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| Product | Description | |
|---|---|---|
| Aspergillus niger Lipase, Food Grade | An enzyme capable of hydrolyzing fats and oils. Typically used in cheese production. Suitable for other food grade applications. Applications: Dietary supplements. Group: Zymogens. Synonyms: Lipase-AN. Lipase. Appearance: powder or liquid. Source: Aspergillus niger. Lipase Feed Grade Enzymes; digestion and utilization of fat; for Fish; piglet; fowl; Feed;Lipase; Feed Grade Enzymes; Lipase Feed Grade Enzymes; FEED-2321. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1028. |  |
| Bovine factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig... activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. CAS No. 9001-28-9. Purity: >95% by SDS-PAGE. Factor IX. Mole weight: 55400. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine factor IX; Factor IX. Pack: 100 ug. Cat No: CZY-003. | |
| Bovine glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...hich remain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine glu-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-015. | |
| Bovine Plasminogen | Purified from freshly collected bovine plasma. The protein purity is determined by SDS-PAGE and shows no reduction upon incubation with 2-mercaptoethanol. No Plasmin activity is detected using chromogenic substrate S-2251. Plasminogen is activated to the serine protease plasmin via urokinase, streptokinase or tissue plasminogen activator. Group: Zymogens. Purity: >94% by SDS-PAGE. Plasminogen. Mole weight: 90,000-94,000. Stability: 30 months. Storage: 2-8°C. Source: Bovine. Bovine Plasminogen; Plasminogen. Pack: 1mg. Cat No: CZY-030. | |
| Bovine Protein C | The vitamin K-dependent zymogen, protein C, is synthesized in the liver as a single chain polypeptide and is subsequently converted to a disulfide linked heterodimer, by removal of a dipeptide (Lys-146 and Arg-147) from the precursor molecule. Trace quantities of the single chain form have been observed in plasma. The light chain, which is responsible for the calcium dependent binding of protein C to phospholipid vesicles, contains 11 γ-carboxyglutamic acid (gla) residues, 1 b-hydroxyaspartic acid residue, and 2 epidermal growth factor (EGF) homology domains. The serine protease catalytic triad is located in the heavy chain. Human protein C is susceptible to proteolytic cleavag...g the proteolytic inactivation of factors Va and VIIIa. APC also contributes to the fibrinolytic response by complex formation with plasminogen activator inhibitors.Bovine protein C is prepared from fresh citrated bovine plasma by a modification of the Walker procedure, as described by Haley et al. Human protein C is prepared from fresh frozen citrated human plasma using a combination of immunoaffinity chromatography, and conventional techniques. Protein C is provided in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a chromogenic substrate based assay. Group: Zymogens. Purity: >95% by SDS-PAGE. Prote | |
| Cellobiase for Alcohol Fermentation (Food Grade) | Cellobiase is an enzyme which can hydrolyze the substrate with β- glucosidic bond. It can be used in the alcohol fermentation. It can hydrolyze the β-D-glucosidic bond of reducing end, which the acquisitions are isomalto-oligosaccharide, sugar ester, glycopeptide and etc. Applications: Enzyme by alcohol fermentation. Group: Zymogens. Synonyms: Cellobiase; enzyme for alcohol fermentation; Cellobiase for Alcohol Fermentation. CAS No. 9033-6-1. Cellobiase. Activity: 5,000u/ml. Storage: Should be stored in a cool place avoiding high temperature. Powder: 12 months at 25°C, activity remain >90%. Increase dosage after shelf life. Form: Liquid. Cellobiase; enzyme for alcohol fermentation; Cellobiase for Alcohol Fermentation. Pack: 25kgs/bag, 1.125kgs/bag. Cat No: ASE-003. | |
| Glucose Oxidase (Food Grade) | Glucose Oxidase is made from selected strains of Aspergillus niger using submerged fermentation, extraction and refining techniques. It has a high conversion rate of starchy substrates into fermentable sugars. This product can hydrolyze α-D-1, 4 glucosidic bonds from the non-reducing end of starch one after. This enzyme also hydrolyzes the α-D-1, 6 glucoside branch bonds of starch and cleaves the α-1, 3 bonds, releasing glucose. It is our excellent glucoamylase that has been especially designed for saccharification in baking enzyme. Applications: Baking enzyme. Group: Zymogens. Synonyms: glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucos. CAS No. 9001-37-0. GOD. Activity: 10,000u/g. Storage: Should be stored in a cool place avoiding high temperature. Powder: 12 months at 25°C, activity remain >90%. Increase dosage after shelf life. Form: Powder. Source: Aspergillus niger. glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; glucose oxidase enzyme; GOx; notatin; glucose oxidase. Pack: 25kgs/bag, 1.125kgs/bag. Cat No: BAK-001. | |
