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1,3-Diphenyl-4,5-dihydro-1H-pyrazole is a heterocyclic compound belonging to the pyrazole family. It is an organic compound composed of two phenyl rings, a nitrogen atom and a hydrogen atom. Pyrazoles are known for their versatile properties, which makes them useful in a wide range of applications. DPDP is of particular interest due to its potential applications in scientific and medical research. Uses: 1,3-diphenyl-4,5-dihydro-1h-pyrazole is a versatile compound that can be used in a variety of scientific research applications. it has been used as a ligand for the binding of metal ions, such as copper, zinc, and iron, in order to study the structure and function of metalloproteins. it has also been used as a fluorescent probe for the study of enzyme kinetics, as well as for the detection of reac. Additional or Alternative Names: 1,3-Diphenylpyrazoline, 1,3-Diphenyl-2-pyrazoline, 2-Pyrazoline, 1,3-diphenyl-, MLS000717825, 1,3-Diphenyl-4,5-dihydro-1H-pyrazole, MolPort-001-631-521, NSC186211, NSC625226, AIDS132054, AIDS-132054, 1,3-Diphenyl-.DELTA.2-pyrazoline, CID302304, ZINC04142401, 1H-Pyrazole, 4,5-dihydro-1,3-diphenyl-, BAS 00363868, SMR000279193, AE-848/30721014, A0944/0044214, 2538-52-5. Product Category: Heterocyclic Organic Compound. CAS No. 2538-52-5. Molecular formula: C15H14N2. Mole weight: 222.2851. Purity: 0.96. IUPACName: 2,5-diphenyl-3,4-dihydropyrazole. Canonical SMILES: C1CN(N=C1C2=CC=
1-pyrroline-4-hydroxy-2-carboxylate deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). This enzyme is also called HPC deaminase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: HPC deaminase; 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). Enzyme Commission Number: EC 3.5.4.22. CAS No. 9054-77-7. 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-4549; 1-pyrroline-4-hydroxy-2-carboxylate deaminase; EC 3.5.4.22; 9054-77-7; HPC deaminase; 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). Cat No: EXWM-4549.
3,8-divinyl chlorophyllide a reductase
The enzyme, found only in bacteriochlorophyll b-producing bacteria, catalyses the introduction of a C-8 ethylidene group. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase. It is very similar to EC 1.3.7.15, chlorophyllide a reductase, and is composed of three subunits. Two of them form the catalytic component, while the third one functions as an ATP-dependent reductase component that catalyses the electron transfer from ferredoxin to the catalytic component. Group: Enzymes. Enzyme Commission Number: EC 1.3.7.14. 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-1395; 3,8-divinyl chlorophyllide a reductase; EC 1.3.7.14. Cat No: EXWM-1395.
4-Amino-1,8-naphthalimide
The poly(ADP-ribose) polymerases (PARPs) form a family of enzymes with roles in DNA repair and apoptosis, particularly in response to reactive oxygen and nitrogen species. 4-Amino-1,8-naphthalimide (4-ANI) is an inhibitor of PARP (IC50 = 180 nM). Synonyms: 4-Aminonaphthalimide; 4-ANI; 6-aminobenzo[de]isoquinoline-1,3-dione. Grades: ≥95%. CAS No. 1742-95-6. Molecular formula: C12H8N2O2. Mole weight: 212.2.
4-(dimethylamino)phenylazoxybenzene reductase
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: N,N-dimethyl-p-aminoazobenzene oxide reductase; dimethylaminoazobenzene N-oxide reductase; NADPH-dependent DMAB N-oxide reductase; NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase. Enzyme Commission Number: EC 1.7.1.11. CAS No. 103843-39-6. 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-1604; 4-(dimethylamino)phenylazoxybenzene reductase; EC 1.7.1.11; 103843-39-6; N,N-dimethyl-p-aminoazobenzene oxide reductase; dimethylaminoazobenzene N-oxide reductase; NADPH-dependent DMAB N-oxide reductase; NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase. Cat No: EXWM-1604.
4-methyleneglutaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-methylene-L-glutamine amidohydrolase. Other names in common use include 4-methyleneglutamine deamidase, and 4-methyleneglutamine amidohydrolase. This enzyme participates in c5-branched dibasic acid metabolism. Group: Enzymes. Synonyms: 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase. Enzyme Commission Number: EC 3.5.1.67. CAS No. 86855-36-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4457; 4-methyleneglutaminase; EC 3.5.1.67; 86855-36-9; 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase. Cat No: EXWM-4457.
5-formyltetrahydrofolate cyclo-ligase
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. This enzyme participates in one carbon pool by folate. Group: Enzymes. Synonyms: 5,10-methenyltetrahydrofolate synthetase; formyltetrahydrofolic cyclodehydrase; 5-formyltetrahydrofolate cyclodehydrase. Enzyme Commission Number: EC 6.3.3.2. CAS No. 37318-64-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5774; 5-formyltetrahydrofolate cyclo-ligase; EC 6.3.3.2; 37318-64-2; 5,10-methenyltetrahydrofolate synthetase; formyltetrahydrofolic cyclodehydrase; 5-formyltetrahydrofolate cyclodehydrase. Cat No: EXWM-5774.
