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| Company | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation |
| Item | CAGE1 Human Pre-designed siRNA Set A | Glukagon (19-29) (human),TFA | Lactate Dehydrogenase from Recombinant, rabbit muscle produced in E. coli | Orexin A (bovine, human, mouse, rat) | Recombinant Carboxypeptidase B |
| Catalog Number | C1465214 | G321154 | L128329 | O275498 | R141077 |
| Price | Supplier Page | Supplier Page | Supplier Page | Supplier Page | Supplier Page |
| Quantity | 1Set | 250mg, 5mg, 50mg, 10mg, 25mg | 5KU, 1KU, 25KU | 100µg, 500µg, 1mg | 100mg, 5mg, 50mg, 1mg, 10mg |
| Type | Bioactive Small Molecules | Chelating Agents & Ligands | Proteins | Chelating Agents & Ligands | Chelating Agents & Ligands |
| Description | CAGE1 Human Pre-designed siRNA Set A contains three designed siRNAs for CAGE1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CAGE1 siRNA-1: 5 nmol (HPLC) CAGE1 siRNA-2: 5 nmol (HPLC) CAGE1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:CAGE1 Human Pre-designed siRNA Set A contains three designed siRNAs for CAGE1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CAGE1 siRNA-1: 5 nmol (HPLC) CAGE1 siRNA-2: 5 nmol (HPLC) CAGE1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Inquire | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Store at -20°C. Store under desiccating conditions. The product can be stored for up to 12 months | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3)Less than 10ppm of recombinant trypsin... Read More |
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