| Human Coagulation Factor VII | Human factor VII is a single chain, vitamin K-dependent, plasma glycoprotein which is synthesized in the liver. Prior to secretion into the blood, post translational modification by a vitamin K-dependent carboxylase produces ten-carboxyglutamic acid (gla) residues located in the NH2-terminal portion of the molecule, which facilitate cell membrane binding. Factor VII is proteolytically activated to the serine protease, factor VIIa, during coagulation. Factor VII can be activated by thrombin, factor IXa, factor Xa or factor XIIa. The activation results in cleavage of the single chain molecule on the COOH-terminal side of arginine-152, to produce an NH2-terminal derived light chai...nzyme complex catalyzes the conversion of both factor IX to factor IXa and factor X to factor Xa. The cDNA for factor VII has been isolated and the nucleotide sequence determined. Factor VII shares extensive sequence homology with other serine proteases including factor IX, factor X and protein C.Human factor VII is purified using a combination of conventional techniques and immunoaffinity chromatography. The purified protein is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured in a factor VII clotting assay. Group: Zymogens. CAS No. 9001-25-6. Purity: >95% by SDS-PAGE. Factor VII. Mole weigh | |
| Human Factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig...lly activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. CAS No. 9001-28-9. Purity: >95% by SDS-PAGE. Factor IX. Mole weight: 55000. Stability: 12 months. Storage: -20°C. Source: Human. Human Factor IX; Factor IX. Pack: 100 ug. Cat No: CZY-002. | |
| Human glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p... a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. CAS No. 9001-91-6. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 88000. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-011. | |
| Human glu-Plasminogen CHOI | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of...remain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen CHOI; Plasminogen. Pack: 1 mg. Cat No: CZY-012. | |
| Human glu-Plasminogen CHOII | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction o...emain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen CHOII; Plasminogen. Pack: 1 mg. Cat No: CZY-013. | |
| Human Kininogen (Single Chain High Molecular Weight) | High Molecular Weight Kininogen (HK) is a non-enzymatic cofactor of the contact activation system. HK is thought to have two functions in the contact activation system. First, HK links Prekallikrein to a negatively charged surface thereby allowing activation of Kallikrein by surface bound Factor a-XIIa. HK also forms a complex with Factor XI and accelerates its activation to XIa by a-XIIa. Additionally HK serves as a source of Bradykinin, a potent vasoactive peptide important in hypotension studies. The protein purity is determined by SDS-PAGE. Group: Zymogens. Purity: >95% by SDS-PAGE. Kininogen. Mole weight: 120000. Storage: 2-8°C. Source: Human. Human Kininogen (Single Chain High Molecular Weight); Kininogen. Pack: 1mg. Cat No: CZY-028. | |
| Human Kininogen (Two Chain High Molecular Weight) | ERL offers the two chain Kinin-free form of Kininogen. This is prepared by Kallikrein digestion of Kininogen which is then repurified to remove traces of Kallikrein. Group: Zymogens. Purity: >95% by SDS-PAGE. Kininogen. Mole weight: 110000. Storage: 2-8°C. Source: Human. Human Kininogen (Two Chain High Molecular Weight); Kininogen. Pack: 1mg. Cat No: CZY-029. | |
| Human lys-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...ently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 83000. Stability: 12 months. Storage: -20°C. Source: Human. Human lys-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-014. | |
| Human Prekallikrein | Purified from fresh frozen human plasma. Human Prekallikrein is a single chain gamma globulin glycoprotein that participates in the early phase of contract activation, kinin formation and fibrinolysis. Prekallikrein purity is determined by SDS-PAGE and shows no reduction upon incubation with 2-mercaptoethanol. Activity is determined via clotting assay. Group: Zymogens. Purity: >95% by SDS-PAGE. Prekallikrein. Mole weight: 86000. Storage: 2-8°C. Source: Human. Human Prekallikrein; Prekallikrein. Pack: 1mg. Cat No: CZY-027. | |
