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| Product | Description | |
|---|---|---|
| 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 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 | |
| Aldosterone secretion inhibiting factor(1-35)(bovine) | Heterocyclic Organic Compound. Alternative Names: ALDOSTERONE SECRETION INHIBITING FACTOR (1-35) (BOVINE);ALDOSTERONE SECRETION INHIBITORY FACTOR (1-35) (BOVINE);H-ALA-LEU-ARG-GLY-PRO-LYS-MET-MET-ARG-ASP-SER-GLY-CYS-PHE-GLY-ARG-ARG-LEU-ASP-ARG-ILE-GLY-SER-LEU-SER-GLY-LEU-GLY-CYS-ASN-VAL-LEU-ARG-ARG-TYR-. CAS No. 120249-06-1. Molecular formula: C164H278N58O45S4. Mole weight: 3910.58. Catalog: ACM120249061. |  |
| Atrial natriuretic factor(3-28)(human,bovine,porcine) | Heterocyclic Organic Compound. Alternative Names: ATRIAL NATRIURETIC PEPTIDE (3-28), HUMAN;ATRIAL NATRIURETIC FACTOR (3-28) (HUMAN);ANF (3-28) (HUMAN, CANINE);H-ARG-ARG-SER-SER-CYS-PHE-GLY-GLY-ARG-MET-ASP-ARG-ILE-GLY-ALA-GLN-SER-GLY-LEU-GLY-CYS-ASN-SER-PHE-ARG-TYR-OH;HANF (3-28). CAS No. 102686-43-1. Molecular formula: C118H187N43O36S3. Mole weight: 2880.21. Catalog: ACM102686431. | |
| GROWTH HORMONE RELEASING FACTOR 1-29*AMI DE, BOVINE | Heterocyclic Organic Compound. CAS No. 112898-04-1. Molecular formula: NULL. Mole weight: 3384.91. Purity: 0.96. Canonical SMILES: CCC (C)C (C (=O)NC (CC1=CC=CC=C1)C (=O)NC (C (C)O)C (=O)NC (CC (=O)N)C (=O)NC (CO)C (=O)NC (CC2=CC=C (C=C2)O)C (=O)NC (CCCNC (=N)N)C (=O)NC (CCCCN)C (=O)NC (C (C)C)C (=O)NC (CC (C)C)C (=O)NCC (=O)NC (CCC (=O)N)C (=O)NC (CC (C)C)C (=O)NC (CO)C (=O)NC (C)C (=O)NC (CCCNC (=N)N)C (=O)NC (CCCCN)C (=O)NC (CC (C)C)C (=O)NC (CC (C)C)C (=O)NC (CCC (=O)N)C (=O)NC (CC (=O)O)C (=O)NC (C (C)CC)C (=O)NC (CCSC)C (=O)NC (CC (=O)N)C (=O)NC (CCCNC (=N)N)C (=O)N)NC (=O)C (C)NC (=O)C (CC (=O)O)NC (=O)C (C)NC (=O)C (CC3=CC=C (C=C3)O)N. Catalog: ACM112898041. | |
| Native Bovine Factor IXa β | Prepared from Bovine Factor IX by activation with Bovine Factor Xla, this Bovine Factor Xla is removed after activation. Complete activation is observed by SDS-PAGE. The Factor Xla activates FIX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce factor IXa&beta. Group: Enzymes. Synonyms: Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Factor IXa Beta. Mole weight: 43.9 kDa. Activity: 3096.00 PEU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Cat No: NATE-0867. | |
| Native Bovine Factor Xa | Bovine Factor Xa is prepared from Bovine Factor X by activation with Russell's Viper Venom. This RVV-X is removed after activation. Complete activation is observed by SDS-PAGE. Factor Xa, as part of the prothrombinase complex along with the cofactor Va, phospholipids and calcium ions, catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Bovine Factor Xa; Factor Xa. Factor Xa. Mole weight: 45.3 kDa. Activity: 210.00 IU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor Xa; Factor Xa. Cat No: NATE-0868. | |
| Native Bovine Factor X Activated (Xa) | Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr | |
| Native Bovine Factor XIa | Bovine Factor Xla is purified from freshly collected Bovine Plasma using a combination of salt precipitations and activation on a negative surface. This Factor Xla is a potent activator of both Human and Bovine Factor IX. Bovine Factor XIa purity is determined by SDS-PAGE and shows complete reduction upon incubation with 2-mercaptoethanol. Group: Enzymes. Synonyms: Bovine Factor XIa; Factor XIa. Factor XIa. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor XIa; Factor XIa. Cat No: NATE-0869. | |
| Prepro-von Willebrand factor (641-650) (bovine) | Prepro-von Willebrand factor (641-650) (bovine), derived from the von Willebrand factor, has an increased affinity for collagen and promotes wound healing. It binds bovine collagen type I with an apparent Kd of 100 μM. Synonyms: pp-vWF (641-650); H-Trp-Arg-Glu-Pro-Ser-Phe-Cys-Ala-Leu-Ser-OH; L-Serine, L-tryptophyl-L-arginyl-L-α-glutamyl-L-prolyl-L-seryl-L-phenylalanyl-L-cysteinyl-L-alanyl-L-leucyl-. Grades: ≥95%. CAS No. 143470-36-4. Molecular formula: C54H78N14O15S. Mole weight: 1195.35. |  |
| Bovine FGF | Heterocyclic Organic Compound. Alternative Names: Bovine FGF;rec FGF acidic (human);Recombinant Human acidic Fibroblast Growth Factor(aFGF). CAS No. 106096-92-8. Catalog: ACM106096928. | |
