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| Product | Description | |
|---|---|---|
| 1, 2, 3, 4-Tetra hydro-N- hydroxy-2- [ (1- methyl -1H-pyrrol-2-yl ) carbonyl ] -6-isoquinolinecarboxamid e | HDAC6 Inhibitor is a potent and selective inhibitor of HDAC6 that poorly blocks other HDAC enzymes. HDAC6 is a predominantly cytoplasmic enzyme that targets α-tubulin, cortactin, and heat shock protein 90, as well as other substrates. Group: Biochemicals. Grades: Highly Purified. CAS No. 1259296-46-2. Pack Sizes: 500ug, 1mg. Molecular Formula: C16H17N3O3, Molecular Weight: 299.32. US Biological Life Sciences. |  Worldwide |
| 1,3,5,7-Tetramethyl-8-(C3-COOH)4,4-difluoro-4-bora-3a,4a-diaza-s-indacene | BODIPY dyes are used to generate fluorescent conjugates of proteins, nucleotides, oligonucleotides and dextrans, as well as to prepare fluorescent enzyme substrates, fatty acids, phospholipids, lipopolysaccharides, receptor ligands and polystyrene microspheres. Synonyms: 4-(4,4-Difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene-8-yl)-butyric Acid. CAS No. 878674-84-1. Molecular formula: C17H22BF2N2O2. Mole weight: 335.18. |  |
| 2,6-Diiodo-1,3,5,7-tetramethyl-8-phenyl-4,4-difluoroboradiazasindacene | BODIPY dyes are used to generate fluorescent conjugates of proteins, nucleotides, oligonucleotides and dextrans, as well as to prepare fluorescent enzyme substrates, fatty acids, phospholipids, lipopolysaccharides, receptor ligands and polystyrene microspheres. Synonyms: 5,5-Difluoro-2,8-diiodo-1,3,7,9-tetramethyl-10-phenyl-5H-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-4-ium-5-uide. CAS No. 1083009-44-2. Molecular formula: C19H17BF2I2N2. Mole weight: 575.974. | |
| 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) | Catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer). Part of a propionate degradation pathway. The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher. 2-methylisocitrate and isocitrate were not substrates. An iron-sulfur protein. Group: Enzymes. Enzyme Commission Number: EC 4.2.1.117. 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-4957; 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming); EC 4.2.1.117. Cat No: EXWM-4957. |  |
| 2-Phenylethyl 1-Thio-β-D-thiogalactoside | 2-Phenylethyl 1-Thio-β-D-thiogalactoside is an indispensable chemical compound widely employed in the realm of biomedical research, holding significant value concerning the comprehensive analysis of enzyme activities, protein interactions, and substrates in diverse biological systems. This exceptionally precious substance plays a pivotal role in delving into the intricate realms of galactose-related disorders, specifically galactosemia. Synonyms: 2-Phenylethyl-β-D-thiogalactoside; Phenylethyl beta-D-thiogalactopyranoside; (2R,3R,4S,5R,6S)-2-(Hydroxymethyl)-6-(phenethylthio)tetrahydro-2H-pyran-3,4,5-triol. Grades: 98%. CAS No. 63407-54-5. Molecular formula: C14H20O5S. Mole weight: 300.37. | |
| (3-Aminopropyl)trimethoxysilane | 97%. Uses: Aptms can be multilayered on siox substrates by a layer by layer self assembly. aptms has also been used as a silane coupling agent on silver nanoparticles.aptms is used for the synthesis of gold nano-bipyramids which can be used as substrates for c-reactive protein (crp) antibodies that were detected by localized surface plasmon resonance(lspr). mesoporous silica matrix can be incorporated with aptms for the removal of chromium (cr) from waste water. it can also be used to silanize magnetic iron oxide nanoparticles(mionps) for the separation of cross-linked enzyme aggregations (cleas) from the reaction medium. it may be coated on tio2 to improve the power conversion efficiency (pce) as a critical parameter to assess the overall performance of heterojunction perovskite solar cells (pscs). Group: Saltself-assembly materials. Alternative Names: 3-(Trimethoxysilyl)propylamine. CAS No. 13822-56-5. Pack Sizes: 5 mL/100 mL/500 mL. Product ID: 3-trimethoxysilylpropan-1-amine. Molecular formula: 179.29 g/mol. Mole weight: C6H17NO3Si. CO[Si](CCCN)(OC)OC. InChI=1S/C6H17NO3Si/c1-8-11(9-2, 10-3)6-4-5-7/h4-7H2, 1-3H3. SJECZPVISLOESU-UHFFFAOYSA-N. 0.97. |  |
| 3-Bodipy-propanoic acid | BODIPY dyes are used to generate fluorescent conjugates of proteins, nucleotides, oligonucleotides and dextrans, as well as to prepare fluorescent enzyme substrates, fatty acids, phospholipids, lipopolysaccharides, receptor ligands and polystyrene microspheres. Synonyms: BDP FL carboxylic acid;4,4-Difluoro-5,7-dimethyl-3-(2-carboxyethyl)-4-bora-3a,4a-diaza-S-indacene; 7-(2-carboxyethyl)-5,5-difluoro-1,3-dimethyl-5H-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-4-ium-5-uide; BDP FL acid; BODIPY FL. Grades: 95%. CAS No. 165599-63-3. Molecular formula: C14H15BF2N2O2. Mole weight: 292.093. | |
| 3-hydroxyacyl-[acyl-carrier-protein] dehydratase | This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The enzyme uses fatty acyl thioesters of ACP in vivo. Different forms of the enzyme may have preferences for substrates with different chain length. For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyses EC 5.3.3.14, trans-2-decenoyl-[acyl-carrier protein] isomerase. Despite the differences both forms...hydratase. Enzyme Commission Number: EC 4.2.1.59. CAS No. 9030-85-7. 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-5047; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; EC 4.2.1.59; 9030-85-7; fabZ (gene name); fabA (gene name); D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase; D-3-hydroxyoctanoyl-acyl carrier protein dehydratase; β-hydroxyoctanoyl-acyl carrier protein dehydrase; β-hydroxyoctanoyl thioester dehydratase; β-hydroxyoctanoyl-ACP-dehydrase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hyd | |
