His Tag), confirmed by MALDI-TOF. Activity: > 1.5 units/mg. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Fructose bisphosphate Aldolase A; ALDOA; ALDA; GSD12; Aldolase A; Aldolase. Cat No: NATE-1663. | |
| Alkaline Phosphatase from Shrimp, Recombinant | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Shrimp alkaline phosphatase is a heat labile, hydrolase enzyme. It is a high specific activity alkaline phosphatase purified from a recombinant source. There are two preferred sites for enzyme activity: 5' protruding, recessive and blunt 5'-termini. The enzyme is irreversibly heat inactivated at 65°C for 15 minutes. Applications: Alkaline phosphatase was used to examine its role in the prevention of high-fat-diet-induced metabolic syndrome in mice. it also may be used in pasteurization process for milks used in dairy products. Group: Enzymes. Synonyms: Alkaline. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Storage: Store at -20°C. Form: Solution in 50% glycerol containing 25 mM Tris-HCl, pH 7.5, 1 mM MgCl2. Source: Proprietary host. Species: Shrimp. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0807. | |
| Alkaline Phosphatase Mutein from Bovine, Recombinant | Part of marker enzyme portfolio. In addition to the AP Mutein, recombinant the lyophilizate contains a mixture of proteins from the Pichia system supporting the interference elimination. AP Mutein is lyophilized from a solution containing in NaCl, 0.2 mol/l; ZnCl2, 0.1 mmol/l; Tea, 30 mmol/l; MgCl2, 1 mmol/l; raffinose, 50% (w/v); pH approximately 7.6. Production is done according to the procedures of the active enzyme. Rely on the special design for reducing alkaline phosphatase-related assay interference interactions. Applications: Use alkaline phosphatase mutein (ap mutein) to eliminate human serum derived ap directed assay interferences. Group: Enzymes. Synonyms: ALKP; ALPase; Alk Phos; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. CAS No. 9001-78-9. ALP. Activity: <10 U/mg protein. Stability: At +2 to +8°C within specification range for 24 months. Appearance: White to yellowish lyophilizate. Source: Pichia pastoris. Species: Calf intestine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0992. | |
| α(1-3,4,6) Galactosidase from Green coffee bean, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. GLA. Mole weight: 39700 daltons. Activity: 71,000 units/mg. Storage: 4°C. Form: 20 mM Tris-HCl (pH 7.5), 50 mM NaCl and 1 mM EDTA. Source: E. coli. Species: Green coffee bean. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α(1-3,4,6) Galactosidase. Cat No: NATE-1263. | |
| α(1-3,6) Galactosidase from Xanthomonas manihotis, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Α1-3,6 galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of α1-3 and α1-6 linked d-galactopyranosyl residues from oligosaccharides. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Purity: > 95% determined by SDS-PAGE. GLA. Mole weight: 70000 daltons. Activity: 137,000 units/mg. Storage: Recommended storage temperature is 4°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM Na2EDTA. Source: E. coli. Species: Xanthomonas manihotis. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α(1-3,6) Galactosidase. Cat No: NATE-1279. | |
| α-2,3/2,6-Sialyltransferase from Pasteurella multocida, recombinant | α-2,3/2,6-Sialyltransferase from Pasteurella multocida, recombinant. Group: Enzymes. Synonyms: Alpha-2,3/2,6-sialyltransferase/sialidase; β-galactoside α-2,6-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acety. Enzyme Commission Number: EC 2.4.99.1, 2.4.99.4, 3.2.1.-. Purity: > 95 % as judged by SDS-PAGE. α-Sialyltransferase. Mole weight: 46240.5 Da. Storage: 4°C. Form: Supplied in 3.2 M ammonium sulphate. Source: Pasteurella multocida. Alpha-2,3/2,6-sialyltransferase/sialidase; β-galactoside α-2,6-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; β-galactoside α-2,3-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactoside α-2,3-N-acetylneuraminyl-transferase; CMP-N-acetylneuraminate:β-D-galactoside α-(2?3)-N-acetylneuraminyl-transferase; beta-galactoside alpha-2,6-sialyltransferase; CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine alpha-2,6-N-acetylneuraminyltransferase; beta-galactoside alpha-2,3-sialyltransferase; CMP-N-acetylneuraminate:beta-D-galactoside alpha-2,3-N-acetylneuraminyl-transferase; CMP-N-acetylneuraminate:beta-D-galactoside alpha-(2?3)-N-acetylneuraminyl-transferase. Cat No: NATE-1921 | |
