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| Product | Description | |
|---|---|---|
| limulus clotting enzyme | From the hemocyte granules of horseshoe crabs Limulus and Tachypleus. Proclotting enzyme is activated by limulus clotting factor. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: clotting enzyme. Enzyme Commission Number: EC 3.4.21.86. 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-4178; limulus clotting enzyme; EC 3.4.21.86; clotting enzyme. Cat No: EXWM-4178. |  |
| Boc-Ile-Glu-Gly-Arg-AMC | Boc-IEGR-AMC is a specific, highly fluorogenic substrate for clotting enzyme factor Xa (coagulation factor Xa). Synonyms: Boc-ile-glu-gly-arg-7-amido-4-methylcoumarin; 7-(Nalpha-tert-butyloxycarbonyl-L-isoleucyl-L-glutamylglycyl-L-arginyl)amino-4-methylcoumarin. Grades: >97%. CAS No. 65147-06-0. Molecular formula: C34H50N8O10. Mole weight: 730.81. |  |
| carboxypeptidase U | Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Enzyme Commission Number: EC 3.4.17.20. CAS No. 156621-18-0. 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-4073; carboxypeptidase U; EC 3.4.17.20; 156621-18-0; arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Cat No: EXWM-4073. | |
| chymosin | Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Found among mammals with postnatal uptake of immunoglobulins. In peptidase family A1(pepsin A family). Group: Enzymes. Synonyms: rennin (but this should be avoided since it leads to confusion with renin). Enzyme Commission Number: EC 3.4.23.4. CAS No. 9001-98-3. Rennin. 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-4276; chymosin; EC 3.4.23.4; 9001-98-3; rennin (but this should be avoided since it leads to confusion with renin). Cat No: EXWM-4276. | |
| limulus clotting factor B | From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor B is activated by limulus clotting factor C. In peptidase family S1 (trypsin family). Group: Enzymes. Enzyme Commission Number: EC 3.4.21.85. CAS No. 848851-53-6. 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-4177; limulus clotting factor B; EC 3.4.21.85; 848851-53-6. Cat No: EXWM-4177. | |
| limulus clotting factor C | From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: factor C; limulus factor C. Enzyme Commission Number: EC 3.4.21.84. CAS No. 115743-27-6. 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-4176; limulus clotting factor C; EC 3.4.21.84; 115743-27-6; factor C; limulus factor C. Cat No: EXWM-4176. | |
| Magnesium L-Threonate | Magnesium L-threonate is a nutritional supplement containing the L-threonate form of magnesium (Mg) that can be used to normalize Mg levels in the body. Upon administration, Mg is utilized by the body for many biochemical functions and reactions including: bone and muscle function, protein and fatty acid formation, activation of B vitamins, blood clotting, insulin secretion, and ATP formation. Mg also serves as a catalyst for many enzymes throughout the body. In addition, magnesium improves the functioning of the immune system by enhancing the expression of natural killer activating receptor NKG2D in cytotoxic T-lymphocytes and natural killer (NK) cells. This increases their anti-viral and anti-tumor cytotoxic effects. Synonyms: MgT, Magnesium L-threonate anhydrous. CAS No. 778571-57-6. Product ID: CDF4-0255. Molecular formula: Mg(C4H7O5)2. Mole weight: 294.495. Product Keywords: Nutrients; CDF4-0255; Magnesium L-Threonate; 778571-57-6; MgT, Magnesium L-threonate anhydrous. UNII: 1Y26ZZ0OTM. Chemical Name: Magnesium bis[(2R,3S)-2,3,4-trihydroxybutanoate]. Grade: Food grade. Administration route: CAPSULE, DELAYED RELEASE PELLETS. Dosage Form: CAPSULE, DELAYED RELEASE PELLETS. Applications: Magnesium L-threonate is a nutritional supplement containing the L-threonate form of magnesium (Mg) that can be used to normalize Mg levels in the body. Upon administration, Mg is utilized by the body for many biochemical fu |  |
| Native Human Factor α-XIIa | Human Factor α-XIIa is a serine protease responsible for the activation of Factor XI to XIa in the contact activation system. Human Factor XII and prekallikrein are thought to be involved in a reciprocal activation mechanism in which Factor XIIa activates prekallikrein to kallikrein, which in turn converts Factor XII to XIIa. Factor XIIa activates Factor XI to XIa thereby triggering the Contact Factor cascade. ERL offers Factor α-XIIa which is activated by the autoactivation process with Dextran Sulfate and re-purified to remove the activator. The protein purity is determined by SDS-PAGE and activity is determined via clotting assay. Group: Enzymes. Synonyms: Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Factor α-XIIa. Mole weight: 80 kDa. Activity: 69.51 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Cat No: NATE-0882. | |
| Native Human Factor VIIa | Prepared from purified Human Factor VII using Human Factor XIIa. The Factor Xlla is removed using affinity chromatography. Purity is determined by SDS-PAGE. Human Factor VIIa reduces to 29,500 and 23,500 with the addition of 2-mercaptoethanol. Activity is determined via clotting assay. Factor Vlla, in the presence of calcium ions and Tissue factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa. Group: Enzymes. Synonyms: Human Factor VII; Factor VII. Factor VIIa. Mole weight: 50 kDa. Activity: 53833.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor VII; Factor VII. Cat No: NATE-0884. | |