| 3-oxoacyl-[acyl-carrier-protein] reductase | Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates. Group: Enzymes. Synonyms: β-ketoacyl-[acyl-carrier protein](ACP) reductase; β-ketoacyl acyl carrier protein (ACP) reductase; β-ketoacyl reductase; β-ketoacyl thioester reductase; β-ketoacyl-ACP reductase; β-ketoacyl-acyl carrier protein reductase; 3-ketoacyl acyl carrier protein reductase; NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase; 3-oxoacyl-[ACP]reductase; (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.100. CAS No. 37250-34-3. 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-0003; 3-oxoacyl-[acyl-carrier-protein] reductase; EC 1.1.1.100; 37250-34-3; β-ketoacyl-[acyl-carrier protein](ACP) reductase; β-ketoacyl acyl carrier protein (ACP) reductase; β-ketoacyl reductase; β-ketoacyl thioester reductase; β-ketoacyl-ACP reductase; β-ketoacyl-acyl carrier protein reductase; 3-ketoacyl acyl carrier protein reductase; NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase; 3-oxoacyl-[ACP]reductase; (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Cat No: EXWM-0003. | |
| 4-Ethylresorcinol | 4-Ethylresorcinol, a derivative of resorcinol, can act as substrates of tyrosinase. 4-Ethylresorcinol possess hypopigmentary effects. 4-Ethylresorcinol attenuates mRNA and protein expression of tyrosinase-related protein (TRP)-2, and possessed antioxidative effect by inhibiting lipid peroxidation [1] [2]. Uses: Scientific research. Group: Natural products. CAS No. 2896-60-8. Pack Sizes: 10 mM * 1 mL; 500 mg. Product ID: HY-W015782. |  |
| 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase | Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory.Octanoyl-S-[BtrI acyl-carrier protein] is also accepted. Group: Enzymes. Synonyms: btrO (gene name). Enzyme Commission Number: EC 1.14.14.13. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0910; 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase; EC 1.14.14.13; btrO (gene name). Cat No: EXWM-0910. | |
| 6-Phosphogluconic Dehydrogenase from Microorganism | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Enzyme Commission Number: EC 1.1.1.44. 6-Phosphogluconic Dehydrogenase. Mole weight: ca. 132,000. Activity: >40 U/mg protein. Storage: Stable at -20 °C for at least six months. Form: Lyophilized. Source: Microorganism. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-1937. | |
| 7-Propargylamino-7-deaza-dATP - ATTO-540Q | 7-Propargylamino-7-deaza-dATP - ATTO-540Q is a fluorescent nucleotide analogue used in biomedical research to label DNA during sequencing and microscopy. It is particularly useful for detecting and studying DNA-protein interactions involved in chromatin remodeling, transcription, and DNA repair pathways. Its unique properties and compatibility with various enzymes and substrates make it a valuable tool for investigating DNA-related diseases such as cancer and genetic disorders. Synonyms: 7-Deaza-7-propargylamino-2'-deoxyadenosine-5'-triphosphate, labeled with ATTO 540Q, Triethylammonium salt. Grades: ≥ 95% by HPLC. Molecular formula: C14H20N5O12P3- ATTO 540Q (free acid). Mole weight: 1083.26 (free acid). | |
| 8(4'-bromophenyl)-1,3,5,7-tetramethyl-BODIPY | BODIPY dyes are used to generate fluorescent conjugates of proteins, nucleotides, oligonucleotides and dextrans, as well as to prepare fluorescent enzyme substrates, fatty acids, phospholipids, lipopolysaccharides, receptor ligands and polystyrene microspheres. Synonyms: 8-(4-Bromophenyl)-4,4-difluoro-1,3,5,7-tetramethyl-4-bora-3a,4a-diaza-s-indacene. CAS No. 850534-66-6. Molecular formula: C19H18BBrF2N2. Mole weight: 403.077. | |
| Acyl-CoA oxidase from Microorganism | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2? trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Mole weight: 78 kDa (SDS-PAGE). Activity: >30U/mg protein. Storage: Store at -20°C. Form: Yellow powder, lyophilized. Source: Microorganism. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Cat No: NATE-1711. | |
| Acyl-CoA oxidase, Recombinant | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Purity: 90% (SDS-PAGE test). Acyl-CoA oxidase. Mole weight: About 90KDa (SDS-PAGE detection). Activity: 40U/mg protein. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preservation. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-292. | |
| acyl-homoserine-lactone synthase | Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. N-(3-Oxohexanoyl)-[acyl-carrier protein] and hexanoyl-[acyl-carrier protein] are the best substrates. The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier protein] rather than from fatty-acid degradation through acyl-CoA. S-Adenosyl-L-methionine cannot be rep...No. 176023-66-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2126; acyl-homoserine-lactone synthase; EC 2.3.1.184; 176023-66-8; acyl-homoserine lactone synthase; acyl homoserine lactone synthase; acyl-homoserinelactone synthase; acylhomoserine lactone synthase; AHL synthase; AHS; AHSL synthase; AhyI; AinS; AinS protein; autoinducer synthase; autoinducer synthesis protein rhlI; EsaI; ExpISCC1; ExpISCC3065; LasI; LasR; LuxI; LuxI protein; LuxM; N-acyl homoserine lactone synthase; RhlI; YspI acyl-[acyl carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadeno | |
