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Product information "Heparin sodium salt from porcine intestinal mucosa"
Heparin is a polysaccharide classified as mucopolysaccharide or glycosaminoglycan. In the organism, it is especially formed and stored in mast cells of various mammalian tissues such as liver, lung and mucous membrane. Heparin is mainly isolated from bovine lung, or pig intestine (intestinal mucosa).
Heparin is mainly responsible for delayed blood clotting. It enhances the antithrombin-mediated inactivation of proteases in the clotting pathway. Therefore, it is also often used as an anticoagulant in blood sampling. Thus, it binds to antithrombin III, a naturally occurring plasma protease inhibitor, thereby increasing the rate at which antithrombin III (AT-III) inhibits the coagulation of coagulating proteases, such as factor Xa or thrombin.
Heparin from Genaxxon bioscience is derived from porcine intestinal mucosa (as sodium salt, specific activity >150 units/mg). It is lyophilized and stabilizer-free. Common concentrations are 5000 units/mL. Thus, about 34 mg should be reconstituted with 5mL ultrapure water and then sterile filtered.
In solution, heparin is stable at +2°C to +8°C for up to 2 years, when previously filtered through a 0.2mm sterile filter. CAUTION: Microorganisms rapidly degrade heparin, as they use the polysaccharide side chains as a source of carbon for their own growth.
Specifications:
Appearance: white to off-white powder
Specific activity: >150 units/mg dry weight
Solubility (1%, H2O): clear, colourless
Loss on drying: max. 8%
Source:
porcine intestinal mucosaSafety Information:
Classification:
Documents:
CertificateThe stability of Heparin in solutions (500 units/mL) was examined by Tunbbridge LJ, et al. He was able to show that Heparin solutions do loss their activity much faster if stored in glass compared to plastic bottles. It might be that this loss of acitivity depends on the higher affinity of Heparin to glass surfaces. However, once diluted, heparin should not be stored in glass containers.
Accessory Items
Accutase® as a cell detachment solution of proteolytic and collagenolytic enzymes useful for the routine detachment of cells from standard tissue culture plastic ware and adhesion coated plastic ware. The reagent is useful for creating single cell suspensions from clumped cell cultures for accurate cell counting, detachment of cells from primary tissue. It is much better suited for cell detachment than trypsin. Proven effective in detaching primary fibroblasts, endothelial cells, neurons, tumor cell lines, and insect cells. Accutase® does not contain mammalian or bacterial derived products. For that reason Accutase® virus or endotoxin contaminations are excluded. Once thawed Accutase® can be used for about 1 week if stored at +2°C to +8°C. Shelf-life at -20°C is 12 months. Note: Accutase is a registered trademark of Innovative Cell Technologies, Inc.
Accessory Items
Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Type II Collagenase is recommended for the preparation of cells from liver, bone, thyroid gland, heart and salivary gland and has a specific activity of >180 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).
Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Collagenase type IV has low tryptic, high collagenase and normal clostripain activity. Type I Collagenase is recommended for cell preparation from epithelial, liver, lung tissue, tissue of the suprarenal gland and adipose tissue. The specific activity of >900 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).
Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Collagenase type III shows normal Collagenase, but very low proteolytic activity. Type III Collagenase is recommended for preparation of cells from mamary gland and fetal cells and has a specific activity of 100 to 250 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).