5-Hydroxymethylcytidine
5-Hydroxymethylcytosine is a DNA pyrimidine nitrogen base. It is formed from the DNA base cytosine by adding a methyl group and then a hydroxy group. It is important in epigenetics, because the hydroxymethyl group on the cytosine can possibly switch a gene on and off. It was first seen in bacteriophages in 1952.[1][2] However, in 2009 it was found to be abundant in human and mouse brains,[3] as well as in embryonic stem cells.[4] In mammals, it can be generated by oxidation of 5-methylcytosine, a reaction mediated by the Tet family of enzymes. 5-Hydroxymethylcytidine is a product in DNA hydroxymethylation. The concentrations of 5-Hydroxymethylcytidine in the brain were used to study Alzheimers disease. Group: Biochemicals. Grades: Highly Purified. CAS No. 19235-17-7. Pack Sizes: 25mg. US Biological Life Sciences.
Worldwide
5-oxoprolinase (ATP-hydrolysing)
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in glutathione metabolism. Group: Enzymes. Synonyms: pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase. Enzyme Commission Number: EC 3.5.2.9. CAS No. 9075-46-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4510; 5-oxoprolinase (ATP-hydrolysing); EC 3.5.2.9; 9075-46-1; pyroglutamase (ATP-hydrolysing); oxoprolinase; pyroglutamase; 5-oxoprolinase; pyroglutamate hydrolase; pyroglutamic hydrolase; L-pyroglutamate hydrolase; 5-oxo-L-prolinase; pyroglutamase. Cat No: EXWM-4510.
acetylindoxyl oxidase
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is N-acetylindoxyl:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism. Group: Enzymes. Enzyme Commission Number: EC 1.7.3.2. CAS No. 9029-37-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1625; acetylindoxyl oxidase; EC 1.7.3.2; 9029-37-2. Cat No: EXWM-1625.
aculeacin-A deacylase
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase. Group: Enzymes. Synonyms: aculeacin A acylase. Enzyme Commission Number: EC 3.5.1.70. CAS No. 121479-50-3. 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-4461; aculeacin-A deacylase; EC 3.5.1.70; 121479-50-3; aculeacin A acylase. Cat No: EXWM-4461.
Acylase I from Aspergillus sp., Immobilized on Eupergit C
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 50 U/g moist material. Storage: 2-8°C. Source: Aspergillus sp. 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 acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0030.
acyl-lysine deacylase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acyl-L-lysine amidohydrolase. Other names in common use include epsilon-lysine acylase, and 6-N-acyl-L-lysine amidohydrolase. This enzyme participates in lysine degradation. Group: Enzymes. Synonyms: ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Enzyme Commission Number: EC 3.5.1.17. CAS No. 9025-11-0. 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-4406; acyl-lysine deacylase; EC 3.5.1.17; 9025-11-0; ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase. Cat No: EXWM-4406.
adenine deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase, and ADase. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: adenase; adenine aminase; ADase. Enzyme Commission Number: EC 3.5.4.2. CAS No. 9027-68-3. 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-4546; adenine deaminase; EC 3.5.4.2; 9027-68-3; adenase; adenine aminase; ADase. Cat No: EXWM-4546.
ADP deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. Group: Enzymes. Synonyms: adenosine diphosphate deaminase; adenosinepyrophosphate deaminase. Enzyme Commission Number: EC 3.5.4.7. CAS No. 9027-79-6. 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-4575; ADP deaminase; EC 3.5.4.7; 9027-79-6; adenosine diphosphate deaminase; adenosinepyrophosphate deaminase. Cat No: EXWM-4575.
ADP-ribosyl-[dinitrogen reductase] hydrolase
The enzyme restores the activity of EC 1.18.6.1, nitrogenase, by catalysing the removal of ADP-ribose from an arginine residue of the dinitrogenase reductase component of nitrogenase. This activity occurs only when the nitrogenase product, ammonium, is not available. The combined activity of this enzyme and EC 2.4.2.37, NAD+-dinitrogen-reductase ADP-D-ribosyltransferase, controls the level of activity of nitrogenase. Group: Enzymes. Synonyms: azoferredoxin glycosidase; azoferredoxin-activating enzymes; dinitrogenase reductase-activating glycohydrolase; ADP-ribosyl glycohydrolase; draG (gene name). Enzyme Commission Number: EC 3.2.2.24. CAS No. 125626-63-3. 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-3978; ADP-ribosyl-[dinitrogen reductase] hydrolase; EC 3.2.2.24; 125626-63-3; azoferredoxin glycosidase; azoferredoxin-activating enzymes; dinitrogenase reductase-activating glycohydrolase; ADP-ribosyl glycohydrolase; draG (gene name). Cat No: EXWM-3978.
agmatinase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine amidinohydrolase. Other names in common use include agmatine ureohydrolase, and SpeB. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: agmatine ureohydrolase; SpeB. Enzyme Commission Number: EC 3.5.3.11. CAS No. 37289-16-0. 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-4513; agmatinase; EC 3.5.3.11; 37289-16-0; agmatine ureohydrolase; SpeB. Cat No: EXWM-4513.