| Adenosine-5'-(γ-thio)-triphosphate tetralithium salt | Adenosine 5-[γ-thio]triphosphate Tetralithium Salt is used as a reagent in the synthesis of DNA N-acetylglucosamine analogs. Adenosine 5'-(γ-thio)-triphosphate (lithium salt) is a stable analog of ATP that acts as a potent agonist of G protein-coupled P2Y2 and P2Y11 receptors (pEC50 = 5.52 for P2Y11).1 It has been used to identify kinase substrates, has been implemented as a reagent in the synthesis of DNA N-acetylglucosamine analogs, and can serve as a substrate for the RNA-stimulated nucleotide hydrolysis and RNA unwinding activities of eukaryotic initiation factor-4A. Group: Biochemicals. Alternative Names: ATP-γS; ATPγS tetralithium salt. Grades: Highly Purified. CAS No. 93839-89-5. Pack Sizes: 1mg, 5mg, 10mg. Molecular Formula: C??H??N?O??P?SLi?, Molecular Weight: 551. US Biological Life Sciences. | Worldwide |
| alditol oxidase | The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly. Belongs in the vanillyl-alcohol-oxidase family of enzymes. Group: Enzymes. Synonyms: xylitol oxidase; xylitol:oxygen oxidoreductase; AldO. Enzyme Commission Number: EC 1.1.3.41. CAS No. 177322-52-0. 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-0414; alditol oxidase; EC 1.1.3.41; 177322-52-0; xylitol oxidase; xylitol:oxygen oxidoreductase; AldO. Cat No: EXWM-0414. | |
| all-trans-retinol dehydrogenase (NAD+) | The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids. Group: Enzymes. Synonyms: retinol (vitamin A1) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name). Enzyme Commission Number: EC 1.1.1.105. CAS No. 9033-53-8. 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-0008; all-trans-retinol dehydrogenase (NAD+); EC 1.1.1.105; 9033-53-8; retinol (vitamin A1) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name). Cat No: EXWM-0008. | |
| Aminopeptidase | Aminopeptidase catalyzes the cleavage of amino acids from the amino terminus of protein or peptide substrates [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9031-94-1. Pack Sizes: 50 U; 100 U. Product ID: HY-P2842. | |
| aminopeptidase S | Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation. This enzyme contains two zinc molecules in its active site and is activated by Ca2+. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe. Peptides with proline in the P1' position are not substrates. Belongs in peptidase family M28. Group: Enzymes. Synonyms: Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Enzyme Commission Number: EC 3.4.11.24. 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-4021; aminopeptidase S; EC 3.4.11.24; Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Cat No: EXWM-4021. | |
| Anaphase-Promoting Complex Inhibitor, TAME (TAME Hydrochloride) | TAME is a potent ubiquitin ligase inhibitor that specifically blocks Anaphase-Promoting Complex (APC) activation by directly binding to APC and disrupts the IR-tail-dependent interactions between APC and its activator proteins Cdc20 or Cdh1. It stabilizes APC substrates and is shown to inhibit cyclin proteolysis in mitotic Xenopus egg extract with an IC50=12uM. Group: Biochemicals. Grades: Highly Purified. CAS No. 1784-03-8. Pack Sizes: 50mg. Molecular Formula: C??H??N?O?S · HCl, Molecular Weight: 378.87. US Biological Life Sciences. | Worldwide |
| arginine-pyruvate transaminase | A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked. Group: Enzymes. Synonyms: arginine:pyruvate transaminase; AruH; ATase. Enzyme Commission Number: EC 2.6.1.84. 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-2925; arginine-pyruvate transaminase; EC 2.6.1.84; arginine:pyruvate transaminase; AruH; ATase. Cat No: EXWM-2925. | |
| ATPγS | ATPγS is an agonist of G protein-coupled P2Y2 and P2Y11 receptors (pEC50 = 5.52 for P2Y11). It has been used to identify kinase substrates, used as a reagent in the synthesis of DNA N-acetylglucosamine analogs and a substrate for the RNA-stimulated nucleotide hydrolysis as well as RNA unwinding activities of eukaryotic initiation factor-4A. Uses: Atpγs is an agonist of g protein-coupled p2y2 and p2y11 receptors (pec50 = 5.52 for p2y11). Synonyms: Adenosine-5'-(γ-thio)-triphosphate, Tetralithium salt; Adenosine-5'-(3-thio)-triphosphate, Adenosine-5'-(3-thiotriphosphate). Grades: ≥ 90% by HPLC, contains < 10% ADP. Molecular formula: C10H16N5O12P3S (free acid). Mole weight: 523.24 (free acid). | |
| ATPγS tetralithium salt | Adenosine 5'-(γ-thio)-triphosphate lithium salt is a stable analog of ATP. It is a potent agonist of G protein-coupled P2Y2 and P2Y11 receptors. Adenosine 5'-(γ-thio)-triphosphate has also been used to identify kinase substrates and can serve as a substrate for the RNA-stimulated nucleotide hydrolysis and RNA unwinding activities of eukaryotic initiation factor-4A. Uses: Affinity labels. Synonyms: Adenosine-5'-(γ-thio)-triphosphate tetralithium salt. Grades: ≥90% by HPLC. CAS No. 93839-89-5. Molecular formula: C10H12Li4N5O12P3S. Mole weight: 546.98. | |
| AZD8055 | A potent, selective, and orally bioavailable ATP-competitive mTOR kinase inhibitor with an IC50 of 0.8 nM. It inhibits the phosphorylation of mTORC1 substrates p70S6K and 4E-BP1 as well as phosphorylation of the mTORC2 substrate AKT and downstream proteins. The rapamycin-resistant T37/46 phosphorylation sites on 4E-BP1 were fully inhibited by AZD8055, resulting in significant inhibition of cap-dependent translation. In vitro, AZD8055 potently inhibits proliferation and induces autophagy in H838 and A549 cells. In vivo, AZD8055 induces a dose-dependent pharmacodynamic effect on phosphorylated S6 and phosphorylated AKT at plasma concentrations leading to tumor growth inhibition. Group: Biochemicals. Alternative Names: 5- [2, 4-Bis [ (3S) -3-methyl-4-morpholinyl] pyrido [2, 3-d] pyrimidin-7-yl] -2-methoxy Benzene methanol; [5-[2,4-Bis((3S)-3-methylmorpholin-4-yl)pyrido[2,3-d]pyrimidin-7-yl]- 2-methoxyphenyl] methanol; AZD 8055; [5- [2, 4-Bis ( (3S) -3-methylmorpholin-4-yl) pyrido [5, 6-e] pyrimidin-7-yl] -2-methoxyphenyl] methanol. Grades: Purified. CAS No. 1009298-09-2. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| BDY FL, SE | BODIPY dyes are used to generate fluorescent conjugates of proteins, nucleotides, oligonucleotides and dextrans, as well as to prepare fluorescent enzyme substrates, fatty acids, phospholipids, lipopolysaccharides, receptor ligands and polystyrene microspheres. Synonyms: 3-(3-((2,5-dioxopyrrolidin-1-yl)oxy)-3-oxopropyl)-5,5-difluoro-7,9-dimethyl-5H-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-4-ium-5-uide; 7-(3-((2,5-Dioxopyrrolidin-1-yl)oxy)-3-oxopropyl)-5,5-difluoro-1,3-dimethyl-5H-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-4-ium-5-uide; 4,4-Difluoro-5,7-Dimethyl-4-Bora-3a,4a-Diaza-s-Indacene-3-Propionic Acid, Succinimidyl Ester; BDP FL NHS ester. Grades: NMR 1H, HPLC-MS (95+%). CAS No. 146616-66-2. Molecular formula: C18H18BF2N3O4. Mole weight: 389.166. | |
| β-(1?3,4,6)-Galactosidase from Streptococcus pneumoniae and Xanthomonas sp., 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. Group: Enzymes. Synonyms: β-(1?3,4,6)-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: > 70 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Streptococcus pneumoniae and Xanthomonas sp. β-(1?3,4,6)-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 0.24 unit. Cat No: NATE-0299. | |
| 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-Galactose Dehydrogenase S from Pseudomonas fluorescens, Recombinant | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Applications: Β-galactose dehydrogenase s has been used in the colorimetric microassay method to determine the level of galactose and galactose-1-phosphate in blood. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.. Enzyme Commission Number: EC 1.1.1.48. Galactose dehydrogenase. Activity: 80 U/mg protein. Storage: Store at -20°C. Form: Suspension in 3.2 M ammonium sulfate solution, pH approximately 6. Source: E. coli. Species: Pseudomonas fluorescens. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Cat No: NATE-1710. | |
| β-Galactosidase from E. coli, Recombinant (EIA Grade) | 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. Synthezise stable, highly active and reproducible ss-gal antigen and antibody conjugates. eliminate the risk of bse contamination: no animal-derived components are used in the production process. Applications: Marker enzyme for the manufacturing of antibody- and antigen-enzyme conjugates incorporated in immunoassays for colorimetric and fluorimetric detection. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosid. CAS No. 9031-11-2. β-gal. Mole weight: 465 kDa. Activity: > 700 U/mg protein. Stability: At -15 to -25°C within specification range for 24 months. Store under nitrogen. Appearance: White lyophilizate, stabilized with phosphate buffer and sucrose. Source: E. coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase; β-Galactosidase EIA Grade. Cat No: NATE-0986. | |
| β-Galactosidase Mutein from E. coli, 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. Eliminate the interference activity of β-galactosidase directed antibodies: β-galactose mutein reacts with β-galactosidase directed antibodies in the same way as the active β-galactosidase. Applications: Use β-galactosidase mutein to eliminate β-galactosidase directed interferences in immunoassays derived from human sera. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; trilactase; β-D-galactanase; β-D-galactoside galactohydrolase. CAS No. 9031-11-2. β-gal. Activity: < 0.2 U/mg protein. Stability: At -15 to -25°C within specification range for 24 months. Appearance: White lyophilizate. Source: E. coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0985. | |
| β-Glucanase 1, thermostable, Recombinant | Beta-glucosidase is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Applications: Β-glucanase is used to study cell wall modifications and for carbohydrate hydrolysis. it has been used to supplement barley-based diets for poultry and to study the reopening signal conduits and release of dormancy in the populusspecies. Group: Enzymes. Synonyms: β-Glucanase 1; β-Glucanase 1, thermostable; 62213-14-3. CAS No. 62213-14-3. Purity: > 90% (SDS-PAGE) 19-21 mg protein/mL (280 nm, UV). β-glucanase. Mole weight: mol wt 45 kDa. Activity: > 10 units/mg protein. Storage: 2-8°C. Form: liquid, Supplied as a solution in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, and 25% glycerol. Source: E. coli. β-Glucanase 1; β-Glucanase 1, thermostable; 62213-14-3. Cat No: NATE-0764. | |
| β-Glucanase 2, thermostable, Recombinant | Beta-glucosidase is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Applications: Β-glucanase is used to study cell wall modifications and for carbohydrate hydrolysis. it has been used to supplement barley-based diets for poultry and to study the reopening signal conduits and release of dormancy in the populus species. Group: Enzymes. Synonyms: β-Glucanase 2; β-Glucanase 2, thermostable; 62213-14-3. CAS No. 62213-14-3. Purity: > 20 mg protein/mL (Bradford) > 90% (SDS-PAGE). β-glucanase. Mole weight: mol wt 38 kDa. Activity: > 1.0 units/mg protein. Storage: 2-8°C. Form: liquid, Supplied as a solution in 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, and 25% glycerol. Source: E. coli. β-Glucanase 2; β-Glucanase 2, thermostable; 62213-14-3. Cat No: NATE-0765. | |
