| Description | HLA-DOB Human Pre-designed siRNA Set A contains three designed siRNAs for HLA-DOB gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HLA-DOB siRNA-1: 5 nmol (HPLC) HLA-DOB siRNA-2: 5 nmol (HPLC) HLA-DOB siRNA-3: 5 nmol (HPLC) siRNA HLA-DOB Human Pre-designed siRNA Set A contains three designed siRNAs for HLA-DOB gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HLA-DOB siRNA-1: 5 nmol (HPLC) HLA-DOB siRNA-2: 5 nmol (HPLC) HLA-DOB 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 | 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent moiety 4-methylumbelliferyl (4-MU). This 4-Methylumbelliferyl α-L-iduronide form is the free acid, which offers a considerable weight for weight advantage over the 4-MU iduronide salt in terms of its application dose.:For further studies, use α-L-iduronidase gene silencing:siRNA and shRNA:reagents and α-L-iduronidase gene editing:CRISPR:knockout and activation products... Read More | Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However, for optimal results, denaturation of the glycoprotein is recommended.Contents60 µl aliquot of enzyme (0.3 U) in 10 mM sodium acetate 25mM NaCl, pH 4.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium acetate, pH 4.5Molecular weight 32,000 daltonsSpecific Activity Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured porcine fibrinogen in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved fibrinogen migrates faster).Formulation The enzyme is provided as a sterile-filtered solution in 10 mM sodium acetate, 25mM NaCl, pH 4.5Specificity Endo F2 cleaves Asparagine-linked biantennary and high mannose glycans (at a 40X reduced rate). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However for optimal results, denaturation of the glycoprotein is recommended.Quality & Purity Endo F2 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.Stability Several days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly.Directions for use 1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water. 2. Add 10 µl 5x Reaction Buffer 4.5 3. Add 2.0 µl of Endo F2 to the reaction. Incubate 1 hour at 37°C. Monitor cleavage by SDS-PAGEThe production host strain has been extensively tested and does not produce any detectable glycosidases... Read More | Store at +4°C. Store under desiccating conditions. The product can be stored for up to 12 months | Tankyrase-IN-2 (compound 5k) is a potent, selective, and orally active tankyrase inhibitor ( IC 50 s of 10, 7, and 710 nM for TNKS1, TNKS2 as well as PARP1, respectively). Tankyrase-IN-2 has favorable physicochemical profile and pharmacokinetic properties modulating Wnt pathway activity in a Tankyrase-IN-2 (compound 5k) is a potent, selective, and orally active tankyrase inhibitor ( IC 50 s of 10, 7, and 710 nM for TNKS1, TNKS2 as well as PARP1, respectively). Tankyrase-IN-2 has favorable physicochemical profile and pharmacokinetic properties modulating Wnt pathway activity in a colorectal xenograft modelIn VitroTankyrase-IN-2 (1-10000 nM; 24 hours) leads to a dose-dependent increase of tankyrase protein abundance with an EC 50 of 320 nM in DLD1 cells. This is in the same potency range as the value for axin2 increase (EC 50 =319 nM). MCE has not independently confirmed the accuracy of these methods. They are for reference only.IC50& Target:IC50: 10 nM (TNKS1), 7 nM (TNKS2), 710 nM (PARP1)... Read More |