Alanine-Valine Aminotransferase (Crude Enzyme)
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Group: Enzymes. Synonyms: valine--isoleucine transaminase; valine-3-methyl-2-oxovalerate aminotransferase; alanine-valine transaminase; valine-2-keto-methylvalerate aminotransferase; valine-isoleucine aminotransferase. Enzyme Commission Number: EC 2.6.1.32. CAS No. 9023-14-7. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. valine--isoleucine transaminase; valine-3-methyl-2-oxovalerate aminotransferase; alanine-valine transaminase; valine-2-keto-methylvalerate aminotransferase; valine-isoleucine aminotransferase. Pack: 100ml. Cat No: NATE-1820.
allantoate deiminase
This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese. Group: Enzymes. Synonyms: allantoate amidohydrolase. Enzyme Commission Number: EC 3.5.3.9. CAS No. 37289-13-7. 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-4535; allantoate deiminase; EC 3.5.3.9; 37289-13-7; allantoate amidohydrolase. Cat No: EXWM-4535.
allantoinase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is (S)-allantoin amidohydrolase. This enzyme participates in purine metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.2.5. CAS No. 9025-20-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4507; allantoinase; EC 3.5.2.5; 9025-20-1. Cat No: EXWM-4507.
amidase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation. Group: Enzymes. Synonyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. 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-4428; amidase; EC 3.5.1.4; 9012-56-0; acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Cat No: EXWM-4428.
Amidase from Pseudomonas aeruginosa, Recombinant
The amidase from Pseudomonas aeruginosa catalyzes the hydrolysis of a small range of short aliphatic amides. Each amidase monomer is formed by a globular four-layer αββα sandwich domain with an additional 81-residue long C-terminal segment. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Applications: The importance of these hydrolases in biotechnology is growing rapidly, because their potential applications span through chemical and pharmaceutical industries as well as in bioremediation. immobilized amidase can be used efficiently for production of ac...onyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. Activity: >200 units/mg protein (biuret). Storage: Store at -20°C. Form: Solution in 50% glycerol containing 7 mM 2-mercaptoethanol and phosphate buffer salt. Source: E. coli. Species: Pseudomonas aeruginosa. acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Cat No: NATE-0809.
AminoAcylase (Industry grade)
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. Purity: 0.98. ACY1. Storage: at -4-25°C, dry, dark conditions for 3 years. Form: Lyophilized powder. 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 acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1620.
Arginine Deiminase (Crude Enzyme)
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; medicine; pharmacology. Group: Enzymes. Synonyms: arginine dihydrolase; citrulline iminase; L-arginine deiminase. Enzyme Commission Number: EC 3.5.3.6. CAS No. 9027-98-9. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. arginine dihydrolase; citrulline iminase; L-arginine deiminase. Pack: 100ml. Cat No: NATE-1841.
arginine kinase
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: arginine phosphokinase; adenosine 5'-triphosphate: L-arginine phosphotransferase; adenosine 5'-triphosphate-arginine phosphotransferase; ATP:L-arginine N-phosphotransferasel ATP:L-arginine ω-N-phosphotransferase. Enzyme Commission Number: EC 2.7.3.3. CAS No. 9026-70-4. 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-3183; arginine kinase; EC 2.7.3.3; 9026-70-4; arginine phosphokinase; adenosine 5'-triphosphate: L-arginine phosphotransferase; adenosine 5'-triphosphate-arginine phosphotransferase; ATP:L-arginine N-phosphotransferasel ATP:L-arginine ω-N-phosphotransferase. Cat No: EXWM-3183.
aspartate-ammonia ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases).This enzyme participates in 3 metabolic pathways: alanine and aspartate metabolism, cyanoamino acid metabolism, and nitrogen metabolism. Group: Enzymes. Synonyms: asparagine synthetase; L-asparagine synthetase. Enzyme Commission Number: EC 6.3.1.1. CAS No. 9023-69-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5712; aspartate-ammonia ligase; EC 6.3.1.1; 9023-69-2; asparagine synthetase; L-asparagine synthetase. Cat No: EXWM-5712.
aspartate-ammonia ligase (ADP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). This enzyme participates in nitrogen metabolism. Group: Enzymes. Synonyms: asparagine synthetase (ADP-forming); asparagine synthetase (adenosine diphosphate-forming). Enzyme Commission Number: EC 6.3.1.4. CAS No. 37318-61-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5724; aspartate-ammonia ligase (ADP-forming); EC 6.3.1.4; 37318-61-9; asparagine synthetase (ADP-forming); asparagine synthetase (adenosine diphosphate-forming). Cat No: EXWM-5724.
aspartate ammonia-lyase
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. Group: Enzymes. Synonyms: aspartase; fumaric aminase; L-aspartase; L-aspartate ammonia-lyase. Enzyme Commission Number: EC 4.3.1.1. CAS No. 9027-30-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5270; aspartate ammonia-lyase; EC 4.3.1.1; 9027-30-9; aspartase; fumaric aminase; L-aspartase; L-aspartate ammonia-lyase. Cat No: EXWM-5270.
