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| Product | Description | |
|---|---|---|
| Native Mammalian Ubiquitin Conjugating Enzyme Fractions | Ubiquitin-conjugating enzymes perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. Applications: Ubiquitin conjugating enzyme fractions mammalian may be used in transferring the activated ubiquitin from e1 to the substrate through an additional high energy thiol ester intermediate e2-s-ubiquitin. ubiquitin-conjugating enzymes, also known as e2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. Group: Enzymes. Synonyms: Ubiquitin con. Ubiquitin Conjugating Enzyme. Storage: -70°C. Source: Mammalian. Ubiquitin conjugating enzymes; Ubiquitin Conjugating Enzyme Fractions; E2 enzymes; ubiquitin-carrier enzymes. Cat No: NATE-0727. |  |
| 17β-estradiol 17-dehydrogenase | The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+. Group: Enzymes. Synonyms: 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Enzyme Commission Number: EC 1.1.1.62. CAS No. 9028-61-9. 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-0348; 17β-estradiol 17-dehydrogenase; EC 1.1.1.62; 9028-61-9; 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Cat No: EXWM-0348. | |
| 1,8-cineole 2-exo-monooxygenase | A heme-thiolate protein (P-450). The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. cf. EC 1.14.13.97 (taurochenodeoxycholate 6-hydroxylase), EC 1.14.13.67 (quinine 3-monooxygenase) and EC 1.14.13.32 (albendazole monooxygenase). Group: Enzymes. Synonyms: CYP3A4. Enzyme Commission Number: EC 1.14.13.157. 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-0757; 1,8-cineole 2-exo-monooxygenase; EC 1.14.13.157; CYP3A4. Cat No: EXWM-0757. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 3α-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3α-hydroxysteroids, such as androsterone and 5 α-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific)]. Group: Enzymes. Synonyms: 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Enzyme Commission Number: EC 1.1.1.357. 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-0273; 3α-hydroxysteroid 3-dehydrogenase; EC 1.1.1.357; 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Cat No: EXWM-0273. | |
| 3β-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase. Group: Enzymes. Synonyms: 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Enzyme Commission Number: EC 1.1.1.270. CAS No. 42616-29-5. 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-0177; 3β-hydroxysteroid 3-dehydrogenase; EC 1.1.1.270; 42616-29-5; 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Cat No: EXWM-0177. | |
| 3-oxo-5α-steroid 4-dehydrogenase (NADP+) | The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor). Group: Enzymes. Synonyms: cholestenone 5α-reductase; testosterone Δ4-5&. Enzyme Commission Number: EC 1.3.1.22. CAS No. 37255-34-8. 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-1297; 3-oxo-5α-steroid 4-dehydrogenase (NADP+); EC 1.3.1.22; 37255-34-8; cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase. Cat No: EXWM-1297. | |
| 4-α-glucanotransferase | This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase). Group: Enzymes. Synonyms: disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Amylomaltase. 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-2479; 4-α-glucanotransferase; EC 2.4.1.25; 9032-09-1; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Cat No: EXWM-2479. | |
| 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside | 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside is a compound widely used in the biomedical industry as an artificial chromogenic substrate. It is primarily employed in the detection and visualization of β-D-glucosidase enzyme activity. This compound finds applications in various biochemical assays, including determination of bacterial and mammalian β-D-glucosidase levels, providing valuable insights into drug discovery and disease research. Synonyms: X-Mannose. CAS No. 129787-67-3. Molecular formula: C14H15BrClNO6. Mole weight: 408.63. |  |