| 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 | |
| CRF, bovine | CRF, bovine is an effective agonist of CRF (Corticotropin-releasing factor) receptor. Synonyms: Corticotropin Releasing Factor bovine; H-Ser-Gln-Glu-D-Pro-D-Pro-Ile-Ser-Leu-Asp-Leu-aThr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-DL-Met-Thr-Lys-D-Ala-D-Asp-D-Gln-D-Leu-D-Ala-D-Gln-D-Gln-D-Ala-D-His-D-Asn-D-Asn-D-Arg-D-Lys-D-Leu-D-Leu-D-Asp-aIle-D-Ala-NH2; L-seryl-L-glutaminyl-L-alpha-glutamyl-D-prolyl-D-prolyl-L-isoleucyl-L-seryl-L-leucyl-L-alpha-aspartyl-L-leucyl-L-allothreonyl-L-phenylalanyl-L-histidyl-L-leucyl-L-leucyl-L-arginyl-L-alpha-glutamyl-L-valyl-L-leucyl-L-alpha-glutamyl-DL-methionyl-L-threonyl-L-lysyl-D-alanyl-D-alpha-aspartyl-D-glutaminyl-D-leucyl-D-alanyl-D-glutaminyl-D-glutaminyl-D-alanyl-D-histidyl-D-asparagyl-D-asparagyl-D-arginyl-D-lysyl-D-leucyl-D-leucyl-D-alpha-aspartyl-L-alloisoleucyl-D-alaninamide. Grades: 95%. CAS No. 92307-52-3. Molecular formula: C206H340N60O63S. Mole weight: 4697.33. | |
| Gabexate mesylate | Gabexate mesylate (FOY) is is a competitive and non-antigenic synthetic inhibitor of trypsin-like serine proteinases. Gabexate mesylate inhibits human thrombin, urokinase, plasmin, and Factor Xa with K i s of 0.97, 1.3, 1.6, and 8.5 μM, respectively. Gabexate mesylate binds to human and bovine tryptase with K i s of 3.4 nM and 18 μM, respectively. Gabexate mesylate exerts an anticoagulant effect on the clotting activity of thrombin and has anti-inflammatory effect by viainhibition of NF-κB, proinflammatory cytokines, and nitric oxide. Gabexate mesylate is used for pancreatitis and disseminated intravascular coagulation [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: FOY. CAS No. 56974-61-9. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-B0385. |  |
| 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 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 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 | |
| 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 | |
| Lecirelin acetate | Lecirelin acetate, a synthetic gonadotropin-releasing hormone (GnRH) analogue, has a good effect in the treatment of bovine ovarian follicular cysts. It is a medication commonly used in veterinary. Synonyms: Luteinizing hormone-releasing factor (pig), 6-(3-methyl-D-valine)-9-(N-ethyl-L-prolinamide)-10-deglycinamide-, acetate; Dalmarelin acetate; Gestran acetate; Gestran Plus acetate; Supergestran acetate; H-Pyr-His-Trp-Ser-Tyr-D-Gly(tBu)-Leu-Arg-Pro-NHEt.CH3CO2H; L-pyroglutamyl-L-histidyl-L-tryptophyl-L-seryl-L-tyrosyl-2-tert-butyl-D-glycyl-L-leucyl-L-arginyl-L-proline ethylamide acetic acid. Grades: ≥95%. Molecular formula: C61H88N16O14. Mole weight: 1269.45. | |
| 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 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 Lipoprotein Lipase | Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. LPL is attached to the luminal surface of endothelial cells in capillaries by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1) and by heparin sulfated proteoglycans. It is most widely distributed in adipose, heart, and skeletal muscle tissue, as well as in lactating mammary glands. Group: Enzymes. Synony. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Activity: > 2,000 units/mg protein (BCA). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.8 M ammonium sulfate, 0.02 M Tris HCl, pH 8.0. Source: Bovine milk. Species: Bovine. lipoprotein lipase; clearing factor lipase; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; EC 3.1.1.34; 9004-02-8; LPL. Cat No: NATE-0416. | |
| Native Bovine Protamine Kinase, Cytosolic | Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase. Applications: Cytosolic protamine kinase (cpk) is isolated from bovine kidney and has a molecular mass of approximately 45 kda. it phosphorylates the eukaryotic initiation factor 4e (eif4e), which initiates translation by mrna. it is used to study protein synthesis and various cellular processes. Group: Enzymes. Synonyms: Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Purity: >90% (SDS-PAGE). CPK. Activity: > 15,000 units/mg protein. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Cat No: NATE-0155. | |
