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1-Methylpyrene is a ubiquitous environmental pollutant and rodent carcinogen. Its mutagenic activity depends on sequential activation by various CYP and sulfotransferase (SULT) enzymes. 1-Methylpyrene induces chromosome loss and mitotic disturbance, proba. Uses: Scientific research. Group: Fluorescent dye. CAS No. 2381-21-7. Pack Sizes: 10 mg. Product ID: HY-W271064.
2,3,4,6,3,4,6-Hepta-O-benzoylsucrose
2,3,4,6,3,4,6-Hepta-O-benzoylsucrose is an efficacious glycosidase inhibitor, ubiquitously utilized in the realm of targeting metabolic maladies including diabetes. Its principal mechanism is the potent and precise suppression of enzymes tasked with the paramount function of complex sugar hydrolysis. Synonyms: 2,3,4,6-Tetra-O-benzoyl-a-D-glucopyranosyl-(1-2)-3,4,6-tri-O-benzoyl-b-D-fructopyranoside. CAS No. 309261-83-4. Molecular formula: C61H50O18. Mole weight: 1071.04.
2,3,4,6-Tetra-O-acetyl-b-D-galactopyranosyl ethylxanthate, a chemical compound ubiquitous in biomedicine, boasts the potential to counter many maladies, including cancer and cardiovascular diseases. It functions by inhibiting various enzymes and flaunts anti-tumor capabilities, thereby rendering it an alluring contender for cancer therapy. Molecular formula: C17H24O10S2. Mole weight: 452.5.
2-Nitrophenyl 2-acetamido-2-deoxy-b-D-galactopyranoside, an essential biochemical compound extensively utilized in the biomedical industry, exhibits its pivotal role by functioning as a substrate for enzymes responsible for the cleavage of glycosidic bonds. Its ubiquitous utilization in exploring enzyme kinetics and comprehending the intricate facets of drug metabolism and disease-associated pathways makes it an invaluable asset within the scientific community. Synonyms: ONP-GalNAc. CAS No. 152957-34-1. Molecular formula: C14H18N2O8. Mole weight: 342.3.
3-hydroxyacyl-[acyl-carrier-protein] dehydratase
This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The enzyme uses fatty acyl thioesters of ACP in vivo. Different forms of the enzyme may have preferences for substrates with different chain length. For example, the activity of FabZ, the ubiquitousenzyme in bacteria, decreases with increasing chain length. Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyses EC 5.3.3.14, trans-2-decenoyl-[acyl-carrier protein] isomerase. Despite the differences both forms...hydratase. Enzyme Commission Number: EC 4.2.1.59. CAS No. 9030-85-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5047; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; EC 4.2.1.59; 9030-85-7; fabZ (gene name); fabA (gene name); D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase; D-3-hydroxyoctanoyl-acyl carrier protein dehydratase; β-hydroxyoctanoyl-acyl carrier protein dehydrase; β-hydroxyoctanoyl thioester dehydratase; β-hydroxyoctanoyl-ACP-dehydrase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hyd
4-Chloro-3-indolyl b-D-galactopyranoside
4-Chloro-3-indolyl β-D-galactopyranoside is a prominent biochemical substrate ubiquitously employed in the biomedical sector, serving as a remarkable catalyst to discern the existence of β-galactosidase activity is an indispensable marker extensively utilized in the realm of molecular biology. Notably, its versatile application aids in the comprehensive investigation of gene expression patterns and enzyme functionality across diverse biological systems. Moreover, this compound, owing to its profound impact, garners immense prominence in assays necessitating a visual representation of β-galactosidase-mediated hydrolytic processes. CAS No. 135313-63-2. Molecular formula: C14H16ClNO6. Mole weight: 329.73.
5-Bromo-4-chloro-3-indolyl b-D-fucopyranoside
5-Bromo-4-chloro-3-indolyl b-D-fucopyranoside, a ubiquitous substrate in molecular and cell biology, is utilized as a tool to indicate the presence of beta-galactosidase in the targeted cells. Upon cleavage by the enzyme, the formerly dormant substrate induces a conspicuously blue hue that unmistakably confirms gene expression and sheds light on cellular localization. Synonyms: X-b-D-Fucoside. CAS No. 17016-46-5. Molecular formula: C14H15BrClNO5. Mole weight: 392.63.
5'-O-(3'-Guanylyl)uridine
5'-O-(3'-Guanylyl)uridine, a biomolecule ubiquitous in the biomedical industry, facilitates RNA processing and translation. Notwithstanding, this biomolecule's salience is not restricted to solely association with these fundamental processes. Remarkably, it also serves as a substrate for various enzymes, mitigating the severity of viral infections, and demonstrating its potential therapeutic applications. Synonyms: guanylyl(3'-5')uridine; GpU RNA Dinucleotide (5'-3'). Grades: ≥95% by AX-HPLC. Molecular formula: C19H24N7O13P. Mole weight: 589.40.
Arginase (Crude Enzyme)
Arginase is a manganese-containing enzyme. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Analysis; medicine; drug development; pharmacology. Group: Enzymes. Synonyms: arginine amidinase; canavanase; L-arginase; arginine transamidinase. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Arginase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. arginine amidinase; canavanase; L-arginase; arginine transamidinase. Pack: 100ml. Cat No: NATE-1840.