| 6-Chloro-5-(2,3-dichlorophenoxy)-2-methylthio-benzimidazole (Triclabendazole) | Triclabendazole is a member of the benzimidazole family of anthelmintics. It is effective against F. hepatica helminths that cause fascioliasis, reducing secreted protease enzyme activities that are critical for the invasion, migration, nutrition, and survival of the parasite.1 In yeast and mammalian cells, triclabendazole was shown to inhibit adenylyl cyclase in the Ras-adenylyl cyclase-protein kinase A nutrient-sensing pathway and to prevent apoptosis induced by the Parkinsons disease-related protein α-synuclein, demonstrating a protective role during various cellular stresses.2,3. Group: Biochemicals. Alternative Names: 5-Chloro-6- (2, 3-dichlorophenoxy) -2- methyl thiobenzimidazole; CGA-89317, egaten; Fasinex; Triclabendazole. Grades: Highly Purified. CAS No. 68786-66-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C14H9Cl3N2OS, Molecular Weight: 359.66. US Biological Life Sciences. |  Worldwide |
| 7, 12-Dimethylbenz [a]anthracene | A highly potent carcinogen that is activated by microsomal enzymes to a diol epoxide metabolite that binds covalently to DNA in mammalian cells, leading ultimately to tumor induction. Group: Biochemicals. Grades: Highly Purified. CAS No. 57-97-6. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| 8R-Brassicasterol | 8R-Brassicasterol is a by-product in the synthesis of Brassicasterol (B676850). Brassicasterol is a phytosterol found in canola oil, rapeseed oil, marine algae and shellfish. This compound has been shown to inhibit sterol Δ24-reductase, an enzyme involved in the mammalian cholesterol biosynthesis pathway. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C28H46O. US Biological Life Sciences. | Worldwide |
| Abl Kinase Mutant active human, Recombinant | Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9. c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene. Human abelson murine leukemia viral oncogene homolog 1 (abl-1) (genbank accession no. nm_007313), amino acids 248-531 with t334i mutation and n-terminal his-tag, mw = 33 kda, expressed in a baculovirus-infected sf9 cell expression system. Group: Enzymes. Synonyms: ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Abl Kinase. Mole weight: mol wt 33 kDa. Stability: -70°C. Form: aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Cat No: NATE-0013. | |
| ABTS Chromophore Diammonium Salt | ABTS Chromophore Diammonium Salt can inhibit catalase, a mammalian antioxidant enzyme which degrades hydrogen peroxide into water and oxygen species. Synonyms: 2,2'-(1,2-Hydrazinediylidene)bis[3-ethyl-2,3-dihydro-6-benzothiazolesulfonic Acid Ammonium Salt (1:2); 2,2'-Azinobis[3-ethyl-2,3-dihydro-6-benzothiazolesulfonic Acid Diammonium Salt; 3-Ethyl-2-oxo-6-Benzothiazolinesulfonic Acid Azine Diammonium Salt; 2,2'-Azino-bis-(3-ethyl-benzthiazoline-6-sulfonate) Diammonium Salt; 2,2'-Azinobis(3-ethylbenzothiazoline-6-sulfonic acid) Diammonium Salt; ABTS Diammonium Salt; Diammonium 2,2'-Azinobis(3-ethyl-6-benzothiazolinesulfonate); Diammonium 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate). Grades: ≥98%. CAS No. 30931-67-0. Molecular formula: C18H24N6O6S4. Mole weight: 548.68. | |
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. | |
| Adenosine deaminase Bovine, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Protein determined by biuret. Applications: Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays. adenosine deaminase is a potential target for treatments of combined immunodeficiency disease. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 32.5-33 kDa. Activity: 60-130 units/mg protein; > 130 units/mg protein; 150-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0. Source: E. coli. Species: Bovine. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-0032. | |
| Adenosine deaminase from Human, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Applications: Adenosine deaminase (ada) is a key enzyme in purine metabolism and is essential for normal immune function. it is important in the study of immune system diseases such as rheumatoid arthritis. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Activity: >1 U/mL. Storage: Store at -20°C. Source: E. coli. Species: Human. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1583. | |
| Adenosine deaminase, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. Purity: > 90 %. ADA. Mole weight: About 53kDa (SDS-PAGE). Activity: 200U/mg protein. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Source: E. coli. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1009. | |
