Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| HRV3C Protease from human, Recombinant | Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln*Gly-Pro. It is supplied as a 47 kDa protein with both GST and Histidine tags for easy removal by His-Select or Glutathione agarose along with the cleaved tag. HRV3C Protease is capable of cleaving small peptides with the sequence of polyprotein processing sites. It cleaves after the glutamine residue. HRV cleavage site generally contains Gln/Gly scissile bond. Hrv3c protease is a recombinant restriction-grade cysteine protease. it folds into two topologically alike six-stranded β barrels. however, β barrels are different in length and ... with both gst and histidine tags for easy removal by his-select or glutathione agarose along with the cleaved tag. hrv3c protease has a therapeutic implication because of its unique protein structure. it may be used for the biochemical and structural characterization conducted on hrv 3c protease along with the development of 3c protease inhibitors. Group: Enzymes. Synonyms: HRV3C Protease; HRV3C; Human rhinovirus 3C protease. HRV3C. Activity: > 1 units/μg. Storage: -20°C. Form: Supplied as a solution in 25 mM Tris-HCl, pH 8.0, 50 mM NaCl, 1 mM TCEP and 50% glycerol. Source: E. coli. Species: Human. HRV3C Protease; HRV3C; Human rhinovirus 3C protease. Cat No: NATE-0345. |  |
| HslU-HslV peptidase | The HslU subunit of the HslU-HslV complex functions as an ATP dependent 'unfoldase'. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolysed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. In peptidase family T1. Group: Enzymes. Synonyms: HslUV; HslV-HslU; HslV peptidase; ATP-dependent HslV-HslU proteinase; caseinolytic protease X; caseinolytic proteinase X; ClpXP ATP-dependent protease; ClpXP protease; ClpXP serine proteinase; Escherichia coli ClpXP serine proteinase; HslUV protease; HslUV proteinase; HslVU protease; HslVU proteinase; protease HslVU; proteinase HslUV. Enzyme Commission Number: EC 3.4.25.2. 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-4375; HslU-HslV peptidase; EC 3.4.25.2; HslUV; HslV-HslU; HslV peptidase; ATP-dependent HslV-HslU proteinase; caseinolytic protease X; caseinolytic proteinase X; ClpXP ATP-dependent protease; ClpXP protease; ClpXP serine proteinase; Escherichia coli ClpXP serine proteinase; HslUV protease; HslUV proteinase; HslVU protease; HslVU proteinase; protease HslVU; proteinase HslUV. Cat No: EXWM-4375. | |
| HspA I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 1000U; 5000U. G↑CGC CGC↓G. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned HspA I gene from Haemophilus species A1. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1124RE. | |
| HtrA2 peptidase | This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). Belongs in peptidase family S1C. Group: Enzymes. Synonyms: high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Enzyme Commission Number: EC 3.4.21.108. 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-4103; HtrA2 peptidase; EC 3.4.21.108; high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Cat No: EXWM-4103. | |
| H+-transporting two-sector ATPase | A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the Δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform...cal conditions, they pump H+ rather than synthesize ATP. Group: Enzymes. Synonyms: ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (F0, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase. Enzyme Commission Number: EC 7.1.2.2 (Formerly EC 3.6.3.14). 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-4650; H+-transporting two-sector ATPase; EC 3.6.3.14; ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (F0, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase. Cat No: EXWM-4650. | |
| 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 endogenous retrovirus K endopeptidase | In peptidase family A2. Group: Enzymes. Synonyms: human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Enzyme Commission Number: EC 3.4.23.50. 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-4288; human endogenous retrovirus K endopeptidase; EC 3.4.23.50; human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Cat No: EXWM-4288. | |
| 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 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 | |
| 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 Prethrombin-1 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature ...Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prethrombin-2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature ...Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| 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 | |