ATP deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. Group: Enzymes. Synonyms: adenosine triphosphate deaminase. Enzyme Commission Number: EC 3.5.4.18. CAS No. 37289-21-7. 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-4544; ATP deaminase; EC 3.5.4.18; 37289-21-7; adenosine triphosphate deaminase. Cat No: EXWM-4544.
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.
Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme)
GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859.
biotin-[acetyl-CoA-carboxylase] ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in biotin metabolism. This protein may use the morpheein model of allosteric regulation. Group: Enzymes. Synonyms: biotin-[acetyl-CoA carboxylase] synthetase; biotin-[acetyl coenzyme A carboxylase] synthetase; acetyl coenzyme A holocarboxylase synthetase; acetyl CoA holocarboxylase synthetase; biotin:apocarboxylase ligase; Biotin holoenzyme synthetase; HCS. Enzyme Commission Number: EC 6.3.4.15. CAS No. 37340-95-7. 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-5784; biotin-[acetyl-CoA-carboxylase] ligase; EC 6.3.4.15; 37340-95-7; biotin-[acetyl-CoA carboxylase] synthetase; biotin-[acetyl coenzyme A carboxylase] synthetase; acetyl coenzyme A holocarboxylase synthetase; acetyl CoA holocarboxylase synthetase; biotin:apocarboxylase ligase; Biotin holoenzyme synthetase; HCS. Cat No: EXWM-5784.
biotin carboxylase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in fatty acid biosynthesis. Group: Enzymes. Synonyms: biotin carboxylase (component of acetyl CoA carboxylase). Enzyme Commission Number: EC 6.3.4.14. CAS No. 9075-71-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5783; biotin carboxylase; EC 6.3.4.14; 9075-71-2; biotin carboxylase (component of acetyl CoA carboxylase). Cat No: EXWM-5783.
biotin-[methylcrotonoyl-CoA-carboxylase] ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in biotin metabolism. Group: Enzymes. Synonyms: biotin-[methylcrotonoyl-CoA-carboxylase] synthetase; biotin-β-methylcrotonyl coenzyme A carboxylase synthetase; β-methylcrotonyl coenzyme A holocarboxylase synthetase; holocarboxylase-synthetase. Enzyme Commission Number: EC 6.3.4.11. CAS No. 37318-68-6. 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-5780; biotin-[methylcrotonoyl-CoA-carboxylase] ligase; EC 6.3.4.11; 37318-68-6; biotin-[methylcrotonoyl-CoA-carboxylase] synthetase; biotin-β-methylcrotonyl coenzyme A carboxylase synthetase; β-methylcrotonyl coenzyme A holocarboxylase synthetase; holocarboxylase-synthetase. Cat No: EXWM-5780.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in biotin metabolism. Group: Enzymes. Synonyms: biotin-[methylmalonyl-CoA-carboxyltransferase] synthetase; biotin-methylmalonyl coenzyme A carboxyltransferase synthetase; biotin-transcarboxylase synthetase; methylmalonyl coenzyme A holotranscarboxylase synthetase; biotin-[methylmalonyl-CoA-carboxyltransferase] ligase; biotin:apo[methylmalonyl-CoA:pyruvate carboxyltransferase] ligase (AMP-forming). Enzyme Commission Number: EC 6.3.4.9. CAS No. 37318-66-4. 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-5801; biotin-[methylmalonyl-CoA-carboxytransferase] ligase; EC 6.3.4.9; 37318-66-4; biotin-[methylmalonyl-CoA-carboxyltransferase] synthetase; biotin-methylmalonyl coenzyme A carboxyltransferase synthetase; biotin-transcarboxylase synthetase; methylmalonyl coenzyme A holotranscarboxylase synthetase; biotin-[methylmalonyl-CoA-carboxyltransferase] ligase; biotin:apo[methylmalonyl-CoA:pyruvate carboxyltransferase] ligase (AMP-forming). Cat No: EXWM-5801.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in biotin metabolism. Group: Enzymes. Synonyms: biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase; biotin-propionyl coenzyme A carboxylase synthetase; propionyl coenzyme A holocarboxylase synthetase. Enzyme Commission Number: EC 6.3.4.10. CAS No. 37318-67-5. 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-5779; biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase; EC 6.3.4.10; 37318-67-5; biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase; biotin-propionyl coenzyme A carboxylase synthetase; propionyl coenzyme A holocarboxylase synthetase. Cat No: EXWM-5779.