| α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277. | |
| α(2-3) Neuraminidase from Salmonella typhimurium LT2, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Α2-3 neuraminidase is a highly specific exogl... sialyl linkages and shows only trace activity against α2-8 sialyl linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Neuraminidase. Mole weight: 41 kDa. Activity: ~11,300,000 units/mg. Storage: Store at 4°C or in small aliquots at -20°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), and 5 mM Na2EDTA. Source: E. coli. Species: Salmonella typhimurium LT2. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase. Cat No: NATE-1276. | |
| α(2-3) Neuraminidase S from Streptococcus pneumoniae, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neurami...;2-3 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 74000 daltons. Activity: 160,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM EDTA. Source: E. coli. Species: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase S; α(2-3) Neuraminidase. Cat No: NATE-1275. | |
| α-tubulin N-acetyltransferase | The enzyme from Chlamydomonas flagella also acetylates mammalian brain α-tubulin. Group: Enzymes. Synonyms: α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Enzyme Commission Number: EC 2.3.1.108. CAS No. 99889-90-4. 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-2046; α-tubulin N-acetyltransferase; EC 2.3.1.108; 99889-90-4; α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Cat No: EXWM-2046. | |
| aminopeptidase B | Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Enzyme Commission Number: EC 3.4.11.6. CAS No. 9073-92-1. 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-4027; aminopeptidase B; EC 3.4.11.6; 9073-92-1; arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Cat No: EXWM-4027. | |
| AMPK Signaling Agonist, F17 (4-hydroxy-1-isobutyl-N-(5-methylthiazol-2-yl)-2-oxo-1,2-dihydroquinoline-3-carboxamide) | A cell-permeable 4-hydroxy-2-oxo quinoline carboxamide that acts as an agonist of AMPK signaling. It is shown to reduce fat storage in C. elegans (EC50 ~0.1uM) and reduce the expression level of fat-7 (a C. elegans ortholog of mammalian stearoyl-CoA desaturase-1), through aak-1 (an ortholog for the AMPK-a1 catalytic subunit) and K08F8.2 (a transcription factor) dependent mechanisms. In addition, it markedly reduces the number of lipid droplets in HepG2 human hepatocarcinoma cells at 25uM, and elicits the phosphorylation and inactivation of acetyl coenzyme A carboxylase (ACC, the enzyme that catalyzes the rate-limiting step in de novo fatty acid synthesis). F17-induced ACC phosphorylation can be abrogated by simultaneous treatment with an AMPK inhibitor compound C. Group: Biochemicals. Grades: Highly Purified. CAS No. 280112-24-5. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| aspartyl aminopeptidase | Aminoacyl-arylamides are poor substrates. This is an abundant cytosolic enzyme in mammalian cells, in peptidase family M18 of aminopeptidase I. Group: Enzymes. Enzyme Commission Number: EC 3.4.11.21. CAS No. 9074-83-3. 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-4018; aspartyl aminopeptidase; EC 3.4.11.21; 9074-83-3. Cat No: EXWM-4018. | |
| β-aspartyl-peptidase | Other isopeptide bonds, e.g. γ-glutamyl and β-alanyl, are not hydrolysed. A mammalian, cytosolic enzyme. Group: Enzymes. Synonyms: β-aspartyl dipeptidase; β-aspartyl peptidase; β-aspartyldipeptidase. Enzyme Commission Number: EC 3.4.19.5. CAS No. 37288-74-7. 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-4089; β-aspartyl-peptidase; EC 3.4.19.5; 37288-74-7; β-aspartyl dipeptidase; β-aspartyl peptidase; β-aspartyldipeptidase. Cat No: EXWM-4089. | |
| Brassicasterol-(2,2',3,4,4',6-D6) | Brassicasterol-(2,2',3,4,4',6-D6) is derived from Brassicasterol (B676850), which is a phytosterol found in canola oil, rapeseed oil, marine algae and shellfish. This compound has been shown to inhibit sterol Δ24-reductase, an enzyme involved in the mammalian cholesterol biosynthesis pathway. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1mg, 2.5mg. Molecular Formula: C28H40D6O, Molecular Weight: 404.7. US Biological Life Sciences. | Worldwide |