| Human Prothrombin | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature p...-Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 1 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mat...1 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 1.2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the ma... (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mat...1 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Huperzia serrata Extract (Ratio) | Huperzia serrata Extract (Ratio). Group: Others. Purity: 4:1~20:1. Huperzia serrata Extract (Ratio). Cat No: EXTW-042. | |
| Huperzia Serrata Extract (Standard) | Huperzia serrata is luxuriant plants, it has the total of eight varieties of medicinal plants in China. China is the biggest wild sugihara. Middle extact from the plants Huperzia serrata is the treatment of senile dementia, specific drug that can improve peoples. Applications: Huperzine a has potent pharmacological effects and particularly since long-term safety has not been determined, it should only be used with medical supervision. it may have some effectiveness in alzheimer's disease and age-related memory impairment. it has been used to treat fever and some inflammatory disorders, but there is no credible scientific evidence to support these uses. Group: Others. CAS No. 120786-18-7. Purity: 1.0%, 5.0% Huperzine A HPLC. Mole weight: 242.316. Huperzia Serrata Extract (Standard); 120786-18-7; C15H18N2O. Cat No: EXTW-007. | |
| hyaluronan synthase | The enzyme from Streptococcus Group A and Group C requires Mg2+.The enzyme adds GlcNAc to nascent hyaluronan when the non-reducing end is GlcA, but it adds GlcA when the non-reducing end is GlcNAc. The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA; no copolymerization is observed if either is replaced by UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. Similar enzymes have been found in a variety of organisms. Group: Enzymes. Synonyms: spHAS; seHAS. Enzyme Commission Number: EC 2.4.1.212. CAS No. 39346-43-5. Hyaluronan synthase. 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-2440; hyaluronan synthase; EC 2.4.1.212; 39346-43-5; spHAS; seHAS. Cat No: EXWM-2440. | |
| Hyaluronan synthase from Pasteurella multocida, Recombinant | Hyaluronan synthases (HAS) are membrane-bound enzymes which use UDP-α-N-acetyl-D-glucosamine and UDP-α-D-glucuronate as substrates to produce the glycosaminoglycan hyaluronan at the cell surface and extrude it through the membrane into the extracellular space. Group: Enzymes. Synonyms: EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Enzyme Commission Number: EC 2.4.1.212. CAS No. 39346-43-5. Purity: min 95% by SDS-PAGE. Hyaluronan synthase. Source: E. coli. Species: Pasteurella multocida. EC 2.4.1.212; spHAS; seHAS; Hyaluronan synthases; HAS. Cat No: NATE-1485. | |
| hyaluronate lyase | The enzyme catalyses the degradation of hyaluronan by a β-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose. Group: Enzymes. Synonyms: hyaluronidase (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous). Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Hyaluronate Lyase. 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-5084; hyaluronate lyase; EC 4.2.2.1; 37259-53-3; hyaluronidase (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous). Cat No: EXWM-5084. | |
| Hyaluronate lyase from Streptococcus equi, Recombinant | Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Purity: > 95 % as judged by SDS-PAGE. Hyaluronate Lyase. Mole weight: 38447.1 Da. Activity: 4.6 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptococcus equi 4047. hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Cat No: NATE-1210. | |
| Hyaluronate Lyase from Streptococcus pyogenes, Recombinant | Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. It is important for the diffusion of toxins and proteins produced by S. pyogenes. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Hyaluronate Lyase. Activity: > 8.0 units/mg protein (5.0-15.0 mg/mL). Storage: 2-8°C. Form: ammonium sulfate suspension. Source: E. coli. Species: Streptococcus pyogenes. hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Cat No: NATE-0346. | |
| Hyaluronate lyase from Streptomyces coelicolor, Recombinant | Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Purity: > 95 % as judged by SDS-PAGE. Hyaluronate Lyase. Mole weight: 82914.2 Da. Activity: 8.1 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptomyces coelicolor A3(2). hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Cat No: NATE-1211. | |
