| Description | Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, thrombin, and trypsin. Potency is strongly enhanced by heparin. Clinically, reduced levels are indicative of hypercoagulability. Extinction Coefficient: 0.65 Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Purified Native Human Antithrombin III, Human PlasmaBulk Qty Available.Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, thrombin, and trypsin. Potency is strongly enhanced by heparin. Clinically, reduced levels are indicative of hypercoagulability. Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.Athens Research & Technology products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research use only.Product Citation:Perera, Natascha C., Oliver Schilling, Heike Kittel, Walter Back, Elisabeth Kremmer, and Dieter E. Jenne. "NSP4, an elastase-related protease in human neutrophils with arginine specificity. Proceedings of the National Academy of Sciences 109, no. 16 (2012): 6229-6234.Guo C, et al.High-resolution probing heparan sulfate–antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies.Phys Chem Chem Phys. 2015 May 28;17(20):13301-6. doi: 10.1039/c5cp01305d.Tafaleng EN, et al.Induced pluripotent stem cells model personalized variations in liver disease resulting from α1-antitrypsin deficiency.Hepatology. 2015 Jul;62(1):147-57. doi: 10.1002/hep.27753. Epub 2015 Apr 13... 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 | Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the Product DescriptionEndo F1 cleaves Asparagine-linked high mannose and some hybrid oligosaccharides. Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. 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.Molecular weight 32,000 daltonsContents60 µl aliquot of enzyme (1 U) in 20 mM Tris-HCl, pH 7.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium phosphate, pH 5.5Specific ActivityDefined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured Ribonuclease B (RNase B) in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved RNase B migrates faster).FormulationThe enzyme is provided as a sterile-filtered solution in 20 mM Tris-HCl, pH 7.5StabilitySeveral days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly. SpecificityEndo F1 cleaves Asparagine-linked high mannose or hybrid oligosaccharides. 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. Quality & PurityEndo F1 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.Directions for use1. 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 5.53. Add 2.0 µl of Endo F1 to the reaction. Incubate 1 hour or more at 37°C.Monitor cleavage by SDS-PAGE... Read More | Inquire | Inquire |