Arginase from Human, Recombinant
Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: >95% as judged by SDS-PAGE. Arginase. Mole weight: 35 kDa. Activity: 390 U/mg protein, 1950 U/ml. Storage: Arginase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: Human liver. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-1572.
Benzyl 2-acetamido-3,4-di-O-benzyl-2-deoxy-a-D-galactopyranoside is a ubiquitous biomedical compound, serving as an active antagonist targeting selective enzymes pivotal in the biogenesis of glycoproteins and glycolipids.
Benzyl D-glucopyranoside
Benzyl D-glucopyranoside: A ubiquitous compound extensively utilized in the realm of biomedical research, functioning as a highly sought-after substrate to probe and scrutinize the intricate functionality of multifarious enzymes. Its employment has pervaded diverse studies centering around carbohydrate metabolism, glycosylation phenomena, and the kinetics of enzymatic reactions. Synonyms: Benzyl D-Glucopyranoside; Benzyl glucopyranoside; 34246-23-6; (2R,3S,4S,5R)-2-(hydroxymethyl)-6-phenylmethoxyoxane-3,4,5-triol; 1-O-Benzyl-D-Glucopyranose; SCHEMBL4866754; GKHCBYYBLTXYEV-HENWMNBSSA-N; Benzyl D-Glucopyranoside (An a-b mixture); W-202397; (3R,4S,5S,6R)-2-(benzyloxy)-6-(hydroxymethyl)oxane-3,4,5-triol. CAS No. 34246-23-6. Molecular formula: C13H18O6. Mole weight: 270.28.
cathepsin O
Cathepsin O is a lysosomal cysteine peptidase of family C1 (papain family). The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64. Cathepsin O is ubiquitously expressed in human tissues and the human gene locus is 4q31-32. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.42. CAS No. 162032-86-2. 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-4217; cathepsin O; EC 3.4.22.42; 162032-86-2. Cat No: EXWM-4217.
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.
CCA tRNA nucleotidyltransferase
The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition. Group: Enzymes. Synonyms: CCA-adding enzyme; tRNA adenylyltransferase; tRNA cytidylyltransferase; tRNA CCA-pyrophosphorylase; tRNA-nucleotidyltransferase; transfer-RNA nucleotidyltransferase; transfer ribonucleic acid nucleotidyl transferase; C. Enzyme Commission Number: EC 2.7.7.72. 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-3284; CCA tRNA nucleotidyltransferase; EC 2.7.7.72; CCA-adding enzyme; tRNA adenylyltransferase; tRNA cytidylyltransferase; tRNA CCA-pyrophosphorylase; tRNA-nucleotidyltransferase; transfer-RNA nucleotidyltransferase; transfer ribonucleic acid nucleotidyl transferase; CTP(ATP):tRNA nucleotidyltransferase; transfer ribonucleate adenylyltransferase; transfer ribonucleate adenyltransferase; transfer RNA adenylyltransferase; transfer ribonucleate nucleotidyltransferase; ATP (CTP):tRNA nucleotidyltransferase; ribonucleic cytidylic cytidylic
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.
cTMP
cTMP (2?,3?-dideoxy-3?-thiothymidine) is an exceptional biomedical compound ubiquitously applied in studying the pernicious Human Immunodeficiency Virus/Acquired Immunodeficiency Syndrome (HIV/AIDS). Functioning as a high-potency antiretroviral compound, cTMP exercises its efficacious mechanism by adeptly obstructing the pernicious reverse transcriptase enzyme. Synonyms: Thymidine- 3', 5'- cyclic monophosphate, sodium salt. Grades: ≥ 98% by HPLC. CAS No. 76567-90-3. Molecular formula: C10H12N2O7P · Na. Mole weight: 326.2.
Cystathionine β Synthase from Human, recombinant
Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8; Cystathionine β-synthase; Beta-thionase; methylcysteine synthase; serine sulfhydrase. Enzyme Commission Number: EC 4.2.1.22. Purity: > 90% by SDS-PAGE. CBS. Mole weight: 61.9 kDa (1-551 aa, NT His Tag). Activity: 100 U/mg. Stability: Stable for at least 1 year as supplied. Avoid repeated freeze and thaw cycles. Storage: Store at -20°C. Form: Liquid. Source: E. coli. Species: Human. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8; Cystathionine β-synthase; Cystathionine β synthase; Beta-thionase; methylcysteine synthase; serine sulfhydrase. Cat No: NATE-1667.
Cystathionine-β-synthase, Recombinant
Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Applications: This protein can be used for producing hcy in vitro diagnosis kit. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Enzyme Commission Number: EC 4.2.1.22. CAS No. 9023-99-8. Purity: >90% (by SDS-PAGE). CBS. Mole weight: 56 KD. Appearance: Lyophilized powder. Storage: The lyophilized powder should be stored at -20°C where it is stable for up to several years. The solution could be stored at 4°C where it is stable for up to 1 year. Repeated freezing and thawing cycles of the reconstituted solution is not recommended. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Cat No: DIA-293.