| carotenoid-9',10'-cleaving dioxygenase | Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene. Group: Enzymes. Synonyms: BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving). Enzyme Commission Number: EC 1.13.11.71. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0591; carotenoid-9',10'-cleaving dioxygenase; EC 1.13.11.71; BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving). Cat No: EXWM-0591. | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| caspase-8 | Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Caspase-8 is the apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. It contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. This enzyme is linked to cell surface death receptors such as Fas. When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. The enzyme has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala, at the P1' position. It has very broad P...ORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Enzyme Commission Number: EC 3.4.22.61. CAS No. 179241-78-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4237; caspase-8; EC 3.4.22.61; 179241-78-2; FLICE, FADD-like ICE; MACH; MORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Cat No: EXWM-4237. | |
| catechol O-methyltransferase | The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols. Group: Enzymes. Synonyms: COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1961; catechol O-methyltransferase; EC 2.1.1.6; 9012-25-3; COMT I COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase. Cat No: EXWM-1961. | |
| cathepsin H | Present in lysosomes of mammalian cells. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin B3; benzoylarginine-naphthylamide (BANA) hydrolase (obsolete); cathepsin Ba, aleurain; N-benzoylarginine-β-naphthylamide hydrolase. Enzyme Commission Number: EC 3.4.22.16. CAS No. 60748-73-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4196; cathepsin H; EC 3.4.22.16; 60748-73-4; cathepsin B3; benzoylarginine-naphthylamide (BANA) hydrolase (obsolete); cathepsin Ba, aleurain; N-benzoylarginine-β-naphthylamide hydrolase. Cat No: EXWM-4196. | |
| cathepsin K | Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin O and cathepsin X (both misleading, having been used for other enzymes); cathepsin O2. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4213; cathepsin K; EC 3.4.22.38; 94716-09-3; cathepsin O and cathepsin X (both misleading, having been used for other enzymes); cathepsin O2. Cat No: EXWM-4213. | |
| cathepsin X | Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13. Group: Enzymes. Synonyms: cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Enzyme Commission Number: EC 3.4.18.1. CAS No. 37217-21-3. 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-4081; cathepsin X; EC 3.4.18.1; 37217-21-3; cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Cat No: EXWM-4081. | |
| CAY10594 | Phospholipase D (PLD) is an enzyme which cleaves the head group from phospholipids, producing the second messenger phosphatidic acid. There are two mammalian isoforms of PLD, which are PLD1 and PLD2. CAY10594 is a potent phospholipase D2 inhibitor (PLD2), which also prevents the invasive migration of breast cancer cells. It ameliorates acetaminophen-induced acute liver injury by regulating the phosphorylated-GSK-3β/JNK axis. Synonyms: CAY 10594; CAY-10594. Grades: ≥98%. CAS No. 1130067-34-3. Molecular formula: C26H28N4O2. Mole weight: 428.5. | |
| CB30865 | CB30865 is a highly potent cytotoxic agent. The compound inhibits isolated mammalian thymidylate synthase (TS), but this inhibition is insufficient to account for its cellular toxicity. Thymidylate synthase (TS) is a critical enzyme in the de novo synthesis of thymidylate (dTTP) and has long been recognized as a target for chemotherapeutic intervention. Synonyms: CB-30865; CB 30865; CB30865; ZM 242421; ZM242421; ZM-242421. Grades: >98%. CAS No. 206275-15-2. Molecular formula: C26H22BrN5O2. Mole weight: 516.39. | |