biuret amidohydrolase
Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.54 (allophanate hydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria.Urea-1-carboxylate rather than urea (as was thought previously) is the 2-nitrogen intermediate in cyanuric-acid metabolism in bacteria. The product, urea-1-carboxylate,can spontaneously decarboxylate under acidic conditions to form urea but, under physiological conditions, it can be converted into CO2 and ammonia by the action of EC 3.5.1.54. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.84. CAS No. 95567-88-7. 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-4475; biuret amidohydrolase; EC 3.5.1.84; 95567-88-7. Cat No: EXWM-4475.
carbamate kinase
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:carbamate phosphotransferase. Other names in common use include CKase, carbamoyl phosphokinase, and carbamyl phosphokinase. This enzyme participates in 4 metabolic pathways: purine metabolism, glutamate metabolism, arginine and proline metabolism, and nitrogen metabolism. Group: Enzymes. Synonyms: CKase carbamoyl phosphokinase; carbamyl phosphokinase. Enzyme Commission Number: EC 2.7.2.2. CAS No. 9026-69-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3174; carbamate kinase; EC 2.7.2.2; 9026-69-1; CKase carbamoyl phosphokinase; carbamyl phosphokinase. Cat No: EXWM-3174.
(carboxyethyl)arginine β-lactam-synthase
Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It has been proposed that L-N2-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the β-lactam ring is then formed by the intramolecular attack of the β-nitrogen on the activated carboxy group. Group: Enzymes. Synonyms: L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). Enzyme Commission Number: EC 6.3.3.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5776; (carboxyethyl)arginine β-lactam-synthase; EC 6.3.3.4; L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). Cat No: EXWM-5776.
carboxymethylhydantoinase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. Group: Enzymes. Synonyms: hydantoin hydrolase. Enzyme Commission Number: EC 3.5.2.4. CAS No. 9025-14-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4506; carboxymethylhydantoinase; EC 3.5.2.4; 9025-14-3; hydantoin hydrolase. Cat No: EXWM-4506.
Chicking biddy feed enzymes
It is developed according to the digestive physiology of chicks and typical diets. The results of experiments showed that the products could not only effectively supplement the digestive enzyme of chicks, but also inhibited the proliferation of pathogen, improved the health condition of chick, and then enhanced feed utilization ratio. Thus the growth rate was increased uniformly. Ingredients: Protease, amylase, lipase, xylanase, β-mannanase, α-galactosidase. Applications: 1. make up inadequate secretion of endogenous enzyme of chicks to improve animal feed intake and feed efficiency; 2. through inhibiting the proliferation of harmful microorganisms, to improve chick growth rate and colony homogeneity; 3. increase their survival rate by enhancing disease resistance of chicks; 4. by means of breaking down anti-nutritional factors in feed, to improve digestion and absorption of the dietary energy and protein; 5. it can reduce excretion of nitrogen and phosphorus, to reduce environmental pollution. Group: Enzymes. Synonyms: Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; impro. Chicking biddy feed enzymes. Appearance: pellet. Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; improve chick growth rate; FEED-2329. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2329.
chlorophyllide a reductase
The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin). The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction. Group: Enzymes. Synonyms: bchX (gene name); bchY (gene name); bchZ (gene name); COR. Enzyme Commission Number: EC 1.3.7.15. 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-1396; chlorophyllide a reductase; EC 1.3.7.15; bchX (gene name); bchY (gene name); bchZ (gene name); COR. Cat No: EXWM-1396.
citrullinase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Group: Enzymes. Synonyms: citrulline ureidase; citrulline hydrolase; L-citrulline 5-N-carbamoyldihydrolase. Enzyme Commission Number: EC 3.5.1.20. CAS No. 59088-17-4. 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-4410; citrullinase; EC 3.5.1.20; 59088-17-4; citrulline ureidase; citrulline hydrolase; L-citrulline 5-N-carbamoyldihydrolase. Cat No: EXWM-4410.
cobyrinate a,c-diamide synthase
This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyses the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source. It is proposed that the enzyme first catalyses the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate. The Km for ammonia is substantially higher than that for L-glutamine. Group: Enzymes. Synonyms: cobyrinic acid a,c-diamide synthetase; CbiA. Enzyme Commission Number: EC 6.3.5.11. 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-5804; cobyrinate a,c-diamide synthase; EC 6.3.5.11; cobyrinic acid a,c-diamide synthetase; CbiA. Cat No: EXWM-5804.
creatinase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is creatine amidinohydrolase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. 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-4529; creatinase; EC 3.5.3.3; 37340-58-2. Cat No: EXWM-4529.
Creatinase from E. coli, 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. Group: Enzymes. Synonyms: Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: ca. 80 kDa. Activity: > 15 U/mg. Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: NATE-1241.
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.