| Human Protein C | The vitamin K-dependent zymogen, protein C, is synthesized in the liver as a single chain polypeptide and is subsequently converted to a disulfide linked heterodimer, by removal of a dipeptide (Lys-146 and Arg-147) from the precursor molecule. Trace quantities of the single chain form have been observed in plasma. The light chain, which is responsible for the calcium dependent binding of protein C to phospholipid vesicles, contains 11 γ-carboxyglutamic acid (gla) residues, 1 b-hydroxyaspartic acid residue, and 2 epidermal growth factor (EGF) homology domains. The serine protease catalytic triad is located in the heavy chain. Human protein C is susceptible to proteolytic cleavag...ng the proteolytic inactivation of factors Va and VIIIa. APC also contributes to the fibrinolytic response by complex formation with plasminogen activator inhibitors.Bovine protein C is prepared from fresh citrated bovine plasma by a modification of the Walker procedure, as described by Haley et al. Human protein C is prepared from fresh frozen citrated human plasma using a combination of immunoaffinity chromatography, and conventional techniques. Protein C is provided in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a chromogenic substrate based assay. Group: Zymogens. CAS No. 42617-41-4. Purity: >95 | |
| Mouse factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig...factor VIIIa/IXa/Ca2+/phospholipid) which proteolytically activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. Purity: >95%. Factor IX. Mole weight: 55000. Storage: -20°C. Source: Mouse. Mouse factor IX; Factor IX. Pack: 50 ug. Cat No: CZY-032. | |
| Mouse glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...tly associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 88000. Stability: 12 months. Storage: -20°C. Source: Mouse. Mouse glu-Plasminogen; Plasminogen. Pack: 100 ug. Cat No: CZY-016. | |
| Native Bovine α-Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748. | |
| Native Bovine Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Group: Zymogens. Synonyms: chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. CAS No. 9035-75-0. Purity: Purified, Five times crystallized, electrophoretically homogeneous. Chymotrypsinogen A. Activity: Activates to at least 45 units per mg protein. Stability: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bovine Pancreas. Species: Bovine. chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. Cat No: NATE-0134. | |
| Native Human Pepsinogen I | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Research life science. Group: Zymogens. Synonyms: Pepsinogen I. Pepsinogen. Activity: >96%. Storage: 4°C. Source: Human Stomach. Species: Human. Pepsinogen I. Cat No: NATE-0545. | |
| Native Human Pepsinogen II | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Research life science. Group: Zymogens. Synonyms: Pepsinogen II. Pepsinogen. Activity: >96%. Storage: 4°C. Source: Human Stomach. Species: Human. Pepsinogen II. Cat No: NATE-0546. | |
| Native Porcine Pepsinogen | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Pepsin is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides. it was discovered in 1836 by theodor schwann who also coined its name from the greek word π?ψΙ? pepsis, meaning "digestion" (from π?πτεΙν peptein "to digest"). it was the first enzyme to be discovered, and, in 1928, it became one of the first enzymes to be crystallized, by john h. northrop. ...rticular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the intestinal lining. pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Group: Zymogens. Synonyms: pepsinogen; 9001-10-9; Pepsinogen from hog stomach. CAS No. 9001-10-9. Pepsinogen. Activity: ~3,000 units/mg protein (after activation to pepsin at pH 2.0 at 25°C). Storage: 2-8°C. Form: lyophilized powder. Source: Porcine Stomach. Species: Porcine. pepsinogen; 9001-10-9; Pepsinogen from hog stomach. Cat No: NATE-0547. | |
| ω-Transaminases | synthesis of chiral amines from ketones and ketoacids. Group: Zymogens. Synonyms: ω-Transaminases; ATA. Form: 1. Enzyme Powder: 58 items*50mg / item, or other quantity2. Screening Kit I: 58 items*1mg / item3. Screening Kit II: 39 items*1mg / item. ω-Transaminases; ATA; Screening Kit; library of enzyme; enzyme library. Cat No: ENLC-002. | |
| Abelacimab | Abelacimab (MAA868) is a fully human IgG1 monoclonal antibody that binds with high affinity to the catalytic structural domain of FXI and locks it in the zymogen conformation, thereby preventing its activation by FXIIa or thrombin. Abelacimab can be used in thromboembolic disease studies [1] [2]. Uses: Scientific research. Group: Inhibitory antibodies. Alternative Names: MAA868. CAS No. 2098724-83-3. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P99415. |  |