| hyaluronoglucosaminidase | Also hydrolyses 1,4-β-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan. Group: Enzymes. Synonyms: hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. 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-3897; hyaluronoglucosaminidase; EC 3.2.1.35; 37326-33-3; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I. Cat No: EXWM-3897. | |
| hyaluronoglucuronidase | This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglucosaminoglycan hyaluronate lyase; orgelase. Enzyme Commission Number: EC 3.2.1.36. CAS No. 37288-34-9. 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-3898; hyaluronoglucuronidase; EC 3.2.1.36; 37288-34-9; hyaluronidase; glucuronoglucosaminoglycan hyaluronate lyase; orgelase. Cat No: EXWM-3898. | |
| HycI peptidase | The reaction requires nickel to be bound to the precursor of the large subunit of hydrogenase 3. The endopeptidase uses the metal in the large subunit of [NiFe]-hydrogenases as a recognition motif. In peptidase family A31. Group: Enzymes. Synonyms: HycI; HycE processing protein. Enzyme Commission Number: EC 3.4.23.51. 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-4289; HycI peptidase; EC 3.4.23.51; HycI; HycE processing protein. Cat No: EXWM-4289. | |
| hydantoin racemase | This enzyme, along with N-carbamoylase (EC 3.5.1.77 and EC 3.5.1.87) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids. The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-(2-methylthioethyl)hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position. In the enzyme from Sinorhizobium meliloti, Cys76 is responsible for recognition and proton retrieval of D-isomers, while Cys181 is responsible for L-isomer recognition and racemization. Group: Enzymes. Synonyms: 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Enzyme Commission Number: EC 5.1.99.5. 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-5437; hydantoin racemase; EC 5.1.99.5; 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Cat No: EXWM-5437. | |
| Hydantoin Racemase (Crude Enzyme) | This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis. Group: Enzymes. Synonyms: 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Enzyme Commission Number: EC 5.1.99.5. CAS No. 111310-51-1. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. 5'-monosubstituted-hydantoin racemase; HyuA; HyuE. Pack: 100ml. Cat No: NATE-1855. | |
| Hydrangea Root Extract | Hydrangea Root Extract. Applications: Used for health care products, dietary supplements, herb medecine, treating autoimmune disorders. Group: Others. Synonyms: Hydrangea Root Extract; Hydrangea macrophylla L. Purity: 4-10:1 by TLC. Appearance: Yellow Brown fine powder. Storage: 2 years under well storage situation and stored away from direct sun light. Source: Root. Species: Hydrangea macrophylla L. Hydrangea Root Extract; Hydrangea macrophylla L.; plant extract. Pack: 25KG/Drum with double plastic bag of foodstuff inside. Cat No: EXTW-139. | |
| hydrazine dehydrogenase | The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis. The electrons derived from hydrazine are eventually transferred to the quinone pool. Group: Enzymes. Synonyms: HDH. Enzyme Commission Number: EC 1.7.2.8. CAS No. 9075-43-8. 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-1623; hydrazine dehydrogenase; EC 1.7.2.8; 9075-43-8; HDH. Cat No: EXWM-1623. | |
| hydrazine synthase | The enzyme, characterized from anaerobic ammonia oxidizers (anammox bacteria), is one of only two enzymes that are known to form an N-N bond (the other being EC 1.7.1.14, nitric oxide reductase [NAD(P)+, nitrous oxide-forming]). The enzyme from the bacterium Candidatus Kuenenia stuttgartiensis is heterotrimeric and contains multiple c-type cytochromes. Group: Enzymes. Synonyms: HZS. Enzyme Commission Number: EC 1.7.2.7. 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-1622; hydrazine synthase; EC 1.7.2.7; HZS. Cat No: EXWM-1622. | |
| hydrogenase (acceptor) | Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel. Group: Enzymes. Synonyms: H2 producing hydrogenase (ambiguous); hydrogen-lyase (ambiguous); hydrogenlyase (ambiguous); uptake hydrogenase (ambiguous); hydrogen:(acceptor) oxidoreductase. Enzyme Commission Number: EC 1.12.99.6. CAS No. 9027-5-8. 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-0528; hydrogenase (acceptor); EC 1.12.99.6; 9027-05-8; H2 producing hydrogenase (ambiguous); hydrogen-lyase (ambiguous); hydrogenlyase (ambiguous); uptake hydrogenase (ambiguous); hydrogen:(acceptor) oxidoreductase. Cat No: EXWM-0528. | |
| hydrogenase (NAD+, ferredoxin) | The enzyme from Thermotoga maritima contains a [FeFe] cluster (H-cluster) and iron-sulfur clusters. It works in the direction evolving hydrogen as a means of eliminating excess reducing equivalents. Group: Enzymes. Synonyms: bifurcating [FeFe] hydrogenase. Enzyme Commission Number: EC 1.12.1.4. 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-0519; hydrogenase (NAD+, ferredoxin); EC 1.12.1.4; bifurcating [FeFe] hydrogenase. Cat No: EXWM-0519. | |