D-(+)-Biotin
D-(+)-Biotin is a coenzyme that offers three possible binding sites. Applications: An important ubiquitous metabolism coenzyme. Group: Coenzymes. Synonyms: Vitamin H; 5-(2-Oxo-hexahydro-thieno[3,4-d]imidazol-6-yl)-pentanoic acid; Biotin. CAS No. 58-85-5. Purity: ≥99%. Mole weight: 244.3. Appearance: Powder. Form: Solid. Vitamin H; 5-(2-Oxo-hexahydro-thieno[3,4-d]imidazol-6-yl)-pentanoic acid; Biotin; D-(+)-Biotin; 58-85-5. Cat No: COEC-007.
Dipeptidyl Peptidase IV from Human, Recombinant
Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contai...zyme from creative enzymes has been used to study the lc-ms (liquid chromatography-mass spectrometry) based assay method for dpp-iv inhibitor screening and substrate discovery. Group: Enzymes. Synonyms: EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; 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; dipeptidy
D(+)-Raffinose Pentahydrate
Raffinose is a trisaccharide composed of galactose, glucose, and fructose. It can be found in beans, cabbage, brussels sprouts, broccoli, asparagus, other vegetables, and whole grains. Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme not found in the human digestive tract. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. The enzyme does not cleave β-linked galactose, as in lactose.The raffinose family of oligosaccharides (RFOs) are alpha-galactosyl derivatives of sucrose, and the most common are the trisaccharide raffinose, the tetrasaccharide stachyose, and the pentasaccharide verbascose. RFOs are almost ubiquitous in the plant kingdom, being found in a large variety of seeds from many different families, and they rank second only to sucrose in abundance as soluble carbohydrates.Humans and other monogastric animals (pigs and poultry) do not possess the α-GAL enzyme to break down RFOs and these oligosaccharides pass undigested through the stomach and upper intestine. In the lower intestine, they are fermented by gas-producing bacteria that do possess the α-GAL enzyme and make carbon dioxide, methane or hydrogenleading to the flatulence commonly associated with eating beans and other vegetables. α-GAL is present in digestive aids such as the product Beano.Pr
EDA-ATP - DY-480XL
EDA-ATP, the synthetic nucleotide ubiquitous in biomedicine, offers a fascinating lens for exploring the architectural and operational intricacies of ATP-substrated enzymes and proteins. This compound is also a hotbed of experimentation in investigating purinergic signaling and the pivotal role of ATP in immune responses. Moreover, the marriage of EDA-ATP with DY-480XL fluorescent dyes, has enabled high-fidelity imaging and detection. Synonyms: 2'/3'-O-(2-Aminoethyl-carbamoyl)-Adenosine-5'-triphosphate, labeled with DY 480XL, Triethylammonium salt. Grades: ≥ 95 % by HPLC. Molecular formula: C39H50N9O20P3S (free acid). Mole weight: 1089.85 (free acid).
Formate dehydrogenase
Formate dehydrogenase is an enzymeubiquitous in prokaryotes and eukaryotes that catalyzes the reversible oxidation of formate to carbon dioxide. According to its metal content, structure and catalytic strategy, Formate dehydrogenase can be divided into two categories, non-metallic and metal-containing, which are often used in biochemical research [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9028-85-7. Pack Sizes: 50 U; 100 U. Product ID: HY-P2907.
Glutamine Synthetase from Human, recombinant
GLUL also known as Glutamine synthetase. It is a trimetallic enzyme containing two divalent cation sites and one monovalent cation site per subunit. GLUL is able to regulate intracellular concentrations of glutamate and catalyzes the synthesis of glutamine form glutamate and ammonia. It is ubiquitously expressed in the human and plays a major role for many metabolic pathways such as cell proliferation, inhibition of apoptosis, and cell signaling. Recombinant Human GLUL was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: > 85% by SDS-PAGE. GS. Mole weight: 42 kDa. Activity: > 2.000 pmol/min/ug. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Cat No: NATE-1675.
Immobilized Lipase-A from Serratia marcescens, Recombinant
Lipase (EC 3.1.1.3) is a ubiquitousenzyme that catalyzes the hydrolysis of fats and oil. The Serratia marcescens lipase is recognized for its excellent enantioselectivity in biocatalytic hydrolysis of trans-3-(4-methoxyphynyl) glycidic acid methyl ester [(±)-MPGM] to produce (2R, 3S)-3-(4-methoxyphenyl) glycidic acid methyl ester [(-)-MPGM], an important intermediate for the synthesis of diltiazem hydrochlorid. Group: Enzymes. Synonyms: Lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Purity: >90%. Lipase. Mole weight: 65 kDa. Stability: Lipase-A although stable at room temp for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Form: Sterile Filtered lyophilized powder. Source: E. Coli. Species: Serratia marcescens. Lipase; Lipase-A; Lipase A; EC 3.1.1.3; Immobilized Lipase-A. Cat No: NATE-1621.
Inorganic Pyrophosphatase from Escherichia coli, Recombinant
Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Inorganic pyrophosphatase (ppase) is a ubiquitousenzyme catalyzing the reaction ppi + h2o ? 2pi. it plays an important role in protein, rna, and dna synthesis. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Purity: > 90%. Inorganic pyrophosphatase. Activity: > 800 units/mg protein. Storage: -20°C. Form: Lyophilized powder in Tris-buffered salts containing protease inhibitors. Source: E. coli. Species: Escherichia coli. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0355.