| Biotinylated Transglutaminase from Human, Proenzyme (Zymogen) | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 3 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. biotinylated transglutaminase 3 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transgl...]. Appearance: Liquid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Transglutaminase is a Ca2+-dependent enzyme. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 100 ug. Cat No: NATE-173 | |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| Bovine Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fa...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| cathepsin D | Occurs intracellularly, in lysosomes. A zymogen form is known. In peptidase family A1 (pepsin A family). Group: Enzymes. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4287; cathepsin D; EC 3.4.23.5; 9025-26-7. Cat No: EXWM-4287. | |
| Cholesterol esterase, Pseudomonas | Cholesterol esterase, Pseudomonas is an enzyme that hydrolyzes cholesterol ester to cholesterol and free fatty acid in the intestinal lumen. Cholesterol synthesized in the acinar cells and is stored in zymogen granules. Cholesterol esterase is also known as bile salt-stimulated lipase and carboxy ester lipasea, acts function for acceleration of cholesterol absorption [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9026-00-0. Pack Sizes: 100 U. Product ID: HY-P2879. | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| Enterokinase from Human, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. > 90% (sds-page), > 90% (hplc), cell culture tested. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 108.7 kDa. Activity: Type I, > 20 units/mg protein. Form: Lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 1 mM Calcium Chloride. Source: CHO cells. Species: Human. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0227. | |
| gastricsin | Formed from progastricsin, apparently in the gastric juice of most vertebrates. In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum. Seminal plasma contains a zymogen that is immunologically identical with progastricsin. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: pepsin C; pig parapepsin II; parapepsin II. Enzyme Commission Number: EC 3.4.23.3. CAS No. 9012-71-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4267; gastricsin; EC 3.4.23.3; 9012-71-9; pepsin C; pig parapepsin II; parapepsin II. Cat No: EXWM-4267. | |
| Human Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fac...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Human Factor XI | Factor XI is a plasma glycoprotein which circulates in a non-covalent complex with high molecular weight kininogen. The mature molecule is synthesized in the liver and is a two-chain homodimer with a molecular weight of approximately 160,000. It is estimated that 5% of the total mass is attributable to carbohydrate. The two identical monomers have molecular weights of 80,000, and are joined together by disulfide bonds. Thus by SDS-PAGE analysis, factor XI appears as a single band both non-reduced (Mr=160,000), and reduced (Mr=80,000).Factor XI circulates as a zymogen and requires proteolytic activation to acquire serine protease activity. The conversion of factor XI to factor XIa is ...activity or antigen levels. This latter observation may be related to the ability of the tissue factor/factor VIIa complex to also activate factor IX to IXa.Historically, factor XI has been difficult to purify due to its relatively low concentration in plasma, and its susceptibility to proteolysis. Factor XI is purified from fresh frozen plasma that is stabilized by added inhibitors. The plasma is first treated with BaCl2 to remove the vitamin K-dependent proteins, and factor XI is then isolated by affinity chromatography. A final chromatography step on heparin sepharose yields a homogeneous preparation of intact factor XI. The finished product is supplied in 50% (vol/vol) glycerol/H2 | |