| cholate-CoA ligase | Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway. Group: Enzymes. Synonyms: BAL; bile acid CoA ligase; bile acid co. Enzyme Commission Number: EC 6.2.1.7. CAS No. 9027-90-1. 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-5709; cholate-CoA ligase; EC 6.2.1.7; 9027-90-1; BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase. Cat No: EXWM-5709. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| Conoidin A | Peroxiredoxins are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels and thereby mediate signal transduction in mammalian cells. Conoidin A inactivates peroxiredoxins by covalently binding to the catalytic cysteine on the enzyme. It has been shown to inhibit peroxiredoxin II (IC50 = 23 μM) in the parasite T. gondii and peroxiredoxin I in the hookworm A. ceylanicum. Synonyms: 2,3-Bis(bromomethyl)quinoxaline 1,4-dioxide. Grades: ≥98%. CAS No. 18080-67-6. Molecular formula: C10H8Br2N2O2. Mole weight: 348. | |
| cyclic GMP-AMP synthase | Cyclic Gp(2'-5')Ap(3'-5') is a signalling molecule in mammalian cells that triggers the production of type I interferons and other cytokines. Group: Enzymes. Synonyms: cGAMP synthase; cGAS. Enzyme Commission Number: EC 2.7.7.86. 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-3299; cyclic GMP-AMP synthase; EC 2.7.7.86; cGAMP synthase; cGAS. Cat No: EXWM-3299. | |
| cytosol alanyl aminopeptidase | A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Enzyme Commission Number: EC 3.4.11.14. CAS No. 243859-94-1. 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-4010; cytosol alanyl aminopeptidase; EC 3.4.11.14; 243859-94-1; arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Cat No: EXWM-4010. | |
| D-2-hydroxyacid dehydrogenase (quinone) | The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors. Group: Enzymes. Synonyms: (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.1.5.10. 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-0428; D-2-hydroxyacid dehydrogenase (quinone); EC 1.1.5.10; (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous). Cat No: EXWM-0428. | |
| DDMS | DDMS is a mechanism-based irreversible inhibitor with a 10-fold selectivity for CYP4A2 enzymes, which are mainly synthesized into 20-hete in mammalian kidneys. Synonyms: Dibromo-dodecenyl-methylsulfimide; 12,12-Dibromo-N-(methylsulfonyl)-11-dodecenamide. Grades: ≥98%. CAS No. 206052-03-1. Molecular formula: C13H23Br2NO3S. Mole weight: 433.2. | |
| 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 |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| dipeptidyl-peptidase IV | A homodimer. An integral protein of the plasma membrane of lymphocytes and other mammalian cells, in peptidase family S9 (prolyl oligopeptidase family). The reaction is similar to that of the unrelated EC 3.4.14.11 Xaa-Pro dipeptidyl-peptidase of lactococci. Group: Enzymes. Synonyms: dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptida. Enzyme Commission Number: EC 3.4.14.5. CAS No. 54249-88-6. DPP IV. 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-4050; dipeptidyl-peptidase IV; EC 3.4.14.5; 54249-88-6; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidyl-aminopeptidase IV; DPP IV/CD26; amino acyl-prolyl dipeptidyl aminopeptidase; T cell triggering molecule Tp103; X-PDAP. Cat No: EXWM-4050. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) | This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH). Group: Enzymes. Synonyms: acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase. Enzyme Commission Number: EC 1.3.1.39. 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-1311; enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific); EC 1.3.1.39; acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific). Cat No: EXWM-1311. | |
| farnesylcysteine lyase | A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine. Group: Enzymes. Synonyms: FC lyase; FCLY. Enzyme Commission Number: EC 1.8.3.6. 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-1663; farnesylcysteine lyase; EC 1.8.3.6; FC lyase; FCLY. Cat No: EXWM-1663. | |
| 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. | |