Na+/K+-exchanging ATPase
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential. Group: Enzymes. Enzyme Commission Number: EC 3.6.3.9. 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-4698; Na+/K+-exchanging ATPase; EC 3.6.3.9. Cat No: EXWM-4698.
Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Inorganic pyrophosphatase (ppase) is a ubiquitousenzyme catalyzing the reaction ppi + h2o ? 2pi. it plays an important role in protein, rna, and dna synthesis. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Activity: 15-25 units/mg protein (biuret). Storage: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0353.
Native Baker's yeast (S. cerevisiae) Inorganic Pyrophosphatase
Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. This ubiquitousenzyme serves to drive metabolic reactions that produce pyrophosphate, since these reactions typically have...phohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa (homodimer consisting of two equal subunits of molecular weight 32-35 kDa). Activity: Type I, > 1,000 units/mg protein (BCA); Type II, > 500 units/mg protein (E1%/280). Storage: -20°C. Form: Type I, lyophilized powder containing 90% buffer salts; Type II, Lyophilized powder containing 85% buffer salts. Source: Baker's yeast (S. cerevisiae). Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0354.
Native Bovine L-Arginase
Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Protein > 70 % by biuret. Arginase. Storage: -20°C. Form: powder. Source: Bovine liver. Species: Bovine. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0379.
Native Bovine Liver Alkaline Phosphatase
Alkaline phosphatases (APs) are highly ubiquitousenzymes, present in all species from bacteria to man. In humans, APs are encoded by a multi-gene family composed of four loci; i.e., tissue-nonspecific AP, also called bone/liver/kidney AP, intestinal. The sequence and complexity of the AP genes from other vertebrates and lower species are now being elucidated. The biological function of AP isozymes is still unknown. In vitro, the enzymes behave as phosphotransferases at neutral pH. The use of phosphate acceptor molecules (diethanolamine, tris, 2-amino-2-methyl-1-propanol) in the buffered substrate solutions increases the reaction rates and, thus, the sensitivity of assays based on AP determinations. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: 100 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Liver. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase; AP. Cat No: NATE-1871.
Native Bovine Protein Phosphatase 2C
Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619.
Native Corn Phospho (enol)pyruvate Carboxylase
Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Phospho (enol)pyruvate Carboxylase from corn was found to be highly susceptible to trypsin digestion. Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Applications: Phospho (enol)pyruvate carboxylase has been used in a study to assess activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress. it has also been used in a study to investigate the specific density of leaf as a characteristic of the photosynthetic apparatus. Group: Enzymes. Synonyms: phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Activity: > 1 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.4 M (NH4)2SO4 solution containing 10 mM phosphate buffer, pH 7.0, 1 mM biotin, 5 mM dithiothreitol and 1 mM phenylmethylsulfonyl fluoride. Source: Corn. phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.1.1.31; 9067-77-0. Cat No: NATE-0543.
Native Cystathionine-β-synthase
Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Human cbs performs a crucial step in the biosynthetic pathway of cysteine by providing a regulatory control po...nates methyl groups to a variety of substrates, e.g., neurotransmitters, proteins, and nucleic acids. in mammals, cbs is a highly regulated enzyme, which contains a heme cofactor that functions as a redox sensor, that can modulate its activity in response to changes in the redox potential. if the resting form of cbs in the cell has ferrous heme, the potential exists for activating the enzyme under oxidizing conditions by conversion to the ferric state. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Enzyme Commission Number: EC 4.2.1.22. CAS No. 9023-99-8. CBS. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Cat No: DIA-272.
Native Human Creatine Kinase MB Fraction
In the cells, the "cytosolic" CK enzymes consist of two subunits, which can be either B (brain type) or M (muscle type). There are, therefore, three different isoenzymes:CK-MM, CK-BB and CK-MB. The genes for these subunits are located on different chromosomes:B on 14q32 and M on 19q13. In addition to those three cytosolic CK isoforms, there are two mitochondrial creatine kinase isoenzymes, the ubiquitous and sarcomeric form. The functional entity of the latter two mitochondrial CK isoforms is an octamer consisting of four dimers each. Applications: The mb isoenzyme of creatine kinase (mbck) can be used as a diagnostic marker for acute myocardial infarction. Group: Enzymes. Synonyms: CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Purity: > 70% (SDS-PAGE). Activity: > 1,000 U/mL. Form: liquid. Source: Human heart. Species: Human. CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Cat No: NATE-0141.
Native Human Dipeptidyl Peptidase-4
Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18....Store at -20°C. Form: Liquid. Source: Human Placenta. Species: Human. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; 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: NATE-0962.