| hydrogen dehydrogenase | An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel. Group: Enzymes. Synonyms: H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase. Enzyme Commission Number: EC 1.12.1.2. CAS No. 9027-5-8. 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-0517; hydrogen dehydrogenase; EC 1.12.1.2; 9027-05-8; H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase. Cat No: EXWM-0517. | |
| hydrogen dehydrogenase (NADP+) | The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase, while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+]. Group: Enzymes. Synonyms: NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Enzyme Commission Number: EC 1.12.1.3. CAS No. 9027-5-8. 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-0518; hydrogen dehydrogenase (NADP+); EC 1.12.1.3; 9027-05-8; NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Cat No: EXWM-0518. | |
| hydrogen dehydrogenase [NAD(P)+] | A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+). Group: Enzymes. Synonyms: hydrogenase II (ambiguous). Enzyme Commission Number: EC 1.12.1.5. 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-0520; hydrogen dehydrogenase [NAD(P)+]; EC 1.12.1.5; hydrogenase II (ambiguous). Cat No: EXWM-0520. | |
| hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) | This step in the aerobic biosynthesis of cobalamin generates hydrogenobyrinic acid a,c-diamide, the substrate required by EC 6.6.1.2, cobaltochelatase, which adds cobalt to the macrocycle. Group: Enzymes. Synonyms: CobB. Enzyme Commission Number: EC 6.3.5.9. CAS No. 132053-22-6. 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-5811; hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing); EC 6.3.5.9; 132053-22-6; CobB. Cat No: EXWM-5811. | |
| hydrogen:quinone oxidoreductase | Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen). Group: Enzymes. Synonyms: hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase. Enzyme Commission Number: EC 1.12.5.1. CAS No. 151616-65-8. 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-0522; hydrogen:quinone oxidoreductase; EC 1.12.5.1; 151616-65-8; hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase. Cat No: EXWM-0522. | |
| hydrogen-sulfide S-acetyltransferase | This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:hydrogen-sulfide S-acetyltransferase. This enzyme is also called hydrogen-sulfide acetyltransferase. Group: Enzymes. Synonyms: hydrogen-sulfide acetyltransferase. Enzyme Commission Number: EC 2.3.1.10. CAS No. 9029-92-9. 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-2038; hydrogen-sulfide S-acetyltransferase; EC 2.3.1.10; 9029-92-9; hydrogen-sulfide acetyltransferase. Cat No: EXWM-2038. | |
| Hydrolysing for apple juice | Starch hydrolysis for apple juice processing. Applications: Apples & pears processing enzymes. Group: Enzymes. Synonyms: Hydrolysing for apple juice; Apples and Pears Processing Enzymes; Starch hydrolysis enzyme; Hydrolysing;apple juice; Pears Processing; Hydrolysing for apple juice; FJE-1419. Enzymes for apple juice. Appearance: powder or liquid. Hydrolysing for apple juice; Apples and Pears Processing Enzymes; Starch hydrolysis enzyme; Hydrolysing;apple juice; Pears Processing; Hydrolysing for apple juice; FJE-1419. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: FJE-1419. | |
| hydroperoxide dehydratase | Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. The product of the above reaction is unstable and is acted upon by EC 5.3.99.6, allene-oxide cyclase, to form the cyclopentenone derivative (15Z)-12-oxophyto-10,15-dienoate (OPDA), which is the first cyclic and biologically active metabolite in the jasmonate biosynthesis pathway. The enzyme from many plants belongs to the CYP-74 family of P-450 monooxygenases. Group: Enzymes. Synonyms: hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-fo. Enzyme Commission Number: EC 4.2.1.92. AOS. 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-5076; hydroperoxide dehydratase; EC 4.2.1.92; hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]; allene oxide synthase; AOS. Cat No: EXWM-5076. | |
| hydroperoxy fatty acid reductase | The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation. Group: Enzymes. Synonyms: slr1171 (gene name); slr1992 (gene name); hydroperoxy fatty acid:NADPH oxidoreductase. Enzyme Commission Number: EC 1.11.1.22. 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-0504; hydroperoxy fatty acid reductase; EC 1.11.1.22; slr1171 (gene name); slr1992 (gene name); hydroperoxy fatty acid:NADPH oxidoreductase. Cat No: EXWM-0504. | |
