| Description | Source: MicroorganismIsoelectric point: 6.0Michaelis constant: 1.0×10^-5M (Palmitoyl-CoA)Optimum pH: 8.0~9.0 Fig. 1Optimum temperature: 37~40℃ Fig. 3pH Stability: 6.0~8.5 (25℃, 15hr) Fig. 2Thermal stability: <45℃ (pH 7.5, 15min) Fig. 4Inhibitors: Co2+, Cu2+, Ni2+, Zn2+, NEMSource: MicroorganismIsoelectric point: 6.0Michaelis constant: 1.0×10^-5M (Palmitoyl-CoA)Optimum pH: 8.0~9.0 Fig. 1Optimum temperature: 37~40℃ Fig. 3pH Stability: 6.0~8.5 (25℃, 15hr) Fig. 2Thermal stability: <45℃ (pH 7.5, 15min) Fig. 4Inhibitors: Co2+, Cu2+, Ni2+, Zn2+, NEM, Proclin, SDSEffect of various chemicals: Table 1Reaction:... Read More | Inquire | Ganglioside GT1b is a brain ganglioside. It is composed of a neutral tetra-saccharide core, with one or two sialic acid on the internal galactose and an extra sialic acid on the non-reducing terminal of galactose | IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 protein kinase inhibitor 2 (compound 1) also inhibits IRAK-1, with an IC 50 of <10 µM. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:IRAK4 4 µM (IC 50 )... 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 |