Native Porcine Dipeptidyl Peptidase IV
Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18...ukocyte 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. Enzyme Commission Number: EC 3.4.14.5. CAS No. 54249-88-6. Purity: >94% by SDS-PAGE. DPP IV. Activity: 1.0 U/mg; Specific Activity >40 U/mg protein. Storage: at -70°C, Avoid freeze/thaw. Form: Liquid. In 20 mM Tris-HCl, 5 mM CaCl?, 1 uM ZnCl?, 0.05% NaN?, pH 8.0. Source: Porcine Kidney. Species: Porcine. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidas
Native Rat Arginase
Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Purified. Arginase. Activity: > 200 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0086.
pectinesterase
Pectinesterase (PE) (EC 3.1.1.11) is a ubiquitous cell-wall-associated enzyme that presents several isoforms that facilitate plant cell wall modification and subsequent breakdown. It is found in all higher plants as well as in some bacteria and fungi. Pectinesterase functions primarily by altering the localised pH of the cell wall resulting in alterations in cell wall integrity. Group: Enzymes. Synonyms: pectin demethoxylase; pectin methoxylase; pectin methylesterase; pectase; pectin methyl esterase; pectinoesterase. Enzyme Commission Number: EC 3.1.1.11. CAS No. 9025-98-3. Pectinesterase. 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-3439; pectinesterase; EC 3.1.1.11; 9025-98-3; pectin demethoxylase; pectin methoxylase; pectin methylesterase; pectase; pectin methyl esterase; pectinoesterase. Cat No: EXWM-3439.
peroxiredoxin
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see mechanism). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydr...se thioredoxin as an electron donor. The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule. Group: Enzymes. Synonyms: thioredoxin peroxidase; tryparedoxin peroxidase; alkyl hydroperoxide reductase C22; AhpC; TrxPx; TXNPx; Prx; PRDX. Enzyme Commission Number: EC 1.11.1.15. CAS No. 207137-51-7. 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-0496; peroxiredoxin; EC 1.11.1.15; 207137-51-7; thioredoxin peroxidase; tryparedoxin peroxidase; alkyl hydroperoxide reductase C22; AhpC; TrxPx; TXNPx; Prx; PRDX. Cat No: EXWM-0496.
Protein Kinase A catalytic subunit human, Recombinant
Ubiquitous serine-threonine kinase that phosphorylates a broad spectrum of substrates, and regulates many cellular processes. The catalytic subunit is released following binding of cyclic AMP to the regulatory subunits of the PKA holoenzyme. The free catalytic subunit has intrinsic activity and does not require added cyclic AMP. >90% (sds-page), recombinant, expressed in e. coli, buffered aqueous glycerol solution. Group: Enzymes. Synonyms: Protein Kinase A catalytic subunit; Protein kinase A; PKA; PKAC; cAMP-dependent protein kinase catalytic subunit; PRKAC. Purity: >90% (SDS-PAGE). PKAC. Mole weight: mol wt 43.5 kDa. Activity: >1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: E. coli. Species: Human. Protein Kinase A catalytic subunit; Protein kinase A; PKA; PKAC; cAMP-dependent protein kinase catalytic subunit; PRKAC. Cat No: NATE-0571.
Used as an alternate carbon source for wild-type yeast. Raffinose is a trisaccharide composed of galactose, glucose, and fructose. It can be found in beans, cabbage, brussels sprouts, broccoli, asparagus, other vegetables, and whole grains. Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme not found in the human digestive tract. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. The enzyme does not cleave β-linked galactose, as in lactose.The raffinose family of oligosaccharides (RFOs) are alpha-galactosyl derivatives of sucrose, and the most common are the trisaccharide raffinose, the tetrasaccharide stachyose, and the pentasaccharide verbascose. RFOs are almost ubiquitous in the plant kingdom, being found in a large variety of seeds from many different families, and they rank second only to sucrose in abundance as soluble carbohydrates. Group: Biochemicals. Alternative Names: D-(+)-Raffinose; Melitose, Melitriose; O-a-D-Galactopyranosyl-(1->6)-a-D-glucopyranosyl-ß-D-fructofuranoside. Grades: Molecular Biology Grade. CAS No. 17629-30-0. Pack Sizes: 100g, 500g, 1Kg, 2.5Kg, 5Kg. Molecular Formula: C18H32O16 5H2O, Molecular Weight: 594.51. US Biological Life Sciences.
Worldwide
S-Adenosyl-L-Homocysteine Hydrolase, Recombinant
Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine. S-adenosyl-l-homocysteine hydrolase (sahh, ec 3.3.1.1) (adohcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of s-adenosyl-l-homocysteine into adenosine and homocysteine. sahh is a ubiquitousenzyme which binds and requires nad+ as a cofactor. adohcyase is a highly conserved protein of about 430 to 470 amino acids. the family contains a glycine-rich region in the central part of adohcyase; aregion thought to be involved in nad-binding. this protein may use themorpheein model of allosteric regulation. Group: Enzymes. Synonyms: Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocyste. Enzyme Commission Number: EC 3.3.1.1. Purity: >90% (SDS-PAGE test). Mole weight: About 44kDa (SDS-PAGE detection). Activity: 140U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Cat No: NATE-1150.
1-Benzyl-I3C
1-Benzyl-I3C is a NEDD4-1 inhibitor with significant anticancer activity. 1-Benzyl-I3C can directly inhibit the ubiquitination activity of NEDD4-1 with an IC50 of 12.3μM, which is significantly better than its precursor compound I3C of 284μM. 1-Benzyl-I3C and its analogs showed good effects in inhibiting the proliferation of human melanoma cells, which is roughly related to their potency as NEDD4-1 enzyme inhibitors. By combining in vitro ubiquitination experiments and thermal stability analysis, 1-Benzyl-I3C was shown to be able to bind to the catalytic HECT domain of NEDD4-1 [1]. Uses: Scientific research. Group: Natural products. CAS No. 60941-76-6. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-N10159.