| Genistein | Cell-permeable, reversible, substrate competitive tyrosine kinase inhibitor (including EGFR phosphorylation), implicated in almost all cell growth and proliferation signal cascades. Inhibitor of mammalian DNA topoisomerase II. Anticancer agent, inducing cell cycle arrest and apoptosis. Antiangiogenic agent, down-regulates the transcription of genes involved in controlling angiogenesis. Binds estrogen receptor beta. Can increase the rate of growth of some ER expressing breast cancers. Potent alpha-glucosidase inhibitor. Anthelmintic. Anti-diabetic. Activates nuclear receptors, oestrogen receptors and peroxisome proliferator-activated receptors (all PPAR isoforms) and it inhibits various enzyme activities. Inhibitor of GLUT4-mediated glucose uptake in 3T3-L1 adipocytes. Stimulator of autophagy vacuolization. Antioxidant. TRAIL sensitizer. Acts as an agonist at the GPR30 receptor. DNA methyltransferase inhibitor. Genistein exhibits synergistic antibacterial effects on MRSA. Group: Biochemicals. Alternative Names: NSC 36586; Baichanin A; Differenol A; 4',5,7-Trihydroxyisoflavone; 5,7-Dihydroxy-3-(4-hydroxyphenyl)-4H-1-benzopyran-4-one. Grades: Highly Purified. CAS No. 446-72-0. Pack Sizes: 10mg, 50mg, 250mg. Molecular Formula: C??H??O?. US Biological Life Sciences. | Worldwide |
| glucan 1,4-α-glucosidase | Most forms of the enzyme can rapidly hydrolyse 1,6-α-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions. Group: Enzymes. Synonyms: glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase. Enzyme Commission Number: EC 3.2.1.3. CAS No. 9032-08-0. Glucoamylase. 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-3893; glucan 1,4-α-glucosidase; EC 3.2.1.3; 9032-08-0; glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase. Cat No: EXWM-3893. | |
| Glucose-6-Phosphate Isomerase from Human, Recombinant | Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a...somerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Purity: Greater than 95.0% as determined by SDS-PAGE. PGI. Mole weight: 65.3 kDa. Stability: GPI although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colorless solution. Source: E. coli. Species: Human. Glucose-6-phosphate isomerase; Phosphoglucose isomerase; Phosphohexose isomerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Cat No: NATE-0841. | |
| Glyceraldehyde-3-phosphate dehydrogenase from Human, Recombinant | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a tetramer of 36 kDa subunits, is a catalytic enzyme involved in glycolysis. GAPDH catalyzes the reversible reduction of glyceraldehyde-3-phosphate to 3-phosphoglycerol phosphate in the presence of NAD+. Besides functioning as a glycolytic enzyme in the cytoplasm, mammalian GAPDH is also involved in a variety of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. Glyceraldehyde-3-phosphate dehydrogenase was also found to bind to mutant polyglutamine proteins formed in neurodegenerative diseases such as Huntingto...horylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Mole weight: 37,984 Da. Activity: > 80 units/mg protein. Stability: Store at -20°C. Form: Lyophilized from a buffered solution with stabilizers. Source: E. coli. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate | |
| glycylpeptide N-tetradecanoyltransferase | The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein. Group: Enzymes. Synonyms: peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Enzyme Commission Number: EC 2.3.1.97. CAS No. 110071-61-9. 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-2279; glycylpeptide N-tetradecanoyltransferase; EC 2.3.1.97; 110071-61-9; peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Cat No: EXWM-2279. | |
| heme ligase | This heme detoxifying enzyme is found in Plasmodium parasites and converts toxic heme to crystalline hemozoin. These organisms lack the mammalian heme oxygenase for elimination of heme. Group: Enzymes. Synonyms: heme detoxification protein; HDP; hemozoin synthase. Enzyme Commission Number: EC 4.99.1.8. 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-5365; heme ligase; EC 4.99.1.8; heme detoxification protein; HDP; hemozoin synthase. Cat No: EXWM-5365. | |
| heme oxygenase (biliverdin-producing) | This mammalian enzyme participates in the degradation of heme. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. The enzyme requires NAD(P)H and EC 1.6.2.4, NADPH-hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin). Group: Enzymes. Synonyms: ORP33 proteins; haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating). Enzyme Commission Number: EC 1.14.14.18. CAS No. 9059-22-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0915; heme oxygenase (biliverdin-producing); EC 1.14.14.18; 9059-22-7; ORP33 proteins; haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); heme,hydrogen-donor:oxygen oxidoreductase (α-methene-oxidizing, hydroxylating). Cat No: EXWM-0915. | |