| β-Glucosidase, thermostable, Recombinant | Beta-glucosidase is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Applications: Β-glucosidase is a lysosomal enzyme which breaks β1->4 bonds that link oligosaccharides. β-glucosidase is used to st...osidase, amygdalase; linamarase; salicilinase; beta-1,6-glucosidase; β-Glucocerebrosidase; acid β-glucosidase. CAS No. 9001-22-3. Purity: > 90% (SDS-PAGE) 19-21 mg protein/mL (UV). β-Glucosidase. Mole weight: mol wt 53 kDa. Activity: > 24 units/mg protein. Storage: 2-8°C. Form: liquid, Supplied as a solution in 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, and 25% glycerol. Source: E. coli. 9001-22-3; β-Glucosidase, thermostable; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase, amygdalase; linamarase; salicilinase; b | |
| β-ketoacyl-[acyl-carrier-protein] synthase I | This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16). The substrate specificity is very similar to that of EC 2.3.1.179, β-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Δ9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. Group: Enzymes. Synonyms: β-ketoa. Enzyme Commission Number: EC 2.3.1.41. CAS No. 9077-10-5. 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-2220; β-ketoacyl-[acyl-carrier-protein] synthase I; EC 2.3.1.41; 9077-10-5; β-ketoacyl-ACP synthase I; β-ketoacyl synthetase; β-ketoacyl-ACP synthetase; β-ketoacyl-acyl carrier protein synthetase; β-ketoacyl-[acyl carrier protein] synthase; β-ketoacylsynthase; condensing enzyme (ambiguous); 3-ketoacyl-acyl carrier protein synthase; fatty acid condensing enzyme; acyl-malonyl(acyl-carrier-protein)-c | |
| β-N-Acetylglucosaminidase from Streptococcus pneumoniae, Recombinant | Hexosaminidase, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Appli...Commission Number: 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: > 80 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Streptococcus pneumoniae. EC 3.2.1.52; 9012-33-3; hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase. Pack: vial of > 1.0 unit. Cat No: NATE-0782. | |
| BODIPY-FL NHS ester | BODIPY FL NHS ester (BODIPY FL, SE) is a cell membranes-penatrable amine-reactive fluorescent probe. The maximum excitation/emission wavelength of the BODIPY-FL NHS ester are 502/511 nm, respectively. BODIPY-FL NHS ester has high stability and is insensitive to the polarity, pH and type of solvent, and can maintain stable fluorescence properties under different environmental conditions. BODIPY-FL NHS ester can be used for the synthesis of protease substrates, live cell imaging, protein labeling and immunoassay [1] [2]. Uses: Scientific research. Group: Fluorescent dye. Alternative Names: BODIPY FL,SE. CAS No. 146616-66-2. Pack Sizes: 1 mg; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-110210. | |
| calpain-3 | This Ca2+-dependent enzyme is found in skeletal muscle and is genetically linked to limb girdle muscular dystrophy type 2A. The enzyme is activated by autoproteolytic cleavage of insertion sequence 1 (IS1),which allows substrates and inhibitors gain access to the active site. Substrates include the protein itself and connectin/titin. Belongs in peptidase family C2. Group: Enzymes. Synonyms: p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Enzyme Commission Number: EC 3.4.22.54. 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-4229; calpain-3; EC 3.4.22.54; p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Cat No: EXWM-4229. | |
| 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-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. | |
| CCT-137690 | CCT137690, an aurora kinase inhibitor CCT137690, is a highly selective, orally bioavailable imidazo[4,5-b]pyridine derivative that inhibits Aurora A and B kinases with low nanomolar IC50 values in both biochemical and cellular assays and exhibits anti-proliferative activity against a wide range of human solid tumour cell lines. CCT137690 efficiently inhibits histone H3 and TACC3 phosphorylation (Aurora B and Aurora A substrates, respectively) in HCT116 and HeLa cells. Continuous exposure of tumour cells to the inhibitor causes multipolar spindle formation, chromosome misalignment, polyploidy and apoptosis. This is accompanied by p53/p21/BAX induction, thymidine kinase 1 (TK1) downregulation and PARP cleavage. Furthermore, CCT137690 treatment of MYCN-amplified neuroblastoma cell lines inhibits cell proliferation and decreases MYCN protein expression. Importantly, in a transgenic mouse model of neuroblastoma (TH-MYCN) that overexpresses MYCN protein and is predisposed to spontaneous neuroblastoma formation, this compound significantly inhibits tumour growth. The potent preclinical activity of CCT137690 suggests that this inhibitor may benefit patients with MYCN amplified neuroblastoma. Synonyms: CCT-137690. CCT 137690. CCT137690. CAS No. 1095382-05-0. Molecular formula: C26H31BrN8O. Mole weight: 551.48. | |
| Cellulase, thermostable from Dictyoglomus turgidum, Recombinant | Product exhibits endo-cellulase, β-glucanase activity and β-mannase activities when assayed using insoluble AZCL-linked substrates as well as exo-cellulase and cellobiohydralase activities. Group: Enzymes. Synonyms: 1,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS. Enzyme Commission Number: EC 3.2.1.4. CAS No. 9012-54-8. Purity: ≥90% (SDS-PAGE). Cellulase. Mole weight: 37 kDa. Activity: ≥200 units/mg protein. Storage: 2-8°C. Form: Supplied as as solution in 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, and 25% glycerol. Source: E. coli. Species: Dictyoglomus turgidum. 1,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS. Cat No: NATE-1928. | |