5'-Biotin-dA-Monophosphate
5'-Biotin-dA-Monophosphate is an efficacious and distinguished modified nucleotide, meticulously crafted for elucidating the mysteries surrounding DNA. It is a versatile and ubiquitous component of biomedical industry, pertinently applied in labeling DNA and proficiently incorporated into DNA molecules during synthesis or enzymatic extension. It offers an exceptional opportunity for elegant detection or isolation of DNA molecules, rendering itself indispensable for a wide range of research applications like DNA-protein interactions, gene expression, and DNA sequencing. Synonyms: 5'-Biotin-dAMP. Grades: ≥90% by AX-HPLC. Molecular formula: C26H34N8O8PS. Mole weight: 656.70.
CC0651
CC0651, a Cdc34 ubiquitin-conjugating enzyme allosteric inhibitor, has been found to restrain the cell proliferation at some extent in cancer cell lines PC-3. IC50: 1.72 uM (inhibited the ubiquitination of p27 Kip1). Uses: Cc0651 is a cdc34 ubiquitin-conjugating enzyme allosteric inhibitor that has been found to restrain the cell proliferation at some extent in cancer cell lines pc-3. ic50: 1.72 um (inhibited the ubiquitination of p27 kip1). Synonyms: CC0651;CC 0651; CC-0651; (2R, 3S, 4S)-5-[4-(3, 5-dichlorophenyl)phenyl]-2, 3-dihydroxy-4-[(2-methoxyacetyl)amino]pentanoicacid; CC0651; 1319207-44-7; 4, 5-Dideoxy-5-(3', 5'-Dichlorobiphenyl-4-Yl)-4-[(Methoxyacetyl)amino]-L-ArabinonicAcid; U94; SCHEMBL14884531. Grades: 95%. CAS No. 1319207-44-7. Molecular formula: C20H21Cl2NO6. Mole weight: 442.29.
desampylase
The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. The enzyme contains Zn2+. cf. EC 3.4.19.12, ubiquitinyl hydrolase 1. In peptidase family M67. Group: Enzymes. Synonyms: SAMP-protein conjugate cleaving protease; HvJAMM1. Enzyme Commission Number: EC 3.4.24.88. 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-4372; desampylase; EC 3.4.24.88; SAMP-protein conjugate cleaving protease; HvJAMM1. Cat No: EXWM-4372.
DKM 2-93
DKM 2-93 covalently modify the catalytic cysteine of the ubiquitin-like modifier activating enzyme 5 (UBA5), thereby inhibiting its activity as a protein that activates the ubiquitin-like protein UFM1 to UFMylate proteins (IC50 = 430 μM). Synonyms: 2-chloro-N-[(3,4-dimethoxyphenyl)methyl]acetamide. CAS No. 65836-72-8. Molecular formula: C11H14ClNO3. Mole weight: 243.69.
E1 ubiquitin-activating enzyme
Catalyses the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step. Group: Enzymes. Synonyms: ubiquitin activating enzyme; E1; ubiquitin-activating enzyme E1. Enzyme Commission Number: EC 6.2.1.45. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5704; E1 ubiquitin-activating enzyme; EC 6.2.1.45; ubiquitin activating enzyme; E1; ubiquitin-activating enzyme E1. Cat No: EXWM-5704.
E2 ubiquitin-conjugating enzyme
The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage. Group: Enzymes. Synonyms: ubiquitin-carrier-protein E2; UBC (ambiguous); ubiquitin-conjugating enzyme E2. Enzyme Commission Number: EC 2.3.2.23. 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-2297; E2 ubiquitin-conjugating enzyme; EC 2.3.2.23; ubiquitin-carrier-protein E2; UBC (ambiguous); ubiquitin-conjugating enzyme E2. Cat No: EXWM-2297.
(E3-independent) E2 ubiquitin-conjugating enzyme
The enzyme transfers a single ubiquitin directly from an ubiquitinated E1 ubiquitin-activating enzyme to itself, and on to a lysine residue of the acceptor protein without involvement of E3 ubiquitin transferases (cf. EC 2.3.2.26, EC 2.3.2.27). It forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and Mg2+-ATP and catalyses the conjugation of ubiquitin to protein substrates, independently of E3. This transfer has only been observed with small proteins. In vitro a transfer to small acceptors (e.g. L-lysine, N-acetyl-L-lysine methyl ester) has been observed. Group: Enzymes. Synonyms: E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Enzyme Commission Number: EC 2.3.2.24. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2298; (E3-independent) E2 ubiquitin-conjugating enzyme; EC 2.3.2.24; E2-230K; UBE2O; E3-independent ubiquitin-conjugating enzyme E2. Cat No: EXWM-2298.
Guanosine 5'-triphosphate tetrasodium salt
Guanosine 5'-triphosphate tetrasodium salt is a paramount compound in the biomedical sector, serving as a pivotal precursor engendering diverse enzymatic reactions. Notably, it finds ubiquitous employment in research laboratories to elucidate G-protein coupled receptor signaling pathways, cellular energy transference and signal transduction mechanisms. Synonyms: Tetrasodium guanosine triphosphate; Guanosine 5'-(tetrasodium triphosphate); Tetrasodium 5'-O- ({[ (phosphonatooxy) phosphinato]oxy}phosphinato) guanosine; Guanosine, 5'-(tetrahydrogen triphosphate), sodium salt (1:4). Grades: ≥97% by HPLC. CAS No. 14356-96-8. Molecular formula: C10H12N5Na4O14P3. Mole weight: 611.11.