| hydroperoxy icosatetraenoate dehydratase | Binds Fe2+. The mammalian enzymes accept a range of hydroperoxyicosatetraenoates (HPETE). The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency. The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE). The enzymes also catalyse the reaction of EC 5.4.4.7, hydroperoxy icosatetraenoate isomerase. Group: Enzymes. Synonyms: epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Enzyme Commission Number: EC 4.2.1.152. 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-4993; hydroperoxy icosatetraenoate dehydratase; EC 4.2.1.152; epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Cat No: EXWM-4993. | |
| hydroperoxy icosatetraenoate isomerase | Binds Fe2+. The enzyme from mammals accepts a range of hydroperoxyicosatetraenoates producing one or several different hydroxyepoxyicosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate. The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate. The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase. Group: Enzymes. Synonyms: epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Enzyme Commission Number: EC 5.4.4.7. 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-5548; hydroperoxy icosatetraenoate isomerase; EC 5.4.4.7; epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Cat No: EXWM-5548. | |
| hydroquinone 1,2-dioxygenase | The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family. It catalyses the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes. Group: Enzymes. Synonyms: hydroquinone dioxygenase; benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.66. 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-0586; hydroquinone 1,2-dioxygenase; EC 1.13.11.66; hydroquinone dioxygenase; benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing). Cat No: EXWM-0586. | |
| hydroquinone glucosyltransferase | Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates. Group: Enzymes. Synonyms: arbutin synthase; hydroquinone:O-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.218. 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-2446; hydroquinone glucosyltransferase; EC 2.4.1.218; arbutin synthase; hydroquinone:O-glucosyltransferase. Cat No: EXWM-2446. | |
| hydroxyacid-oxoacid transhydrogenase | 4-Hydroxybutanoate and (R)-2-hydroxyglutarate can also act as donors; 4-oxobutanoate can also act as acceptor. Group: Enzymes. Synonyms: transhydrogenase, hydroxy acid-oxo acid. Enzyme Commission Number: EC 1.1.99.24. CAS No. 117698-31-4. 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-0453; hydroxyacid-oxoacid transhydrogenase; EC 1.1.99.24; 117698-31-4; transhydrogenase, hydroxy acid-oxo acid. Cat No: EXWM-0453. | |
| hydroxyacylglutathione hydrolase | Also hydrolyses S-acetoacetylglutathione, but more slowly. Group: Enzymes. Synonyms: glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase. Enzyme Commission Number: EC 3.1.2.6. CAS No. 9025-90-5. 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-3569; hydroxyacylglutathione hydrolase; EC 3.1.2.6; 9025-90-5; glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase. Cat No: EXWM-3569. | |
| (hydroxyamino)benzene mutase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. This enzyme participates in naphthalene and anthracene degradation. Group: Enzymes. Synonyms: HAB mutase; hydroxylaminobenzene hydroxymutase; hydroxylaminobenzene mutase. Enzyme Commission Number: EC 5.4.4.1. CAS No. 261765-91-7. 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-5542; (hydroxyamino)benzene mutase; EC 5.4.4.1; 261765-91-7; HAB mutase; hydroxylaminobenzene hydroxymutase; hydroxylaminobenzene mutase. Cat No: EXWM-5542. | |
| hydroxyanthraquinone glucosyltransferase | A range of anthraquinones and some flavones can act as acceptors; best substrates are emodin, anthrapurpurin, quinizarin, 2,6-dihydroanthraquinone and 1,8-dihydroxyanthraquinone. Group: Enzymes. Synonyms: uridine diphosphoglucose-anthraquinone glucosyltransferase; anthraquinone-specific glucosyltransferase. Enzyme Commission Number: EC 2.4.1.181. CAS No. 112198-78-4. 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-2407; hydroxyanthraquinone glucosyltransferase; EC 2.4.1.181; 112198-78-4; uridine diphosphoglucose-anthraquinone glucosyltransferase; anthraquinone-specific glucosyltransferase. Cat No: EXWM-2407. | |
| hydroxybutyrate-dimer hydrolase | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is (R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase. This enzyme is also called D-(-)-3-hydroxybutyrate-dimer hydrolase. This enzyme participates in butanoate metabolism. Group: Enzymes. Synonyms: D-(-)-3-hydroxybutyrate-dimer hydrolase. Enzyme Commission Number: EC 3.1.1.22. CAS No. 37278-37-8. 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-3447; hydroxybutyrate-dimer hydrolase; EC 3.1.1.22; 37278-37-8; D-(-)-3-hydroxybutyrate-dimer hydrolase. Cat No: EXWM-3447. | |