| Native Bovine Tautomerase | In enzymology, phenylpyruvate tautomerase or Macrophage migration inhibitory factor (EC 5.3.2.1) is an enzyme that catalyzes the chemical reaction:keto-phenylpyruvate<-> enol-phenylpyruvate. Phenylpyruvate tautomerase has also been found to exhibit the same keto-enol tautomerism for 4-Hydroxyphenylpyruvic acid, which is structurally similar to phenylpyruvate but contains an additional hydroxyl moiety in the para position of the aromatic ring. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto-and enol-groups. This enzyme participates in tyrosine metabolism and phenylalanine metabolism. Applications: Tautomerase from bovine kidney has been used in a study to assess tritium isotope effects in the reaction catalyzed by 4-hydroxyphenylpyruvate dioxygenase. tautomerase from bovine kidney has also been used in a study to investigate human macrophage migration inhibitory factor. Group: Enzymes. Synonyms: Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-. Enzyme Commission Number: EC 5.3.2.1. CAS No. 9023-54-5. Tautomerase. Activity: 1-4 units/mg protein (Lowry), ~10 units/mL. Storage: -20°C. Form: aqueous solution. Source: Bovine kidney. Species: Bovine. Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-enol isomerase; 9023-54-5. Cat No: NATE-0691. | |
| Native Bovine 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. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of ...Ia; E thrombin; β-thrombin; γ-thrombin. 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). Form: Type I, Lyophilized from saline sodium Citrate buffer, pH 6.5; Type II, buffered aqueous solution, In 0.05 M phosphate buffer, pH 7.0. Source: Bovine plasma. Species: Bovine. 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-0698. | |
| Native Flavobacterium heparinum Heparinase II | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Group: Enzymes. Synonyms: Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. CAS No. 149371-12-0. Heparinase. Mole weight: mol wt 84.1 kDa. Activity: > 100 units/mg protein (enzyme + BSA). Form: Lyophilized powder stabilized with approx. 25% bovine serum albumin. Source: Flavobacterium heparinum. Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. Cat No: NATE-0339. | |
| Native Human Factor IXa β | Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa&beta. Group: Enzymes. Synonyms: Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Factor IXa Beta. Mole weight: 45 kDa. Activity: 12500.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Cat No: NATE-0883. | |
| Thymidine Phosphorylase from Escherichia coli, Recombinant | An enzyme that catalyzes the reversible conversion of thymidine to thymine. Thymidine phosphorylase is part of the pyrimidine nucleoside salvage pathway. This pathway allows pyrimidine bases to be recycled for nucleotide biosynthesis, while the pentose 1-phosphates are converted to intermediates of the pentose phosphate shunt and glycolysis. The E. coli thymidine phosphorylase shares 40% sequence homology with the human sequence, which has been found to be identical to the angiogenic agent platelet-derived endothelial growth factor. The purified E. coli enzyme has been shown to stimulate blood vessel growth in chick chorioallantoic membrane assays. Applications: ...hosphate deoxy-D-ribosyltransferase; EC 2.4.2.4; 9030-23-3. Enzyme Commission Number: EC 2.4.2.4. CAS No. 9030-23-3. Thymidine Phosphorylase. Activity: Type I, > 900 units/mL, aseptically filled; Type II, > 500 units/mL. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 0.5 M potassium phosphate containing 2 mM uracil, 0.02% sodium azide and bovine serum albumin. Source: E. coli. Species: Escherichia coli. thymidine phosphorylase; pyrimidine phosphorylase; thymidine-orthophosphate deoxyribosyltransferase; animal growth regulators, blood platelet-derived endothelial cell growth factors; blood platelet-derived endothelial cell growth factor; deoxythymidi | |
| Fibrin (Bovine) | Fibrinogen has been used in studies of haemostatic therapy in surgical and massive trauma patients. These studies have shown that fibrinogen may prove to be more superior in stopping blood loss when compared to using fresh frozen plasma (FFP). Group: Biochemicals. Alternative Names: Factor I. Grades: Molecular Biology Grade. CAS No. 9001-31-4. Pack Sizes: 1g. US Biological Life Sciences. |  Worldwide |
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