| (+)-α-barbatene synthase | The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% α-barbatene, 17.8% thujopsene (cf. EC 4.2.3.79, thujopsene synthase) and 9.9% β-chamigrene (cf. EC 4.2.3.78, β-chamigrene synthase) plus traces of other sesquiterpenoids. Group: Enzymes. Synonyms: AtBS. Enzyme Commission Number: EC 4.2.3.69. 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-5230; (+)-α-barbatene synthase; EC 4.2.3.69; AtBS. Cat No: EXWM-5230. | |
| α-eudesmol synthase | The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% β-eudesmol, 16.8% 10-epi-γ-eudesmol, 10% α-eudesmol, and 5.6% aristolene. cf. EC 4.2.3.68 (β-eudesmol synthase) and EC 4.2.3.84 (10-epi-γ-eudesmol synthase). Group: Enzymes. Enzyme Commission Number: EC 4.2.3.85. 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-5248; α-eudesmol synthase; EC 4.2.3.85. Cat No: EXWM-5248. | |
| α-Galactosidase 110A from Bacteroides fragilis, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.-. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 67.9 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides fragilis. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 110A. Cat No: NATE-1405. | |
| α-Galactosidase 110A from Bacteroides thetaiotaomicron, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >50% by SDS-PAGE. GLA. Mole weight: 65.1 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 110A. Cat No: NATE-1403. | |
| α-Galactosidase 27A from Clostridium cellulolyticum, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 44.0 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Clostridium cellulolyticum. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 27A. Cat No: NATE-1400. | |
| α-Galactosidase 4A from Bacillus halodurans, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 51.8 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus halodurans. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 27A. Cat No: NATE-1404. | |
| α-Galactosidase 95A from Bacteroides ovatus, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 91 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides ovatus. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 95A. Cat No: NATE-1406. | |
| α-Galactosidase 97A from Bacteroides thetaiotaomicron, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >50% by SDS-PAGE. GLA. Mole weight: 74.7 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 97A. Cat No: NATE-1402. | |
| α-Galactosidase 97B from Bacteroides thetaiotaomicron, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: >90% by SDS-PAGE. GLA. Mole weight: 74.9 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 97B. Cat No: NATE-1401. | |
| α-Galactosidase from Cellvibrio mixtus, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: > 95 % as judged by SDS-PAGE. GLA. Mole weight: 44582.3 Da. Activity: 150 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Lyophilised powder. Source: Cellvibrio mixtus ATCC 12120. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-1175. | |
| α-Galactosidase from Clostridium cellulolyticum, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: > 95 % as judged by SDS-PAGE. GLA. Mole weight: 64179.5 Da. Activity: 186.7 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium cellulolyticum H10. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-1176. | |
| α-Galactosidase, positionally specific from Escherichia coli, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Activity using maltose as substrate at ph 6.0 at 25 deg c is ~2x > that obtained using p-nitrophenyl-α-d-glucoside as substrate at ph 6.8 at 37 oc. protein determined by biuret. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: E. coli. Species: Escherichia coli. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0293. | |