| Human Factor XII | Factor XII (XII) (Hageman Factor) is a single chain (Mr=78,000) glycoprotein zymogen that circulates in plasma at a concentration of 40 ug/ml. Reciprical activation of XII to the active serine protease factor XIIa (XIIa) by kallikrein is central to initiation of the intrinsic coagulation pathway. Surface bound α-XIIa in turn activates factor XI to XIa. Secondary cleavage of α-XIIa by kallikrein yields β-XIIa, which catalyzes solution phase activation of kallikrein, factor VII and the classical complement cascade.The ability of a variety of negatively charged substances, both physiological and nonphysiological to promote XII activation and, thus, initiation of the int...ain (Mr=28,000) contains the catalytic triad (His-40, Asp-89, Ser-191), while the NH2-terminal heavy chain (Mr=52,000) conatins the anionic surface binding portion of the molecule. A secondary cleavage of α-XIIa by kallikrein outside the disulfide bond yields β-XIIa (XIIf, BHFa, HFf, hageman factor fragments) (Mr=28,000), which no longer binds anionic surfaces. β-XIIa can activate prekallikrein, but has little procoagulant activity. Several other minor intermediate forms of XIIa are indicated in the figure above.Inhibitors of XIIa include C1-INH, α2-antiplasmin, α2-macroglobulin and antithrombin III. At physiological concentrations, the relative effectiven | |
| Human Factor XIII | Factor XIII is the zymogenic form of the glutaminyl-peptide g-glutamyl transferase factor XIIIa (fibrinoligase, plasma transglutaminase, fibrin stabilizing factor, E.C. 2.3.2.13). Factor XIII is unique among transamidases in that it is a zymogen in vivo. Factor XIII is found both extracellularly in plasma and intracellularly in platelets, megakaryocytes, monocytes, placenta, uterus, liver and prostrate tissues. Plasma factor XIII is synthesized in the liver and circulates as a tetramer (Mr=320,000), composed of 2 pairs of nonidentical subunits (A2B2). The intra-cellular forms are synthesized in the tissues where they reside as dimers (Mr=146,000) of 2 identical A chains (A2). The A ...nly after the Ca2+ (Kd=10-3M) and fibrin(ogen) (Kd=10-8M) dependent dissociation of the B subunit dimer from the A2' dimer.In the coagulation cascade, factor XIIIa functions to stabilize the fibrin clot by crosslinking the a and g-chains of fibrin. Other proteins known to be substrates for Factor XIIIa which may be hemostatically important include fibronectin, α2-antiplasmin, collagen, factor V, von Willebrand Factor and thrombospondin.Factor XIII is purified from fresh frozen human plasma by a modification of the procedures described by Folke and Lorand involving barium citrate, ammonium sulfate and glycine precipitations, ion exchange chromatography and gel filtration. Factor | |
| Human gla-domainless Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor ...e prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Mouse Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fac...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Native Bovine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Enterokinase is a highly specific serine protease that is used for the removal of the flag peptide from n-terminal and met-n-terminal fusion proteins. it does not remove the c-terminal flag. Applications...ytic activation of trypsin from trypsinogen. enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. removes flag peptide from n-terminal and met-n-terminal fusion proteins. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa (consisting of 115kDa and 35kDa subunits.). Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: powder. Source: Bovine intestine. Species: Bovine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0224. | |
| Native Calf Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. for the processing of recombinant proteins, the desired protein is fused with enterokinase recognition sequence. after purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa. Storage: Store at 2-8°C. Form: Lyophilized. Source: Calf intestine. Species: Calf. enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Cat No: NATE-0872. | |
| Native Human Protein C | Protein C is a plasma, vitamin κ-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating Factors Va and VIIIa. The Protein C anticoagulant pathway is triggered when thrombin binds to the endothelial cell proteoglycan, thrombomodulin. This complex, which cannot clot blood, is a potent activator of the protein C zymogen. Activation involves the release of a dodecapeptide from the N-terminal domain of the heavy chain. The activated Protein C (APC) then binds to protein S on cell surfaces and inactivates the coagulation factors Va and VIIIa by proteolysis. APC has also been shown to bind to receptors on the endothelium of large blood vessels. Group: Enzymes. Synonyms: PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothr. Enzyme Commission Number: EC 3.4.21.69. CAS No. 42617-41-4. Purity: > 90% (SDS-PAGE). Protein C. Mole weight: heavy chain mol wt 41 kDa; light chain mol wt 21 kDa. Storage: -20°C. Form: Lyophilized powder from 20 mM Tris-HCl, pH 7.4, containing 0.1 M NaCl. Source: Human plasma. Species: Human. PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC; 42617-41-4; EC 3.4.21.69; PROC1. Cat No: NATE-0626. | |