Creatine monohydrate
Creatine is a nitrogenous compound that acts as a high-energy reservoir for the rapid regeneration of ATP. Approximately 95% of creatine is found in skeletal muscle, primarily as phosphocreatine. Creatine can be acquired through dietary consumption or formed from L-arginine, glycine, and L-methionine in a multi-step reaction that occurs in the kidneys and liver. Creatine is then transported to muscle tissue. Creatine is also being investigated as a treatment of neuromuscular diseases, where it may aid in neuroprotection and by improving the cellular bioenergetic state. Applications: Involved with rapid atp production primarily in skeletal muscle tissue via the action of creatine kinase(s). Group: Coenzymes. Synonyms: N-Amidinosarcosine monohydrate. CAS No. 6020-87-7. Mole weight: 149.15. Form: Solid. N-Amidinosarcosine monohydrate; Creatine monohydrate; 6020-87-7. Cat No: COEC-096.
creatininase
Creatininase is a member of the urease-related amidohydrolases, the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: creatinine hydrolase. Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. 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-4493; creatininase; EC 3.5.2.10; 9025-13-2; creatinine hydrolase. Cat No: EXWM-4493.
Creatininase, Microorganism
Creatininase, Microorganism (Creatinine amidohydrolase; CAH), namely creatinine amidohydrolase, from Pseudomonas putida , is a homohexameric enzyme commonly used in biochemical research. Creatininase acts on carbon-nitrogen bonds other than peptide bonds, and can catalyze the hydrolysis of creatinine to creatine, which can then be metabolized by creatinase to urea and sarcosine [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Creatinine amidohydrolase; CAH. CAS No. 9025-13-2. Pack Sizes: 1 KU. Product ID: HY-P2838.
creatinine deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Other names in common use include creatinine hydrolase, and creatinine desiminase. This enzyme participates in arginine and proline metabolism. Group: Enzymes. Synonyms: creatinine hydrolase; creatinine desiminase. Enzyme Commission Number: EC 3.5.4.21. CAS No. 37289-15-9. Creatinine Deiminase. 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-4548; creatinine deaminase; EC 3.5.4.21; 37289-15-9; creatinine hydrolase; creatinine desiminase. Cat No: EXWM-4548.
cyanase
This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen. Reaction (1) can be considered as the reverse of 'carbamate = cyanate + H2O', where this is assisted by reaction with bicarbonate and carbon dioxide (see mechanism above), and hence is classified in sub-subclass 4.2.1. Bicarbonate functions as a recycling substrate. Group: Enzymes. Synonyms: cyanate lyase; cyanate hydrolase; cyanate aminohydrolase; cyanate C-N-lyase; cyanate hydratase. Enzyme Commission Number: EC 4.2.1.104. CAS No. 37289-24-0. 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-4943; cyanase; EC 4.2.1.104; 37289-24-0; cyanate lyase; cyanate hydrolase; cyanate aminohydrolase; cyanate C-N-lyase; cyanate hydratase. Cat No: EXWM-4943.
cyanophycin synthase (L-arginine-adding)
Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.29, cyanophycin synthase (L-aspartate-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store. Both enzymes are found in the same protein but have different active sites. Both L-Asp and L-Arg must be present before either enzyme will display significant activity. Canavanine and lysine can be incoporated into the polymer instead of arginine. Group: Enzymes. Synonyms: CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous). Enzyme Commission Number: EC 6.3.2.30. CAS No. 131554-17-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5747; cyanophycin synthase (L-arginine-adding); EC 6.3.2.30; 131554-17-1; CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous). Cat No: EXWM-5747.
cyanophycin synthase (L-aspartate-adding)
Requires Mg2+ for activity. Both this enzyme and EC 6.3.2.30, cyanophycin synthase (L-arginine-adding), are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store. Both enzymes are found in the same protein but have different active sites. Both L-Asp and L-Arg must be present before either enzyme will display significant activity. Group: Enzymes. Synonyms: CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous). Enzyme Commission Number: EC 6.3.2.29. CAS No. 131554-17-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5745; cyanophycin synthase (L-aspartate-adding); EC 6.3.2.29; 131554-17-1; CphA (ambiguous); CphA1 (ambiguous); CphA2 (ambiguous); cyanophycin synthetase (ambiguous); multi-L-arginyl-poly-L-aspartate synthase (ambiguous). Cat No: EXWM-5745.