Heclin
Heclin is an HECT E3 ubiquitin ligase inhibitor. It also inhibits Nedd4, Smurf2 and WWP1 (IC50 = 6.3, 6.8 and 6.9 μM, respectively). Uses: Enzyme inhibitors. Synonyms: N-(4-Acetylphenyl)-3-(5-ethyl-2-furanyl)-2-propenamide. Grades: ≥98% by HPLC. CAS No. 890605-54-6. Molecular formula: C17H17NO3. Mole weight: 283.32.
HECT-type E3 ubiquitin transferase
In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the ε-amino group of an L-lysine residue of the acceptor protein. Group: Enzymes. Synonyms: HECT E3 ligase (misleading); ubiquitin transferase HECT-E3. Enzyme Commission Number: EC 2.3.2.26. 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-2300; HECT-type E3 ubiquitin transferase; EC 2.3.2.26; HECT E3 ligase (misleading); ubiquitin transferase HECT-E3. Cat No: EXWM-2300.
HIF-1 Signaling Pathway Compound Library
A unique collection of 1352 HIF-1 related small chemicals can be used for drug discovery in ischemic disease and cancer and related mechanism studies?- Covers PI3K-AKT, MAPK, Ubiquitination signaling pathways and targets such as HIF, HIF Prolyl-Hydroxylase, E1/E2/E3 Enzyme, PI3K, MAPK, Proteasome, etc. - Part of them are in clinical trial phase or FDA approved?- Detailed compound information with structure, target, and biological activity description?- NMR and HPLC validated to ensure high purity and quality. Uses: Scientific use. Product Category: L8500. Categories: HIF-1 Signaling Pathway Compounds Libraries.
IκB kinase
The enzyme phosphorylates IκB proteins at specific serine residues, which marks them for destruction via the ubiquitination pathway. Subsequent degradation of the IkB complex (IKK) activates NF-κB, a translation factor that plays an important role in inflammation, immunity, cell proliferation and apoptosis. If the serine residues are replaced by threonine residues, the activity of the enzyme is decreased considerably. Group: Enzymes. Synonyms: CHUK; IKBKA; IKBKB; IKK; IKK-1; IKK-2; inhibitor of NFκB kinase; inhibitor of NF-κB kinase; STK12; TANK-binding kinase 1; TBK1. Enzyme Commission Number: EC 2.7.11.10. 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-3129; IκB kinase; EC 2.7.11.10; CHUK; IKBKA; IKBKB; IKK; IKK-1; IKK-2; inhibitor of NFκB kinase; inhibitor of NF-κB kinase; STK12; TANK-binding kinase 1; TBK1. Cat No: EXWM-3129.
Lanosterol
Lanosterol is an intermediate of cholesterol synthesis and use of lanosterol induces ubiquitination and degradation of a rate-controlling enzyme of cholesterol synthesis, i.e., HMG CoA reductase. Lanosterol suppresses the aggregation and cytotoxicity of misfolded proteins linked with neurodegenerative diseases [1] [2]. Uses: Scientific research. Group: Natural products. CAS No. 79-63-0. Pack Sizes: 1 mg; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-W020033.
Lanosterol-d6
Lanosterol-d 6 is deuterium labeled Lanosterol. Lanosterol is an intermediate of cholesterol synthesis and use of lanosterol induces ubiquitination and degradation of a rate-controlling enzyme of cholesterol synthesis, i.e., HMG CoA reductase. Lanosterol s. Uses: Scientific research. Group: Isotope-labeled compounds. CAS No. 28290-39-3. Pack Sizes: 100 μg; 1 mg. Product ID: HY-W020033S.
Lurtotecan
liposomal lurtotecan is a liposome-encapsulated formulation of lurtotecan with antineoplastic activity. Lurtotecan, a semisynthetic analogue of camptothecin, selectively stabilizes the topoisomerase I-DNA covalent complex and forms an enzyme-drug-DNA ternary complex during S phase of the cell cycle, thereby inhibiting religation of topoisomerase I-mediated single-stranded DNA breaks. This ultimately results in an inhibition of DNA replication, inducing double-stranded DNA breakages, obstruction of RNA and protein synthesis and triggering apoptosis. Furthermore, this agent also stimulates degradation of topoisomerase I, likely mediated through ubiquitin-proteasomal pathway. Liposomal delivery of lurtotecan improves its penetration and delivery into tumors while lowering systemic side effects. Synonyms: OSI-221; OSI 221; OSI221; NX211; NX 211; NX-211; (S)-8-ethyl-8-hydroxy-15-((4-methylpiperazin-1-yl)methyl)-11,14-dihydro-2H-[1,4]dioxino[2,3-g]pyrano[3',4':6,7]indolizino[1,2-b]quinoline-9,12(3H,8H)-dione. CAS No. 149882-10-0. Molecular formula: C28H30N4O6. Mole weight: 518.57.