| α,γ-Homocysteinase from Trichomonas vaginalis, Recombinant | Recombinant Homocysteine α,γ-lyase is a pyridoxal-5-phosphate dependent enzyme. It is a mutant of homocysteinase from Trichomonas vaginalis encoded by mgl1 gene, containing three point mutations, such as; Phe47Leu, Asp172Glu, Ser308Tyr. The enzyme can metabolize homocysteine into α-keto butyrate, hydrogen sulfide and ammonia. Group: Enzymes. Synonyms: α,γ-Homocysteinase; Methionine gamma-lyase; mgl1. Purity: > 95% by SDS-PAGE. α,γ-Homocysteinase. Mole weight: 43 kDa. Activity: > 5 mU/mg. Storage: Reconstituted enzyme can be stored in working aliquots at -20°C and use within 3 months. Avoid repeated freeze-thaw cycles. Form: Lyophilized. Source: E. coli and fused to His-tag at N-terminus. Species: Trichomonas vaginalis. α,γ-Homocysteinase; Methionine gamma-lyase; mgl1; Homocysteine α,γ-Lyase; rHCYase. Cat No: NATE-1640. | |
| α-Methyl-glucuronidase 115A from Bacteroides ovatus, Recombinant | α-Methyl-glucuronidase 115A from Bacteroides ovatus, Recombinant. Group: Enzymes. Synonyms: EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase. Enzyme Commission Number: EC 3.2.1.-. Purity: >90% by SDS-PAGE. α-Glucuronidase. Mole weight: 96.6 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides ovatus. EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase; α-Methyl-glucuronidase 115A. Cat No: NATE-1452. | |
| Altenusin | Altenusin is a a biphenyl derivative with an IC50 value of 4.3±0.3 μM in the TR assay, which is isolated from the endophytic fungus Alternaria. It inhibits Src kinase with an IC50 value of 20 nM. Altenusin inhibits fibrillization of recombinant tau fragments in vitro and phosphorylation of tau in SH-SY5Y cells expressing human P301L mutant tau when used at a concentration of 10 μM. Altenusin is known to have antioxidant properties and to inhibit several enzymes, including myosin light chain kinase, sphingomyelinase, acetylcholinesterase, cFMS kinase, pp60c-SRc kinase and HIV-1 integrase. Synonyms: Alutenusin; MS 341; MS-341; MS341. Grade: ≥98%. CAS No. 31186-12-6. Molecular formula: C15H14O6. Mole weight: 290.27. | |
| AminoAcylase-1 from Human, Recombinant | Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes. Acy1 recombinant human produced in e. coli is a single, non-... SDS-PAGE. ACY1. Mole weight: 48 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. N-acyl-L-amino-acid amidohydrolase; ACY-1, ACY1D; ACYLASE; ACY1; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short | |
| Aminopeptidase from Aeromonas, Recombinant | Aeromonas Aminopeptidase is used in the processing of pharmaceutical proteins produces by genetic engineering as well as for physical and structural investigations and for sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at -X-Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins. Group: Enzymes. Synonyms: Aeromonas Aminopeptidase; Aminopeptidase. Aminopeptidase. Activity: 120 Units/mg protein. Stability: Two years when stored at -20°C, 2 weeks at 4°C. Please avoid freeze-thaw cycles. Appearance: Sterile filtered liquid formulation. Source: Aeromonas. Aeromonas Aminopeptidase; Aminopeptidase. Cat No: NATE-0811. | |
| AMPK (?1/?1/?1), His Tag, Human, Recombinant, S. frugiperda | AMPK (?1/?1/?1), Human, Recombinant, is a full length enzyme. Group: Fluorescence/luminescence spectroscopy. |  |
| anthocyanidin 3-O-glucoside 6''-O-acyltransferase | Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian). Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. It did not act on delphinidin 3,3',7-tri-O-glucoside. Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.215. 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-2161; anthocyanidin 3-O-glucoside 6''-O-acyltransferase; EC 2.3.1.215. Cat No: EXWM-2161. | |
| APC 366 trifluoroacetate salt | APC 366 is a mast cell tryptase inhibitor with Ki of 7.1 μM for human recombinant enzyme. It is a selective inhibitor of mast cell tryptase, which has been shown to inhibit antigen-induced early asthmatic response (EAR), late asthmatic response (LAR), and bronchial hyperresponsiveness (BHR) in a sheep model of allergic asthma. APC 366 can reduce maximum contractile response to histamine in isolated bronchial tissue from ovalbumin-sensitized guinea pigs. It can also reduce airway resistance and increases dynamic lung compliance in A. suum antigen-challenged pigs. Grade: ≥95%. Molecular formula: C22H28N6O4·xCF3COOH. Mole weight: 440.50. | |