Cyclohexanone Monooxygenase from Acinetobacter sp., Recombinant
Purified cyclohexanone monooxygenase is a versatile oxygenation catalyst. The enzyme uses the bound FAD-4a-OOH oxygenating intermediate to initiate transfer of oxygen to electrophilic substrate sites. The reaction consequently yields the corresponding sulfoxide and selenoxide products. This enzyme is also capable of oxygenating at nitrogen, trivalent phosphorus, and boron sites in boronic acids. Hence, it is one of the most broad-based flavoprotein oxygenases known. Applications: Cyclohexanone monooxygenase has been used in a study that cloned and overexpressed the 2-oxo-δ(3)-4,5,5-trimethylcyclopentenylacetyl-coa monooxygenase (otemo) in escherichia col....22; 52037-90-8; cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming). Enzyme Commission Number: EC 1.14.13.22. CAS No. 52037-90-8. Cyclohexanone Monooxygenase. Mole weight: 59 kDa. Activity: >12 U/ml. Storage: Store at -20°C. Form: Suspension in 80% saturated ammonium sulfate, 20 mM K-Na-phosphate buffer pH 7, 3.5 mM 1,4-Dithioerythritol (DTE). Source: E. coli. Species: Acinetobacter sp. yclohexanone 1,2-monooxygenase; cyclohexanone oxygenase; cyclohexanone:NADPH:oxygen oxidoreductase (6-hydroxylating, 1,2-lactonizing); cyclohexanone monooxygenase; EC 1.14.13.22; 52037-90-8; cyclohexanone,NADPH:oxygen oxidoreductase (lactone-forming). Cat No: NATE-0822.
cysteine desulfurase
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. Group: Enzymes. Synonyms: IscS; NIFS; NifS; SufS; cysteine desulfurylase. Enzyme Commission Number: EC 2.8.1.7. CAS No. 149371-08-4. 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-3365; cysteine desulfurase; EC 2.8.1.7; 149371-08-4; IscS; NIFS; NifS; SufS; cysteine desulfurylase. Cat No: EXWM-3365.
D-Amino Acid Transaminase (Crude Enzyme)
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Group: Enzymes. Synonyms: D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase; D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Enzyme Commission Number: EC 2.6.1.21. CAS No. 37277-85-3. ALT. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase; D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Pack: 100ml. Cat No: NATE-1819.
D-Asparagine
D-Asparagine (H-D-Asn-OH) is a competitive inhibitor of L-Asparagine hydrolysis with a K i value of 0.24 mM. D-Asparagine is a source of nitrogen for yeast strains. D-Asparagine is a good substrate for the external yeast asparaginase but is a poor substrate for the internal enzyme [1]. Uses: Scientific research. Group: Natural products. Alternative Names: H-D-Asn-OH. CAS No. 2058-58-4. Pack Sizes: 10 mM * 1 mL; 1 g. Product ID: HY-W010378.
D-benzoylarginine-4-nitroanilide amidase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Group: Enzymes. Synonyms: benzoyl-D-arginine arylamidase; D-BAPA-ase. Enzyme Commission Number: EC 3.5.1.72. CAS No. 119345-26-5. 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-4463; D-benzoylarginine-4-nitroanilide amidase; EC 3.5.1.72; 119345-26-5; benzoyl-D-arginine arylamidase; D-BAPA-ase. Cat No: EXWM-4463.
dCTP deaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase. Other names in common use include deoxycytidine triphosphate deaminase, and 5-methyl-dCTP deaminase. This enzyme participates in pyrimidine metabolism. Group: Enzymes. Synonyms: deoxycytidine triphosphate deaminase; 5-methyl-dCTP deaminase. Enzyme Commission Number: EC 3.5.4.13. CAS No. 37289-18-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4540; dCTP deaminase; EC 3.5.4.13; 37289-18-2; deoxycytidine triphosphate deaminase; 5-methyl-dCTP deaminase. Cat No: EXWM-4540.
D-glutaminase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is D-glutamine amidohydrolase. This enzyme participates in d-glutamine and d-glutamate metabolism and nitrogen metabolism. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.35. CAS No. 37289-12-6. 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-4424; D-glutaminase; EC 3.5.1.35; 37289-12-6. Cat No: EXWM-4424.
D-Glutamine tert-Butyl Ester Hydrochloride
D-Glutamine tert-Butyl Ester Hydrochloride is a protected form of D-Glutamine. D-Glutamine is an unnatural isomer of L-Glutamine that is present in human plasma an is a source of liberated ammonia. D-Glutamine can be synthesized by enzymatic means or can be found in cheeses, wine and vinegars as well. It is often used to determine the activity of Glutamine synthetase, an enzyme that is commonly found in the mammalian liver and brain that controls the use of nitrogen in cells. Group: Biochemicals. Alternative Names: D-Glutamine 1,1-Dimethylethyl Ester Hydrochloride; (R)-2-Amino-4-carbamoylbutyric Acid tert-Butyl Ester Hydrochloride. Grades: Highly Purified. CAS No. 422324-35-4. Pack Sizes: 250mg, 500mg, 1g. Molecular Formula: C?H??ClN?O?, Molecular Weight: 238.71. US Biological Life Sciences.