| heme oxygenase (biliverdin-producing, ferredoxin) | The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the α-carbon to CO. Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4, NADPH-hemoprotein reductase. Group: Enzymes. Synonyms: HO1 (gene name); HY1 (gene name); HO3 (gene name); HO4 (gene name); pbsA1 (gene name). Enzyme Commission Number: EC 1.14.15.20. 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-0945; heme oxygenase (biliverdin-producing, ferredoxin); EC 1.14.15.20; HO1 (gene name); HY1 (gene name); HO3 (gene name); HO4 (gene name); pbsA1 (gene name). Cat No: EXWM-0945. | |
| [heparan sulfate]-glucosamine 3-sulfotransferase 3 | Two major substrates contain the tetrasaccharides: ? undetermined 2-sulfo-uronic acid? GlcN2S? IdoA2S? GlcN*? and ? undetermined 2-sulfo-uronic acid? GlcN2S? IdoA2S? GlcN6S*? (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk). Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)]. Group: Enzymes. Enzyme Commission Number: EC 2.8.2.30. 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-3390; [heparan sulfate]-glucosamine 3-sulfotransferase 3; EC 2.8.2.30. Cat No: EXWM-3390. | |
| HtrA2 peptidase | This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). Belongs in peptidase family S1C. Group: Enzymes. Synonyms: high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Enzyme Commission Number: EC 3.4.21.108. 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-4103; HtrA2 peptidase; EC 3.4.21.108; high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Cat No: EXWM-4103. | |
| hydroperoxy icosatetraenoate dehydratase | Binds Fe2+. The mammalian enzymes accept a range of hydroperoxyicosatetraenoates (HPETE). The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency. The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE). The enzymes also catalyse the reaction of EC 5.4.4.7, hydroperoxy icosatetraenoate isomerase. Group: Enzymes. Synonyms: epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Enzyme Commission Number: EC 4.2.1.152. 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-4993; hydroperoxy icosatetraenoate dehydratase; EC 4.2.1.152; epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Cat No: EXWM-4993. | |
| inositol-hexakisphosphate kinase | Three mammalian isoforms are known to exist. Group: Enzymes. Synonyms: ATP:1D-myo-inositol-hexakisphosphate phosphotransferase; IP6K. Enzyme Commission Number: EC 2.7.4.21. CAS No. 176898-37-6. 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-3203; inositol-hexakisphosphate kinase; EC 2.7.4.21; 176898-37-6; ATP:1D-myo-inositol-hexakisphosphate phosphotransferase; IP6K. Cat No: EXWM-3203. | |
| inositol-polyphosphate 5-phosphatase | One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids. Group: Enzymes. Synonyms: type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP3/Ins(1,3,4,5)P4 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-. Enzyme Commission Number: EC 3.1.3.56. CAS No. 106283-14-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3661; inositol-polyphosphate 5-phosphatase; EC 3.1.3.56; 106283-14-1; type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP3/Ins(1,3,4,5)P4 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-phosphatase; D-myo-inositol 1,4,5-trisphosphate 5-phosphatase; L-myo-inositol 1,4,5-trisphosphate-monoesterase; inositol phosphate 5-phosphomonoesterase; inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase; Ins(1,4,5)P3 5-phosphatase; D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase; inositol 1,4,5-trisphosphate phosphatase; inositol polyphosphate-5-phosphatase; myo-inositol-1,4,5-trisphosphate 5-phosphatase; inositol-1,4,5-trisphosphate 5-phosphatase. Cat No: EXWM-3661. | |
| legumain | Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13. Group: Enzymes. Synonyms: asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Enzyme Commission Number: EC 3.4.22.34. CAS No. 149371-18-6. 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-4209; legumain; EC 3.4.22.34; 149371-18-6; asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Cat No: EXWM-4209. | |