| Native Human Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Pineapple Bromelain | Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit. Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus. Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics. Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity. Applications: Bromelain may be used to inhibit the biosysnthesis of proinflammatory prostaglandins. it may be used to reduce clotting efficiency. bromelain, from pineapple stem, has been used to make enzymatic hydrolysates of honeybee-collected pollen. Group: Enzymes. Synonyms: stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineappl. Enzyme Commission Number: EC 3.4.22.32. CAS No. 37189-34-7. Bromelain. Activity: > 3 units/mg protein; 5-15 units/mg protein. Form: Lyophilized powder containing mannitol and potassium phosphate buffer salts. Source: Pineapple stem. Species: Pineapple. stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineapple stem bromelain; SBM. Cat No: NATE-0665. | |
| Native Rabbit Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. The nih assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1 ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of biggs. only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations. activity is expressed in nih units obtained by direct comparison to a nih thrombin reference standard. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Source: Rabbit plasma. Species: Rabbit. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0700. | |
| Native Russell's viper venom Factor V Activating Enzyme | Factor V activator for RVV contains fucose, mannose, galactose, glucosamine, and neuraminic acid. Factor V activating enzyme from RVV is an arginine esterase that is sensitive to diisopropyl fluorophosphate (DFP). Applications: Factor v activating enzyme from russells viper venom (rvv) is a single-chain glycoprotein that is involved in the rapid clotting of blood. factor v circulates in the blood as an inactive cofactor and must be activated by proteases such as factor v activating enzyme from rvv 1. this product may be useful in studying the blood coagulation cascade as well as the inherited deficiency called parahemophilia. Group: Enzymes. Synonyms: EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Enzyme Commission Number: EC 3.4.21.95. CAS No. 65522-14-7. Factor V activator. Activity: 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Stabilized in albumin and sodium chloride. Source: Russell's viper venom. EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Cat No: NATE-0249. | |
| peptidyl-glutamate 4-carboxylase | The enzyme can use various vitamin-K derivatives, including menaquinol, but does not contain iron. The mechanism appears to involve the generation of a strong base by oxygenation of vitamin K. It catalyses the post-translational carboxylation of glutamate residues of several proteins of the blood-clotting system. 9-12 glutamate residues are converted to 4-carboxyglutamate (Gla) in a specific domain of the target protein. The 4-pro-S hydrogen of the glutamate residue is removed and there is an inversion of stereochemistry at this position. Group: Enzymes. Synonyms: vitamin K-dependent carboxylase; γ-glutamyl carboxylase; peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing). Enzyme Commission Number: EC 4.1.1.90. 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-4840; peptidyl-glutamate 4-carboxylase; EC 4.1.1.90; vitamin K-dependent carboxylase; γ-glutamyl carboxylase; peptidyl-glutamate 4-carboxylase (2-methyl-3-phytyl-1,4-naphthoquinone-epoxidizing). Cat No: EXWM-4840. | |
| Alkaline Cellulase for detergent | Cellulase is a kind of enzyme preparation which produced by cellulase modification. The cellulase of which with high alkaline be used as an ingredient for detergent. In the washing process, cellulase can effectively remove microfiber on fabric for wear. It also can keep cotton fiber fabric with bright color and good smoothness. Therefore, after the washing with cellulase, white clothes will be whiter and color clothes will be brighter and softer. At the same time, it can get off the granular dirt in the fiber. Applications: A. reduce fiber debris b. brighten clothes and make clothes look newly c. keep fabric with bright color and good smoothnes d. remove granular dirt e. dissolve dirt mixture. Group: Enzymes. Synonyms: Alkaline Cellulase; for detergent; Reduce fiber debris; alkaline Cellulase; remove microfiber; fabric; keep bright color; cotton fiber ;fabric ;Detergent Enzymes; Detergents; Alkaline Cellulase for detergent; DETE-2621. CAS No. 9012-54-8. Cellulase. Appearance: powder or liquid. Alkaline Cellulase; for detergent; Reduce fiber debris; alkaline Cellulase; remove microfiber; fabric; keep bright color; cotton fiber ;fabric ;Detergent Enzymes; Detergents; Alkaline Cellulase for detergent; DETE-2621. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2621. | |
| Alkaline Protease for detergent | Protease is a kind of enzyme preparation produced by one microbes submerged fermentation. It is also a kind of modified enzyme preparation after DNA recombination. As a common used enzyme preparation in detergent industry, the main activated composition alkaline protease can rapidly decompose protein. Protease can hydrolyze the hardly soluble protein on fabric into soluble peptide chain and amino acid in detergent solution. smoothness. Therefore, after the washing with cellulase, white clothes will be whiter and color clothes will be brighter and softer. At the same time, it can get off the granular dirt in the fiber. Applications: Protease can effectively remove sweat stain, blood stains, food protein dirt, cream stain and etc, the detergent contains protease will make fabric get perfect effect after washing. Group: Enzymes. Synonyms: Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. CAS No. 37259-58-8. Alkaline Protease. Appearance: powder or liquid. Alkaline Protease; for detergent; Protease; decompose protein; Detergent Enzymes; Detergents; Alkaline Protease for detergent; DETE-2623. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DETE-2623. | |