| hydroxycinnamate 4-β-glucosyltransferase | Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120 sinapate 1-glucosyltransferase). Group: Enzymes. Synonyms: uridine diphosphoglucose-hydroxycinnamate glucosyltransferase; UDP-glucose-hydroxycinnamate glucosyltransferase; hydroxycinnamoyl glucosyltransferase. Enzyme Commission Number: EC 2.4.1.126. CAS No. 77848-85-2. 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-2351; hydroxycinnamate 4-β-glucosyltransferase; EC 2.4.1.126; 77848-85-2; uridine diphosphoglucose-hydroxycinnamate glucosyltransferase; UDP-glucose-hydroxycinnamate glucosyltransferase; hydroxycinnamoyl glucosyltransferase. Cat No: EXWM-2351. | |
| hydroxycyclohexanecarboxylate dehydrogenase | Acts on hydroxycyclohexanecarboxylates that have an equatorial carboxy group at C-1, an axial hydroxy group at C-3 and an equatorial hydroxy or carbonyl group at C-4, including (-)-quinate and (-)-shikimate. Group: Enzymes. Synonyms: dihydroxycyclohexanecarboxylate dehydrogenase; (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.166. CAS No. 55467-53-3. 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-0069; hydroxycyclohexanecarboxylate dehydrogenase; EC 1.1.1.166; 55467-53-3; dihydroxycyclohexanecarboxylate dehydrogenase; (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase. Cat No: EXWM-0069. | |
| hydroxydechloroatrazine ethylaminohydrolase | Contains Zn2+. This bacterial enzyme is involved in degradation of the herbicide atrazine. The enzyme has a broad substrate range, and requires a monohydroxylated s-triazine ring with a minimum of one primary or secondary amine substituent and either a chloride or amine leaving group. It catalyses both deamination and dechlorination reactions. Group: Enzymes. Synonyms: atzB (gene name); 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase. Enzyme Commission Number: EC 3.5.4.43. 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-4572; hydroxydechloroatrazine ethylaminohydrolase; EC 3.5.4.43; atzB (gene name); 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase. Cat No: EXWM-4572. | |
| hydroxyethylthiazole kinase | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase. Other names in common use include hydroxyethylthiazole kinase (phosphorylating), and 4-methyl-5-(beta-hydroxyethyl)thiazole kinase. This enzyme participates in thiamine metabolism. Thiamine pyrophosphate (TPP), a required cofactor for many enzymes in the cell, is synthesised de novo in Salmonella typhimurium. Group: Enzymes. Synonyms: hydroxyethylthiazole kinase (phosphorylating); 4-methyl-5-(β-hydroxyethyl)thiazole kinase. Enzyme Commission Number: EC 2.7.1.50. CAS No. 9026-56-6. 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-3081; hydroxyethylthiazole kinase; EC 2.7.1.50; 9026-56-6; hydroxyethylthiazole kinase (phosphorylating); 4-methyl-5-(β-hydroxyethyl)thiazole kinase. Cat No: EXWM-3081. | |
| hydroxyglutamate decarboxylase | A pyridoxal-phosphate protein. Group: Enzymes. Synonyms: 3-hydroxy-L-glutamate 1-carboxy-lyase. Enzyme Commission Number: EC 4.1.1.16. CAS No. 9024-59-3. 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-4760; hydroxyglutamate decarboxylase; EC 4.1.1.16; 9024-59-3; 3-hydroxy-L-glutamate 1-carboxy-lyase. Cat No: EXWM-4760. | |
| hydroxyisourate hydrolase | The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly. Group: Enzymes. Synonyms: HIUHase; 5-hydroxyisourate hydrolase. Enzyme Commission Number: EC 3.5.2.17. CAS No. 255885-20-2. 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-4500; hydroxyisourate hydrolase; EC 3.5.2.17; 255885-20-2; HIUHase; 5-hydroxyisourate hydrolase. Cat No: EXWM-4500. | |
| hydroxylamine dehydrogenase | The enzymes from the nitrifying bacterium Nitrosomonas europaea and the methylotrophic bacterium Methylococcus capsulatus are hemoproteins with seven c-type hemes and one specialized P-460-type heme per subunit. The enzyme converts hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate. While nitrite is the main product, the enzyme from Nitrosomonas europaea can produce nitric oxide as well. Group: Enzymes. Synonyms: HAO (ambiguous); hydroxylamine oxidoreductase (ambiguous); hydroxylamine oxidase (misleading). Enzyme Commission Number: EC 1.7.2.6. CAS No. 9075-43-8. 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-1621; hydroxylamine dehydrogenase; EC 1.7.2.6; 9075-43-8; HAO (ambiguous); hydroxylamine oxidoreductase (ambiguous); hydroxylamine oxidase (misleading). Cat No: EXWM-1621. | |
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