| Apyrase from Potato, Recombinant | Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis. Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM. Apyrase (recombinant, e. coli) is a highly active atp-diphosphohydrolase that catalyses the sequential hydrolysis of atp to adp and adp to amp releasing inorganic phosphate. it is a recombinant version of one of several isoforms of apyrase. it can also hydrol...version of 5? triphosphorylated rna to ligatable monophosphorylated form that can be used for 5? rna adaptor ligation. conversion of 5? triphosphorylated rna to 5? exonuclease xrn-1 sensitive monophosphorylated rna. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Apyrase. Mole weight: 47 kDa. Activity: 3,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM MES (pH 6.5 25°C), 0.1 mM CaCl2, 1 mM DTT, 0.1% Tween-20 and 50% glycerol. Source: E. coli. Species: Potato. ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Cat No: NATE-1268. | |
| ARN 14686 | ARN14686 is a NAAA (N-acylethanolamine acid amidase) activity-based protein profiling (ABPP) probe. ARN14686 can be used to detect NAAA by using click chemistry in cell lysates or intact cells, which binds covalently to the N-terminal cysteine of catalytically active NAAA to form a thioester adduct. ARN14686 inhibits the hydrolysis of the NAAA substrate PAMCA in HEK293 cells. The IC50s for human is 6 and the IC50s for rat recombinant enzymes is 13 nM. Synonyms: (S)-Undec-10-yn-1-yl (2-oxoazetidin-3-yl)carbamate. Grade: ≥98% by HPLC. CAS No. 1628345-10-7. Molecular formula: C15H24N2O3. Mole weight: 280.36. | |
| AS-605240 potassium salt | Phosphoinositide 3-kinases (PI3Ks), also called phosphatidylinositol 3-kinases, are a family of enzymes involved in cellular functions such as cell growth, proliferation, differentiation, motility, survival and intracellular trafficking, which in turn are involved in cancer. AS-605240 inhibits human recombinant PI3Kγ, α, β, and δ in an ATP-competitive manner with IC50 values of 8, 60, 270, and 300 nM, respectively. AS-605240 also inhibits C5a-mediated phosphorylation of protein kinase B in RAW 264 cells with an IC50 value of 90 nM. AS-605240 potassium salt is the potassium salt form of AS-605240, which increase the water-solubility. Synonyms: AS-605240. Grade: ≥98%. Molecular formula: C12H6N3O2S·K. Mole weight: 295.4. | |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile filtered colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. | |
| ATP Sulfurylase from S. cerevisiae, Recombinant | In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate<-> diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism. Adenosine 5-triphosphate sulfurylase yeast recombinant produced in e. coli is a non-glycosylated, polypeptide chain containin...formed from aps and ppi. adenosine 5-triphosphate sulfurylase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. CAS No. 9012-39-9. ATP-sulfurylase. Storage: at -20°C. Source: E. coli. Species: S. cerevisiae. ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Cat No: NATE-1280. | |
| Autotaxin Inhibitor III, PF-8380 (Atx Inhibitor III, PF-8380, 6-(3-(Piperazin-1-yl)propanoyl)-benzo[d]oxazol-2(3H)-one) | An orally bioavailable piperazinyl benzoxazolone compound that acts as a substrate competitive and tight-binding inhibitor of autotaxin activity {IC50=2.8 and 1.7nM for recombinant human enzyme-b isoform employing FS-3 and LPC (lysophosphatidyl choline) as substrates, respectively; 1.16 and 1.15nM for rat/murine enzyme-FS-3 and fetal fibroblast cell-LPC; 101nM for human whole blood}. Displays desirable pharmacokinetics properties and efficiently blocks inflammation-induced LPA (lysophosphatidic acid) production both in plasma and at the site of inflammation by 95% in rat adjuvant-induced arthritis model (30mg/kg, p.o.).CAS No:1144035-53-9. Group: Biochemicals. Grades: Highly Purified. CAS No. 1144035-53-9. Pack Sizes: 10mg. Molecular Formula: C??H??Cl?N?O?. US Biological Life Sciences. |  Worldwide |
| β-(1?3,6)-Galactosidase from Xanthomonas manihotis, Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Recombinant, expressed in e. coli, buffered aqueous solution. Group: Enzymes. Synonyms: β-(1?3,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 120 units/mg protein. Stability: 2-8°C. Form: buffered aqueous solution. Source: E. coli. Species: Xanthomonas manihotis. β-(1?3,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: vial of 1.9 units. Cat No: NATE-0301. | |