| L-Homoarginine hydrochloride | L-Homoarginine may be used to create non-natural proteins for studies of post-translational protein modifications. Arginine residues are often located at the active centers of proteins and enzymes. Replacing these arginines with homoarginine can elucidate protein function and structural requirements. L-Homoarginine is used to study the mechanisms of nitric oxide production by cells via nitric oxide synthase(s). L-Homoarginine is used as a selective mammalian alkaline phosphatase isoenzyme inhibitor. The substitution of homoarginine for arginine or lysine renders proteins resistant to proteolysis by trypsin. Group: Amino acids. Alternative Names: (S)-2-Amino-6-guanidinohexanoic acid hydrochloride. CAS No. 1483-01-8. Molecular formula: H2NC(=NH)NH(CH2)4CH(NH2)CO2H · HCl. Mole weight: 224.69. Canonical SMILES: Cl[H].N[C@@H](CCCCNC(N)=N)C(O)=O. ECNumber: 216-045-6. Catalog: ACM1483018-1. |  |
| long-chain fatty acid ω-monooxygenase | The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4). Group: Enzymes. Synonyms: CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Enzyme Commission Number: EC 1.14.13.205. 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-0807; long-chain fatty acid ω-monooxygenase; EC 1.14.13.205; CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Cat No: EXWM-0807. | |
| L-serine-phosphatidylethanolamine phosphatidyltransferase | This mammalian enzyme catalyses an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine. Group: Enzymes. Synonyms: phosphatidylserine synthase 2; serine-exchange enzyme II; PTDSS2 (gene name). Enzyme Commission Number: EC 2.7.8.29. 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-3328; L-serine-phosphatidylethanolamine phosphatidyltransferase; EC 2.7.8.29; phosphatidylserine synthase 2; serine-exchange enzyme II; PTDSS2 (gene name). Cat No: EXWM-3328. | |
| methionine synthase | Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin-NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase, which acts only on the triglutamate. Group: Enzymes. Synonyms: 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethy. Enzyme Commission Number: EC 2.1.1.13. CAS No. 9033-23-2. 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-1727; methionine synthase; EC 2.1.1.13; 9033-23-2; 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethylase; N-methyltetrahydrofolate:L-homocysteine methyltransferase; N5-methyltetrahydrofolate methyltransferase; N5-methyltetrahydrofolate- | |
| methylglyoxal reductase (NADH) | This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Enzyme Commission Number: EC 1.1.1.78. CAS No. 37250-16-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0361; methylglyoxal reductase (NADH); EC 1.1.1.78; 37250-16-1; methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Cat No: EXWM-0361. | |
| mitogen-activated protein kinase | Phosphorylation of specific tyrosineand threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth...pk; PMK-1; PMK-2; PMK-3; pp42; pp44mapk; p44mpk; SAPK; STK26; stress-activated protein kinase. Enzyme Commission Number: EC 2.7.11.24. 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-3144; mitogen-activated protein kinase; EC 2.7.11.24; c-Jun N-terminal kinase; Dp38; ERK; ERK1; ERK2; extracellular signal-regulated kinase; JNK; JNK3α1; LeMPK3; MAP kinase; MAP-2 kinase; MAPK; MBP kinase I; MBP kinase II; microtubule-associated protein 2 kinase; microtubule-associated protein kinase; myelin basic protein kinase; p38Δ; p38-2; p42 mitogen-activated protein kinase; p42mapk; PMK-1; PMK- | |
| mitogen-activated protein kinase kinase | This enzyme is a dual-specific protein kinase and requires mitogen-activated protein kinase kinase kinase (MAPKKK) for activation. It is required for activation of EC 2.7.11.24, mitogen-activated protein kinase. Phosphorylation of MEK1 by Raf involves phosphorylation of two serine residues. Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury. Group: Enzymes. Synonyms: MAP kinase kinase; MAP kinase kinase 4; MAP kinase kinase 7; MAP kinase or ERK . Enzyme Commission Number: EC 2.7.12.2. 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-3162; mitogen-activated protein kinase kinase; EC 2.7.12.2; MAP kinase kinase; MAP kinase kinase 4; MAP kinase kinase 7; MAP kinase or ERK kinase; MAP2K; MAPKK; MAPKK1; MEK; MEK1; MEK2; MKK; MKK2; MKK4; MKK6; MKK7; STK27. Cat No: EXWM-3162. | |
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