| Description | DDR2 Human Pre-designed siRNA Set A contains three designed siRNAs for DDR2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DDR2 siRNA-1: 5 nmol (HPLC) DDR2 siRNA-2: 5 nmol (HPLC) DDR2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 DDR2 Human Pre-designed siRNA Set A contains three designed siRNAs for DDR2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DDR2 siRNA-1: 5 nmol (HPLC) DDR2 siRNA-2: 5 nmol (HPLC) DDR2 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 | description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many description：Bovine pancreatic deoxyribonuclease I produced recombinantly in yeast, Pichia pastoris, to decrease levels of contaminating RNase and eliminate potential pathogens associated with animal based materials.Bovine pancreas is a rich source of RNase A which is often found in many commercial DNase preparations. Producing DNase I by recombinant means in an organism with much lower levels of endogenous RNase greatly facilitates purification of an enzyme with undetectable levels of RNase. The processes involved in the production and isolation of recombinant DNase I are completely devoid of animal based components which eliminates the possibility of introducing animal derived pathogens into bioprocessing procedures.Animal Free/AF. Recombinant Bovine pancreatic deoxyribonuclease 1 produced in Pichia pastoris. Chromatographically purified. Free of animal derived components, RNases & proteases. A liquid preparation in 5mM Calcium Acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol. Supplied with 10x reaction buffer.Storage Buffer : 5mM calcium acetate, 4mg/ml glycine, pH 5.0 and 50% glycerol.DNase I Reaction Buffer (10X): 500mM Tris-HCl, 10mM MgSO4, 1mM CaCl2, pH 7.8, provided.application：Recombinant DNase I is suitable for such applications as:• Removing genomic DNA from RNA preparations prior to RT-PCR• Degradation of DNA templates after transcription reactions• Removing unwanted DNA from samples prior to Northern blotting• Removing DNA during biopharma and bioprocessing procedures... 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 | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universalPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universal strategy for the identification and purification of proteins derived by recombinant DNA technology. The insertion of a Maltose Binding Protein (MBP) tag creates a stable fusion product that does not interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product... Read More |