| Native Human Urokinase | Urokinase is a serine protease (EC 3.4.21.73). Urokinase was originally isolated from human urine, but is present in several physiological locations, such as blood stream and the extracellular matrix. The primary physiological substrate is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. Activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. This links urokinase to vascular diseases and cancer. Urokinase from human urine. Group: Enzymes. Synonyms: Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Enzyme Commission Number: EC 3.4.21.73. CAS No. 9039-53-6. Purity: Purity by SDS Electrophoresis ? 95 %. uPA. Activity: > 500 units/mg protein. Form: Lyophilized from 1 mL of 50 mM Tris-HCl, pH 7.4 with 100 mM NaCl, 0.1% PEG 6000, and 200 mM mannitol. Source: Human urine. Species: Human. Urokinase; EC 3.4.21.73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Cat No: PHAM-262. | |
| Native Porcine Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.21.36. CAS No. 39445-21-1. ELA1. Activity: Type I, > 15 units/mg; Type II, > 4.0 units/mg protein; Type III, > 1 units/mg protein (biuret). Storage: -20°C. Form: Type I, white powder; Type II, Type III, lyophilized powder, Contains sodium carbonate. Source: Porcine pancreas. Species: Porcine. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Pack: Package size based on protein content. Cat No: NATE-0211. | |
| Native Porcine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase from porcine intestine has been used in a study to report a new experimental model of the anomalous pancreatico-biliary junction. enterokinase from porcine intestine has also ...peptide. the enzyme from creative enzymes has been used for the activation of trypsinogen in order to measure the activity of trypsin in hog pancreas. the study showed that antimicrobial treatment reduces intestinal microflora and improves protein digestive capacity without changes in villous structure of weanling pigs. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Porcine intestine. Species: Porcine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0225. | |
| Native Pseudomonas aeruginosa Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.24.26. CAS No. 9004-6-2. Purity: > 90% by SDS-PAGE. ELA1. Mole weight: 33000. Stability: Following reconstitution, aliquot and freeze (-20°C) for long-term storage or refrigerate (4°C) for short-term storage. Stock solutions are stable for up to 1 week at 4°Cor for up to 2 months at-20°C. Appearance: Lyophilized. Storage: Storage at-20°C. Source: Pseudomonas aeruginosa. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Cat No: NATE-0212. | |
| Pro-Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Single chain Urokinase-type plasminogen activator; s. Purity: > 90% by SDS-PAGE. Pro-Urokinase. Mole weight: 49.3 kDa. Activity: >1200 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Single chain Urokinase-type plasminogen activator; scuPA; Urokinase-type Plasminogen Activator uPA; PLAU; Pro-Urokinase. Cat No: NATE-1689. | |
| Transglutaminase from Mouse, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant mouse transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutaminase; EC ...ng to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Biotinylated-transglutaminase is a Ca2+-dependent enzyme. Source: Insect cells. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltra | |
| Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Two chain urokinase-type plasminogen acti. Enzyme Commission Number: EC 3.4.21.73. Purity: > 90% by SDS-PAGE. uPA. Mole weight: 49.3 kDa. Activity: >1500 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Two chain urokinase-type plasminogen activator; tcuPA; PLAU; ATF; UPA; URK; u-PA; BDPLT5; QPD; Urokinase. Cat No: NATE-1690. | |
| Urokinase, Human urine | Urokinase (peptidolytic) (EC 3.4.21.73) is a serine protease, an inactive form (zymogen) of the serine protease plasminogen. Activation of plasmin triggers a proteolytic cascade reaction, which in turn participates in thrombolysis or extracellular matrix degradation, implicated in vascular disease and cancer-related research [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Urokinase-type plasminogen activator; Uronase; Win 22005; Win-Kinase. CAS No. 9039-53-6. Pack Sizes: 1 mg; 5 mg. Product ID: HY-108904. | |
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