| BC 11 hydrobromide | BC 11 hydrobromide is a selective urokinase (uPA) inhibitor (IC50 = 8.2 μM) with no activity at 8 other related enzymes. BC 11 inhibits clot lysis displaying no effect on clot formation. It also decreases viability of MDA-MB231 breast cancer cells in vitro. Synonyms: BC11 hydrobromide; BC-11 hydrobromide; BC 11 hydrobromide; BC-11 HBr Carbamimidothioic acid (4-boronophenyl)methyl ester hydrobromide; [4- (carbamimidoylsulfanylmethyl) phenyl]boronic acid hydrobromide. CAS No. 443776-49-6. Molecular formula: C8H11BN2O2S.HBr. Mole weight: 290.97. | |
| 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 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. | |
| Cotarnine chloride | Cotarnine chloride is a covalent, active agent that is particulate in form. It has been shown to have hemostatic properties by forming a covalent bond with the fibers of blood vessels, as well as hydrogen bonds and hydrogen bonding. Cotarnine chloride also inhibits the formation of clots and thrombi by inhibiting platelet aggregation, which is mediated by adenosine diphosphate (ADP) and collagen. This drug also has anti-inflammatory properties due to its ability to inhibit an enzyme that catalyzes the conversion of arachidonic acid into prostaglandins. Group: Other alkaloids. Alternative Names: 7,8-Dihydro-4-methoxy-6-methyl-1,3-dioxolo[4,5-g]isoquinolinium chlorideCotarninium chlorideStypticin. CAS No. 10018-19-6. Molecular formula: C12H14ClNO3. Mole weight: 255.7 g/mol. Canonical SMILES: C[N+]1=CC2=C(C3=C(C=C2CC1)OCO3)OC. [Cl-]. Catalog: ACM10018196. |  |
| 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 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 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. | |
| Lumbrokinase | Lumbrukinase extracted from earthworm alimentary canal.Lumbrukinasehas the functions of hydrolyzing fibrin directly as well as indirectly by activating plasminogen into plasmin.The product has evident anti-thrombus and thrombolytic effects. Lumbrokinase in the medical profession is known as the King of thrombolytic therapy, extraction in the earthworm. Apply to affected area after the rapid infiltration of silt to dissolve the clot resistance to vascular flow, varicose veins falling gradually. Applications: Functional food, health care products and pharmaceuticals. Group: Others. Purity: 5000-20000 u/mg. Appearance: Light yellow or grey. Source: Earthworm. Lumbrokinase; Pheretima. Cat No: EXTC-133. | |
| 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. | |
| 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 Mucor miehei Rennin | Mucorpepsin is an enzyme that catalyses the following chemical reaction: Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen. This enzyme is isolated from the zygomycete fungi Mucor pusillus and M. miehei. Group: Enzymes. Synonyms: Mucorpepsin; EC 3.4.23.23; Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin; 9073-79-4. Enzyme Commission Number: EC 3.4.23.23. CAS No. 9073-79-4. Rennin. Mole weight: Mr ~40 kDa. Activity: ~0.1 units/mg. Storage: -20°C. Form: lyophilized powder; slightly brown. Source: Mucor miehei. Mucorpepsin; EC 3.4.23.23; Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin; 9073-79-4. Cat No: NATE-0652. | |
| Nattokinase, Natto fermentation | Nattokinase, Natto fermentation is a potent fibrinolytic enzyme. Nattokinase can break down blood clots by directly hydrolyzing fibrin and plasmin substrate. Nattokinase can be used for the research of cardiovascular diseases [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 133876-92-3. Pack Sizes: 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-P2373. |  |
| 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. | |
| Staphylokinase from Staphylococcus aureus, Recombinant | Staphylokinase (SAK), a 16kDa profibrinolytic protein from the Staphylococcus aureus, has been demonstrated to induce highly fibrin-specific thrombolysis in both human plasma and in limited clinical trials. Recent studies on the thrombolytic potential of recombinant SAK in achieving early perfusion in myocardial infarction and in the dissolution of platelet-rich clot have clearly established its immense utility in clinical medicine as a thrombolytic agent and suggested that it can be developed as a potent clot-dissolving agent. Group: Enzymes. Synonyms: Staphylokinase; SAK. Purity: > 97% by SDS-PAGE and HPLC analyses. SAK. Mole weight: 15.6 kDa. Activity: 50000 IU/mg. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Storage: This lyophilized preparation is stable at 2-8 °C, but should be kept at -20 °C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8 °C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 °C to -70 °C. Avoid repeated freeze/thaw cycles. Form: Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Source: E. coli. Species: Staphylococcus aureus. Staphylokinase; SAK. Cat No: NATE-0914. | |
| 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. | |
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