| cGMP-dependent protein kinase | CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase. Group: Enzymes. Synonyms: 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Enzyme Commission Number: EC 2.7.11.12. CAS No. 141588-27-4. 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-3131; cGMP-dependent protein kinase; EC 2.7.11.12; 141588-27-4; 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Cat No: EXWM-3131. | |
| chloride peroxidase | Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter ...peroxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols. Group: Enzymes. Synonyms: chloroperoxidase; CPO; vanadium haloperoxidase. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. 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-0491; chloride peroxidase; EC 1.11.1.10; 9055-20-3; chloroperoxidase; CPO; vanadium haloperoxidase. Cat No: EXWM-0491. | |
| cholesterol 25-hydroxylase | Unlike most other sterol hydroxylases, this enzyme is not a cytochrome P-450. Instead, it uses diiron cofactors to catalyse the hydroxylation of hydrophobic substrates. The diiron cofactor can be either Fe-O-Fe or Fe-OH-Fe and is bound to the enzyme through interactions with clustered histidine or glutamate residues. In cell cultures, this enzyme down-regulates cholesterol synthesis and the processing of sterol regulatory element binding proteins (SREBPs). Group: Enzymes. Synonyms: cholesterol 25-monooxygenase. Enzyme Commission Number: EC 1.14.99.38. CAS No. 60202-07-5. 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-1049; cholesterol 25-hydroxylase; EC 1.14.99.38; 60202-07-5; cholesterol 25-monooxygenase. Cat No: EXWM-1049. | |
| Cholesterol-25-Hydroxylase, Human (CH25H) | Cholesterol-25-Hydroxylase (CH25H) is an intronless gene that is involved in cholesterol and lipid metabolism. The encoded protein is a membrane protein and contains clusters of histidine residues essential for catalytic activity. Unlike most other sterol hydroxylases, this enzyme is a member of a small family of enzymes that utilize diiron cofactors to catalyze the hydroxylation of hydrophobic substrates. Group: Molecular Biology. Pack Sizes: 10ug, 50ug, 100ug. US Biological Life Sciences. | Worldwide |
| CMP-Sialic Acid Synthetase from Neisseria meningitidis group B, Recombinant | In enzymology, a N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) is an enzyme that catalyzes the chemical reaction:CTP + N-acylneuraminate<-> diphosphate + CMP-N-acylneuraminate. Thus, the two substrates of this enzyme are CTP and N-acylneuraminate, whereas its two products are diphosphate and CMP-N-acylneuraminate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in aminosugars metabolism. Applications: The enzyme has been utilized to synthesize cmp-sialic acid and its derivatives. Group: Enzymes. Synonyms: EC 2.7.7.43; N-acylneuraminate cytidylyltransferase; CMP-sialate pyrophosp. Enzyme Commission Number: EC 2.7.7.43. CAS No. 9067-82-7. Acid Synthetase. Activity: > 10 units/mg protein. Storage: -20°C. Form: , Supplied as a lyophilized powder containing Tris-HCl and NaCl. Source: E. coli BL21. Species: Neisseria meningitidis group B. EC 2.7.7.43; N-acylneuraminate cytidylyltransferase; CMP-sialate pyrophosphorylase; CMP-sialate synthase; cytidine 5'-monophosphosialic acid synthetase; CMP-Neu5Ac synthetase; CMP-NeuAc synthetase; acylneuraminate cytidyltransferase; CMP-N-acetylneuraminate synthetase; CMP-N-acetylneuraminate synthase; CMP-N-acetylneuraminic acid synthase; CMP- | |
| colneleate synthase | A heme-thiolate protein (P-450). It catalyses the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. It forms also (8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid (i.e. colnelenate) from (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate. The corresponding 13-hydroperoxides are poor substrates. The divinyl ethers colneleate and colnelenate have antimicrobial activity. Group: Enzymes. Synonyms: 9-divinyl ether synthase; 9-DES; CYP74D; CYP74D1; CYP74 cytochrome P-450; DES1; (8E)-9-[(1E,3E)-nona-1,3-dien-1-yloxy]non-8-enoate synthase. Enzyme Commission Number: EC 4.2.1.121. 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-4962; colneleate synthase; EC 4.2.1.121; 9-divinyl ether synthase; 9-DES; CYP74D; CYP74D1; CYP74 cytochrome P-450; DES1; (8E)-9-[(1E,3E)-nona-1,3-dien-1-yloxy]non-8-enoate synthase. Cat No: EXWM-4962. | |
| Creatinase from Pseudomonas sp., Recombinant | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O<-> sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Recombinant, expressed in e. coli, lyophilized powder, 10-15 units/mg protein. Applications: Creatine amidinohydrolase is a clinically important enzyme used in the determination of creatinine in blood and urine. Group: Enzymes. Synonyms: Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Activity: 10-20 units/mg protein. Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Pseudomonas sp. Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Cat No: NATE-0162. | |
| Cystathionine β-lyase, Recombinant | In enzymology, a cystathionine beta-lyase (EC 4.4.1.8) is an enzyme that catalyzes the chemical reaction: L-cystathionine + H2O ? L-homocysteine + NH3 + pyruvate. Thus, the two substrates of this enzyme are L-cystathionine and H2O, whereas its 3 products are L-homocysteine, NH3, and pyruvate. This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. Applications: This protein can be used for producing hcy in vitro diagnosis kit. Group: Enzymes. Synonyms: L-cystathionineL-homocysteine-lyase (deaminating; pyruvate-forming); beta-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionineL-homoc. Enzyme Commission Number: EC 4.4.1.8. Purity: >90% (by SDS-PAGE). Mole weight: 43KD. Activity: >500U/mg. Appearance: Lyophilized powder. Storage: The lyophilized powder should be stored at -20°C where it is stable for up to several years. The solution could be stored at 4°C where it is stable for up to 1 year. Repeated freezing and thawing cycles of the reconstituted solution is not recommended. Form: Freeze dried powder. L-cystathionineL-homocysteine-lyase (deaminating; pyruvate-forming); beta-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionineL-homocysteine-lyase (deaminating); Cystathionine β-lyase; EC 4.4.1.8. Cat No: NATE-1146. | |