| β (1?4)-Galactosidase from Streptococcus pneumoniae, Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Recombinant, expressed in e. coli, buffered aqueous solution. Group: Enzymes. Synonyms: β (1?4)-Galactosidase; 9031-11-2; β-Galactosidase; beta-gal; β-gal; GLB; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 6 units/mg protein. Stability: 2-8°C. Form: buffered aqueous solution. Source: E. coli. Species: Streptococcus pneumoniae. β (1?4)-Galactosidase; 9031-11-2; β-Galactosidase; beta-gal; β-gal; GLB; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: vial of 0.06 unit. Cat No: NATE-0300. | |
| β-Acetylglucosaminidase 18A from Bacteroides thetaiotaomicron, Recombinant | β-acetylglucosaminidase 18A, is an enzyme from Bacteroides thetaiotaomicron that participates in the endohydrolysis of the diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the (Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Recombinant BtAcp18A (GH18), purified from Escherichia coli, is a single domain family 18 Glycoside Hydrolase (GH18). Group: Enzymes. Synonyms: beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: >50% by SDS-PAGE. β-N-Acetylhexosaminidase. Mole weight: 50.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-1291. | |
| β-chamigrene synthase | The recombinant enzyme from the plant Arabidopsis thaliana produces 27.3% (+)-α-barbatene, 17.8% (+)-thujopsene and 9.9% (+)-β-chamigrene plus traces of other sesquiterpenoids. See EC 4.2.3.69 (+)-α-barbatene synthase, and EC 4.2.3.79 thujopsene synthase. Group: Enzymes. Enzyme Commission Number: EC 4.2.3.78. 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-5240; β-chamigrene synthase; EC 4.2.3.78. Cat No: EXWM-5240. | |
| β-Enolase from Human, Recombinant | Beta-enolase, also known as ENO3, is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in skeletal muscle cells in the adult. ENO3 play a role in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in its gene can be associated with metabolic myopathies that may result from decreased stability of the enzyme. Recombinant human ENO3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Purity: > 95% (SDS-PAGE). Enolase. Mole weight: 49 kDa. Storage: Store at -70°C. Form: Liquid; 0.5 mg/mL solution in 20 mM Tris-HCl (pH 8.0) containing 1 mM DTT, 20% glycerol and 0.1 mM NaCl. Source: E. coli. Species: Human. 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Cat No: NATE-0941. | |
| β-eudesmol synthase | The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% β-eudesmol, 16.8% 10-epi-γ-eudesmol (cf. EC 4.2.3.84, 10-epi-γ-eudesmol synthase), 10% α-eudesmol (cf. EC 4.2.3.85, α-eudesmol synthase), and 5.6% aristolene. Group: Enzymes. Enzyme Commission Number: EC 4.2.3.68. 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-5229; β-eudesmol synthase; EC 4.2.3.68. Cat No: EXWM-5229. | |
| Beta Lactamase from E.coli, Recombinant | Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Group: Enzymes. Synonyms: b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Enzyme Commission Number: EC 3.5.2.6. Purity: Greater than 90.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. β-Lactamase. Mole weight: 29 kDa. Activity: 700IU/mg. Stability: Lyophilized Beta Lactamase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Beta Lactamase Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Form: Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7. Source: E. coli. Species: E. coli. b-Lactamase; EC 3.5.2.6; TEM precursor; β-lactamase. Cat No: NATE-1886. | |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| Bpu10I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 5-fold overdigestion with enzyme 80% of the dna fragments can be ligated. of these 90% can be recut. in the presence of 10% peg ligation is better. Group: Restriction Enzymes. Purity: 200U; 1000U. CC↑TNAGC GGANT↓CG. Activity: 5000u.a./ml. Appearance: 10 X SE-buffer K. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries recombinant plasmids. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0.1 mM EDTA; 1 mM DTT; 50% glycerol. Cat No: ET-1039RE. | |
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