Native Human Annexin A3
Annexins form a family of proteins that bind phospholipids in a calcium dependent manner with repeats of 70-80 amino acid domains that are highly conserved, with the different properties being conferred by the variable N-termini. Annexin III is expressed in differentiated cells of myeloid lineage which is expressed less ubiquitously than Annexin V.Annexin III associates with cytoplasmic granules in both neutrophils and monocytes and it is suggested to be enzymatically active. It is thought to have prognostic value in a number of cancers including colorectal and upper tract urethral carcinoma. It may also play a specific role as a non-invasive marker for early detection of prostate cancer. Applications: Annexin a3 levels have been reported to be of clinical significance in prostate cancer, upper tract urethral carcinoma, colorectal cancer, breast cancer and lung adenocarcinoma. Group: Others. Synonyms: Annexin III; Annexin-3, 35-alpha calcimedin; inositol 1,2-cyclic phosphate 2-phosphohydrolase; Lipocor. Purity: >90% by SDS-polyacrylamide electrophoresis, Purified using conventional chromatography procedures. Mole weight: 36 kDa. Source: Human Neutrophils. Species: Human. Annexin III; Annexin-3, 35-alpha calcimedin; inositol 1,2-cyclic phosphate 2-phosphohydrolase; Lipocortin III; Placental anticoagulent protein III; PAP-III; Annexin A3. Cat No: NATE-1596.
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.
NSC 624206
NSC 624206 is a ubiquitin-activating enzyme inhibitor that blocks ubiquitin-thioester formation with IC50 value of 13 μM. Synonyms: NSC 624206; NSC624206; NSC-624206; N-[2-[[(4-Chlorophenyl)methyl]dithio]ethyl]-1-decanamine hydrochloride. Grades: ≥98% by HPLC. CAS No. 13116-77-3. Molecular formula: C19H32ClNS2.HCl. Mole weight: 410.51.
N-terminal E2 ubiquitin-conjugating enzyme
The enzyme ubiquitinylates the N-terminus of the acceptor protein. It is not reactive towards free lysine. Group: Enzymes. Synonyms: Ube2w; N-terminal ubiquitin-conjugating enzyme E2. Enzyme Commission Number: EC 2.3.2.25. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2299; N-terminal E2 ubiquitin-conjugating enzyme; EC 2.3.2.25; Ube2w; N-terminal ubiquitin-conjugating enzyme E2. Cat No: EXWM-2299.
NX-1607
NX-1607 (Compound 23) is an inhibitor of Cbl-b , an E3 enzyme in the ubiquitin-proteasome pathway, with an IC 50 value of less than 1 nM. NX-1607 can be used in cancer research [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Cbl-b-IN-3. CAS No. 2573775-59-2. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-141432.
P005091
P005091 is a potent and selective inhibitor of ubiquitin-specific protease (USP) 7 (IC50 = 4.2 μM). P005091 induces elevated p53 and apoptosis in cancer cell lines and displays antiangiogenic activity in vivo. The deubiquitylating enzyme USP7 (HAUSP) sits at a critical node regulating the activities of numerous proteins broadly characterized as tumor suppressors, DNA repair proteins, immune responders, viral proteins, and epigenetic modulators. Aberrant USP7 activity may promote oncogenesis and viral disease making it a compelling target for therapeutic intervention. Synonyms: P005091; P-005091; P 005091; P5091; P-5091; P 5091. Grades: 0.98. CAS No. 882257-11-6. Molecular formula: C12H7Cl2NO3S2. Mole weight: 348.212.
prokaryotic ubiquitin-like protein ligase
The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. It catalyses the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation. Group: Enzymes. Synonyms: PafA (ambiguous); Pup ligase; proteasome accessory factor A. Enzyme Commission Number: EC 6.3.1.19. 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-5721; prokaryotic ubiquitin-like protein ligase; EC 6.3.1.19; PafA (ambiguous); Pup ligase; proteasome accessory factor A. Cat No: EXWM-5721.
Pup amidohydrolase
The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis. The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein. Group: Enzymes. Synonyms: dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Enzyme Commission Number: EC 3.5.1.119. 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-4399; Pup amidohydrolase; EC 3.5.1.119; dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase. Cat No: EXWM-4399.
PYR-41
PYR-41 is a selective and cell permeable inhibitor of ubiquitin-activating enzyme E1 with an IC 50 of < 10 μM, with little activity at E2 and E3. Uses: Scientific research. Group: Signaling pathways. CAS No. 418805-02-4. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-13296.
PYR-41
PYR-41 is a ubiquitin-activating enzyme inhibitor (UBE1 inhibitor). PYR-41 blocks ubiquitination reactions but paradoxically leads to the accumulation of high MW ubiquitinated proteins. PYR-41 also mediated cross-linking of specific protein kinases (Bcr-Abl, Jak2) to inhibit their signaling activity. PYR-41 has demonstrated anti-tumor activity in animal studies, partially selective protein cross-linking may represent an alternate approach to affect signal transduction modules and ubiquitin cycle-regulatory proteins for cancer therapy. Synonyms: PYR-41; PYR 41; PYR41. Grades: 0.98. CAS No. 418805-02-4. Molecular formula: C17H13N3O7. Mole weight: 371.305.
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