| Description | DMXL1 Human Pre-designed siRNA Set A contains three designed siRNAs for DMXL1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DMXL1 siRNA-1: 5 nmol (HPLC) DMXL1 siRNA-2: 5 nmol (HPLC) DMXL1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:DMXL1 Human Pre-designed siRNA Set A contains three designed siRNAs for DMXL1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components DMXL1 siRNA-1: 5 nmol (HPLC) DMXL1 siRNA-2: 5 nmol (HPLC) DMXL1 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 | Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towardsArachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towards ?-D-Gal(1-3)-D-galNAc. It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose. PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa.● Ultrapure quality ● Strong anti-T activity ● Sugar specificity: ?-D-Gal-(1-3)-D-GalNAc ● Agglutinates rabbit erythrocytes at < 0.1 µg/ml after trypsin treatment of the cells ● Lyophilized powderProbe in histochemistry and immuno-histochemistry;Human erythrocyte/lymphocyte studies... Read More | Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically highly purified class I and class II collagenase (1).Largely free from clostripain, trypsin-like protease and neutral protease.Vial contains not less than 2000 PZ U collagenase.Activity (Wünsch): ≥ 3.00 U/mgEndotoxin: ≤ 10.0 EU/mg (Ph. Eur.)(Clostridiopeptidase A)EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1]ApplicationCollagenase NB 1 is, mostly in combination with Neutral Protease NB, suitable for cell isolation from several tissue types.References and DefinitionsUnit definition: Collagenase: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmole 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1.Endotoxin: Ph. Eur. (1 Endotoxin Unit is equal to 1 International Unit of a WHO approved reference standard endotoxin (RSE)).References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51... 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 | Lipoprotein Lipase Activator is a cell-permeable benzylphosphonate derivative that selectively induces lipoprotein lipase (LPL) mRNA and protein levels, but does not exhibit PPARα or PPARγ agonistic activities. Lipoprotein Lipase Activator lowers serum lipid levels and plasma triglyceridesLipoprotein Lipase Activator is a cell-permeable benzylphosphonate derivative that selectively induces lipoprotein lipase (LPL) mRNA and protein levels, but does not exhibit PPARα or PPARγ agonistic activities. Lipoprotein Lipase Activator lowers serum lipid levels and plasma triglycerides with concomitant elevation in high-density lipoprotein cholesterol (HDL-C) in animal models. Lipoprotein Lipase Activator also induces fatty acid oxidation related enzymes, lowers free fatty acids (FFA), and minimizes fat accumulation. Also reported to suppress the plasma levels of TNF-a and COX-2 and displays anti-tumor properties... Read More |