| cysteamine dioxygenase | A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates. Group: Enzymes. Synonyms: persulfurase; cysteamine oxygenase;cysteamine:oxygen oxidoreductase. Enzyme Commission Number: EC 1.13.11.19. CAS No. 9033-41-4. 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-0538; cysteamine dioxygenase; EC 1.13.11.19; 9033-41-4; persulfurase; cysteamine oxygenase;cysteamine:oxygen oxidoreductase. Cat No: EXWM-0538. | |
| D-amino acid oxidase from Human, Recombinant | D-amino-acid oxidase (DAAO) is a peroxisomal enzyme which uses flavin adenine dinucleotide (FAD) as a cofactor and oxidizes D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. Its substrates include a wide variety of D-amino acids, but it is inactive on the naturally occurring L-amino acids. It has been suggested that it is involved in acid base balance in the kidney or it could act as a detoxifying agent which removes D-amino acids accumulated during aging. Recombinant human daao protein, fused to his-tag at n-terminus, was expressed in e.coli and purified by using conventional chromatography. Group: Enzymes. Synonyms: DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase. Enzyme Commission Number: EC 1.4.3.3. Purity: > 90% by SDS-PAGE. DAAO. Mole weight: 41.6 kDa. Activity: > 3.5 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli. Species: Human. DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase. Cat No: NATE-1653. | |
| D-aspartate ligase | This enzyme forms part of the peptidoglycan assembly pathway of Gram-positive bacteria grown in medium containing D-Asp. Normally, the side chains the acylate the 6-amino group of the L-lysine residue contain L-Ala-L-Ala but these amino acids are replaced by D-Asp when D-Asp is included in the medium. Hybrid chains containing L-Ala-D-Asp, L-Ala-L-Ala-D-Asp or D-Asp-L-Ala are not formed. The enzyme belongs in the ATP-grasp protein superfamily. The enzyme is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malic acid are not substrates. In Enterococcus faecium, the substrate D-aspartate is produced by EC 5.1.1.13, aspartate racemase. Group: Enzymes. Synonyms: Aslfm; UDP-MurNAc-pentapeptide:D-aspartate ligase; D-aspartic acid-activating enzyme. Enzyme Commission Number: EC 6.3.1.12. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5715; D-aspartate ligase; EC 6.3.1.12; Aslfm; UDP-MurNAc-pentapeptide:D-aspartate ligase; D-aspartic acid-activating enzyme. Cat No: EXWM-5715. | |
| D-dopachrome decarboxylase | This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-α-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase). Group: Enzymes. Synonyms: phenylpyruvate tautomerase II; D-tautomerase;D-dopachrome tautomerase; D-dopachrome carboxy-lyase. Enzyme Commission Number: EC 4.1.1.84. CAS No. 184111-06-6. 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-4833; D-dopachrome decarboxylase; EC 4.1.1.84; 184111-06-6; phenylpyruvate tautomerase II; D-tautomerase;D-dopachrome tautomerase; D-dopachrome carboxy-lyase. Cat No: EXWM-4833. | |
| diaminobutyrate decarboxylase | A pyridoxal-phosphate protein that requires a divalent cation for activity. N4-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate-2-oxoglutarate transaminase, which can supply the substrate for this enzyme. Group: Enzymes. Synonyms: DABA DC; L-2,4-diaminobutyrate decarboxylase; L-2,4-diaminobutanoate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.86. 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-4835; diaminobutyrate decarboxylase; EC 4.1.1.86; DABA DC; L-2,4-diaminobutyrate decarboxylase; L-2,4-diaminobutanoate carboxy-lyase. Cat No: EXWM-4835. | |
| D-Lactate dehydrogenase from Bacteria, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Mole weight: 44 kD (SDS-PAGE). Activity: > 800 U/mg Protein. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-1042. | |
| D-lactate Dehydrogenase from E. coli, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This protein is fused with 6x his tag at n terminus and the protein has a calculated mw of 39.1 kda (353aa). Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c . Enzyme Commission Number: EC 1.1.1.28. Purity: > 95% by SDS-PAGE. D-LDH. Mole weight: 39.1 kDa. Activity: > 200 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D- (-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D- (-)-lactic cytochrome c reductase; D-lactate Dehydrogenase. Cat No: NATE-1654. | |
| (E3-independent) E2 ubiquitin-conjugating enzyme | The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed. Group: Enzymes. Synonyms: E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Enzyme Commission Number: EC 2.3.2.24. 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-2298; (E3-independent) E2 ubiquitin-conjugating enzyme; EC 2.3.2.24; E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Cat No: EXWM-2298. | |