Worldwide
D-Hydantoinase (Crude Enzyme)
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. This enzyme participates in 3 metabolic pathways: pyrimidine metabolism,beta-alanine metabolism, and pantothenate and coa biosynthesis. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; nutrition. Group: Enzymes. Synonyms: hydantoinase; hydropyrimidine hydrase; hydantoin peptidase; pyrimidine hydrase; dihydropyrimidinase. Enzyme Commission Number: EC 3.5.2.2. CAS No. 9030-74-4. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. hydantoinase; hydropyrimidine hydrase; hydantoin peptidase; pyrimidine hydrase; dihydropyrimidinase. Pack: 100ml. Cat No: NATE-1838.
diamine transaminase
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: amine transaminase; amine-ketoacid transaminase; diamine aminotransferase; diamine-ketoglutaric transaminase. Enzyme Commission Number: EC 2.6.1.29. CAS No. 9031-83-8. 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-2868; diamine transaminase; EC 2.6.1.29; 9031-83-8; amine transaminase; amine-ketoacid transaminase; diamine aminotransferase; diamine-ketoglutaric transaminase. Cat No: EXWM-2868.
dihydropyrimidine dehydrogenase (NAD+)
An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus, Pseudomonas strains and Escherichia coli. Group: Enzymes. Synonyms: dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+). Enzyme Commission Number: EC 1.3.1.1. CAS No. 9026-89-5. 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-1270; dihydropyrimidine dehydrogenase (NAD+); EC 1.3.1.1; 9026-89-5; dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+). Cat No: EXWM-1270.
DPQ
DPQ is a potent inhibitor of poly(ADP-ribose) polymerases (PARPs), which is a family of enzymes that plays an important role in DNA repair and apoptosis in response to reactive oxygen and nitrogen species. DPQ inhibits PARP1 with an IC50 value of 40 nM. It is approximately 10-fold less potent against PARP2. Uses: Poly(adp-ribose) polymerase inhibitors. Synonyms: PARP Inhibitor III; 3,4-dihydro-5-[4-(1-piperidinyl)butoxy]-1(2H)-isoquinolinone. Grades: ≥99%. CAS No. 129075-73-6. Molecular formula: C18H26N2O2. Mole weight: 302.4.
Endo-protease
A protease enzyme used to hydrolyze protein to produce free-form amino acids for use as Free-Amino-Nitrogen (FAN).To increase the free amino-nitrogen content when brewing with high levels of raw wheat. Applications: Adding in the beginning of the mash, increasingremarkably the wort extract yield and the free amino-nitrogen content. Group: Enzymes. Synonyms: Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Endo-protease. Appearance: powder or liquid. Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: BRE-1615.
Enzyme blend for enhancing dairy-food flavors
Enzyme complex used to enhance dairy-food flavors by modifiying milk proteins in hard and soft cheeses to yield water-soluble peptides, amino acids and other nitrogen-containing compounds. Applications: Enhance dairy-food flavors. Group: Enzymes. Synonyms: enhancing dairy-food flavors; enhancing dairy-food flavors enzyme; modifiying milk proteins enzyme; Dairy Enzymes; Dairy; Enzyme blend for enhancing dairy-food flavors; DAI-1214. Dairy-food flavors enzymes. Appearance: inquire. enhancing dairy-food flavors; enhancing dairy-food flavors enzyme; modifiying milk proteins enzyme; Dairy Enzymes; Dairy; Enzyme blend for enhancing dairy-food flavors; DAI-1214. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DAI-1214.
Enzyme blend for FAN Production
A glucoamylase and protease combination that produces large amounts of glucose and Free-Amino-Nitrogen for simultaneous fermentation. Applications: Combination saccharification & fan production. Group: Enzymes. Synonyms: FAN Production; glucoamylase and protease combination; Fuel Alcohol; Alcohol and Starch Enzymes; Saccharification; Combination Saccharification; FAN Production Enzymes; glucoamylase; protease. Enzyme blend for FAN Production. Appearance: inquire. FAN Production; glucoamylase and protease combination; Fuel Alcohol; Alcohol and Starch Enzymes; Saccharification; Combination Saccharification; FAN Production Enzymes; glucoamylase; protease. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: ASE-3111.
Enzyme for laying hen
Based on the digestive physiology and typical diets of laying hen, It is developed to enhance the laying rate and average egg weight, keep laying cycle longer, make the egg shell stronger and not easy to be broke, and then improve feed conversion ratio (FCR). Applications: 1. make up the digestive enzyme of laying hen to improve animal feed intake and feed efficiency; 2. by means of breaking down anti-nutritional factors in feed, to improve digestion and absorption of the dietary energy and protein; 3. enhance the laying rate and averaged egg weight, kept laying cycle longer; 4. reducing the differences between different batches of feed, to steady products quality; 5. it can reduce nitrogen and phosphorus excretion, to reduce environmental pollution. Group: Enzymes. Synonyms: Enzyme for laying hen; laying hen; laying rate; Enhance the laying rate; Enhance averaged egg weight; egg weight; laying cycle; kept laying cycle longer; Feed Grade Enzymes; FEED-2331. Enzyme for laying hen. Appearance: pellet. Enzyme for laying hen; laying hen; laying rate; Enhance the laying rate; Enhance averaged egg weight; egg weight; laying cycle; kept laying cycle longer; Feed Grade Enzymes; FEED-2331. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2331.
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