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| Company | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation |
| Item | α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens | Fumarate hydratase-IN-2 sodium salt | PHM 27 (human) TFA | SHP2 protein degrader-2 | Trypsin from bovine pancreas(0.22 µm,Filtered) |
| Catalog Number | N755087 | F658719 | P407257 | S648891 | T128775 |
| Price | Supplier Page | Supplier Page | Supplier Page | Supplier Page | Supplier Page |
| Quantity | 1T | 10mg, 5mg, 50mg, 1mg, 25mg | 50mg, 10mg, 100mg, 5mg, 25mg, 1mg | 50mg, 10mg, 100mg, 5mg, 25mg, 1mg | 50mg |
| Type | Proteins | Chelating Agents & Ligands | Chelating Agents & Ligands | Chelating Agents & Ligands | Proteins |
| Description | Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α(2→6), α(2→3), α(2→8), and α(2→9) linkages (affinity in the order given). Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α(2→6), α(2→3), α(2→8), and α(2→9) linkages (affinity in the order given). Branched sialic acids may also be cleaved with the use of high concentrations of enzyme and prolonged incubations. Desialylated glycoproteins may then be further characterized by treatment with various exoglycosidases resulting in partial or complete O-deglycosylation. SDS-PAGE and MALDI-TOF MS are typically utilized in purification, structural analysis, and sequencing process. These techniques also remove heterogeneity and charge from the glycoprotein... Read More | Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity.Appearance:SolidIC50& Target:Ki: 4.5 µM (Fumarate hydratase)Biological Activity:Fumarate hydratase-IN-2 sodium salt (Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity.Appearance:SolidIC50& Target:Ki: 4.5 µM (Fumarate hydratase)Biological Activity:Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity... Read More | Inquire | SHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has beenSHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has been degraded) values of 2.6 nM and 6.0 nM for MV4;11 and KYSE520 cells, respectively. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |
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