| Elastase, Human leukocytes | Elastase, Human leukocytes is a serine protease present in the nitrogen-loving granules of neutrophils. Elastase, Human leukocytes potential substrates include almost all components of the extracellular matrix, as well as a variety of proteins such as coagulation factors, complement, immunoglobulins and cytokines. It has a strong proteolytic function and participates in the pathogenesis of inflammatory tissue damage [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9004-6-2. Pack Sizes: 1 U. Product ID: HY-P2751. | |
| enoyl-[acyl-carrier-protein] reductase (NADH) | The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. Group: Enzymes. Synonyms: enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name). Enzyme Commission Number: EC 1.3.1.9. CAS No. 37251-08-4. 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-1359; enoyl-[acyl-carrier-protein] reductase (NADH); EC 1.3.1.9; 37251-08-4; enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name). Cat No: EXWM-1359. | |
| Enzyme blend for short-chain protein | For using on most protein-based substrates for the production of non-bitter, short-chain protein hydrolysates with reduced viscosity, improved solubility, flavor, nutritional, and emulsifying characteristics. Applications: Meat & fish proteins. Group: Enzymes. Enzyme for short-chain protein. Appearance: powder or liquid. hydrolysates enzyme; Meat & Fish Proteins enzyme; non-bitter enzyme; short-chain protein hydrolysates enzyme; improved solubility; flavor enzyme; Enzyme blend for short-chain protein; Fish Proteins; fish; Meat; PRO-1821. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1821. | |
| ERK Inhibitor | ERK inhibitor, a reversible thiazolidinedione compound, is a cell-permeable inhibitor that binds ERK2 near its docking domain with a KD of 5 μM and prevents its interaction with protein substrates. Synonyms: Extracellular Regulated Kinase Inhibitor; 3-(2-aminoethyl)-5-[(4-ethoxyphenyl)methylene]-2,4-thiazolidinedione, monohydrochloride. Grades: ≥95%. CAS No. 1049738-54-6. Molecular formula: C14H16N2O3S·HCl. Mole weight: 328.8. | |
| fatty-acid peroxygenase | A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction. Group: Enzymes. Synonyms: fatty acid hydroxylase (ambiguous); P450 peroxygenase; CYP152A1; P450BS; P450SP&alpha. Enzyme Commission Number: EC 1.11.2.4. 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-0515; fatty-acid peroxygenase; EC 1.11.2.4; fatty acid hydroxylase (ambiguous); P450 peroxygenase; CYP152A1; P450BS; P450SP&alpha. Cat No: EXWM-0515. | |
| FMN Reductase from Escherichia coli (Fre), Recombinant | E.coli. Applications: Bacterial (e. coli) nad(p)h-dependent fmn-oxidoreductase is a recombinant protein of ca. 26kda overexpressed in e.coli. the sequence of cloned fre (swissprot accession number p0aen1) was confirmed by dna sequencing (100% identity). Group: Enzymes. Synonyms: NAD(P)H:flavin oxidoreduct. Enzyme Commission Number: EC 1.5.1.29. Mole weight: 26kDa. Activity: >2U/mg. Appearance: Coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for thequantification of NADH and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol,oxaloacetate). Although FMN-reductase often present in luciferase enzyme preparations may be sufficient for producing light in the presence of NAD(P)H, highly purified and characterized Fre enzyme can offer some advantages such as an increased sensitivity,better control of the signal intensity and duration, and saving of the luciferase enzyme. Species: FMN Reductase. NAD(P)H:flavin oxidoreductase; NAD(P)H:flavin mono-nucleotide oxidoreductase; NAD(P)H(2):FMN oxidoreductase; NAD(P)H-FMN reductase; NAD(P)H-dependent FMN reductase; NAD(P)H:FMN oxidoreductase; riboflavin mononucleotide reductase; flavin mononucleotide reductase; EC 1.5.1.29. Pack: stable lyophilized form. Cat No: NATE-1744. | |
| Furamidine dihydrochloride | Furamidine dihydrochloride (DB75 dihydrochloride) is a selective protein arginine methyltransferase 1 (PRMT1) inhibitor with an IC 50 of 9.4 μM. Furamidine dihydrochloride is selective for PRMT1 over PRMT5, PRMT6, and PRMT4 (CARM1) (IC 50 s of 166 μM, 283 μM, and >400 μM, respectively). Furamidine dihydrochloride is a potent, reversible and competitive tyrosyl-DNA phosphodiesterase 1 (TDP-1) inhibitor. Inhibition of TDP-1 by Furamidine dihydrochloride is effective both with single- and double-stranded DNA substrates but is slightly stronger with the duplex DNA. Furamidine dihydrochloride is also an antiparasite agent [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: DB75 dihydrochloride; NSC 305831 dihydrochloride. CAS No. 55368-40-6. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-110137. | |
| Furin from Human, Recombinant | Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It has a molecular mass of 52.7 kDa. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin cleaves precursor proteins at their paired basic amino acid processing sites. Some substrates of furin include von Willebrand factor, transforming growth factor beta 1 precursor, pro-beta-secretase and proparathyroid hormo...terial exotoxins, typically at sites marked by the consensus sequence arg-xaa-(lys/arg)-arg. Group: Enzymes. Synonyms: furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Furin. Activity: > 2,000 unit/mL. Storage: -70°C. Form: buffered aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Cat No: NATE-0268. | |
| galactan endo-1,6-β-galactosidase | The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals.1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death. Group: Enzymes. Synonyms: endo-1,6-β-galactanase. Enzyme Commission Number: EC 3.2.1.164. 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-3846; galactan endo-1,6-β-galactosidase; EC 3.2.1.164; endo-1,6-β-galactanase. Cat No: EXWM-3846. | |
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