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| Product | Description | |
|---|---|---|
| glutathione γ-glutamylcysteinyltransferase | This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. Group: Enzymes. Synonyms: phytochelatin synthase; γ-glutamylcysteine dipeptidyl transpeptidase. Enzyme Commission Number: EC 2.3.2.15. CAS No. 125390-02-5. 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-2288; glutathione γ-glutamylcysteinyltransferase; EC 2.3.2.15; 125390-02-5; phytochelatin synthase; γ-glutamylcysteine dipeptidyl transpeptidase. Cat No: EXWM-2288. |  |
| Native Bovine Gamma-Glutamyl Transferase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular ...transferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. Purity: Purified. γ-GT. Activity: > 30 U/mg (Dimension Clinical Chemistry System). Appearance: Tan Powder. Storage: -20°C. Form: Lyophilized. Source: Bovine Kidney. Species: Bovine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0790. | |
| Native Human Gamma-Glutamyl Transferase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl tr. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: >50 U/mg. Storage: 4°C. Source: Human Liver. Species: Human. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0792. | |
| protein-glutamine γ-glutamyltransferase | Requires Ca2+. The γ-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII. Group: Enzymes. Synonyms: transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. 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-2286; protein-glutamine γ-glutamyltransferase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase. Cat No: EXWM-2286. | |
| ribostamycin:4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoate transferase | The enzyme attaches the side chain of the aminoglycoside antibiotics of the butirosin family. The side chain confers resistance against several aminoglycoside-modifying enzymes. Group: Enzymes. Synonyms: btrH (gene name). Enzyme Commission Number: EC 2.3.2.19. 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-2292; ribostamycin:4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoate transferase; EC 2.3.2.19; btrH (gene name). Cat No: EXWM-2292. | |
| Biotinylated Transglutaminase from Human, Proenzyme (Zymogen) | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 3 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. biotinylated transglutaminase 3 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transgl...]. Appearance: Liquid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Transglutaminase is a Ca2+-dependent enzyme. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 100 ug. Cat No: NATE-173 | |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| Endotoxin free Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. this product is suitable for cell culture use. Group: Enzymes. Synonyms: transglutaminase; ...rand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is supplied in 10 mM Tris-HCl pH 7.2, 150 mM NaCl, 0.5 mM EDTA, 0.5 mM DTT, 10% Glycerol. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. Cat No: NATE-1729. | |
| Ezatiostat hydroChloride | Ezatiostat hydrochloride is the hydrochloride salt form of Ezatiostat. Ezatiostat, also called as Telintra or TER 199, is a liposomal small-molecule glutathione analog inhibitor of glutathione S-transferase (GST) P1-1 with hematopoiesis-stimulating activi. Synonyms: ethyl (2S)-2-amino-5-[[(2R)-3-benzylsulfanyl-1-[[(1R)-2-ethoxy-2-oxo-1-phenylethyl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoate;hydrochloride ezatiotsat gamma-Glu-S-BzCys-PhGly diethyl ester gamma-glutamyl-S-(benzyl)cysteinyl-phenylglycine diethyl ester. CAS No. 286942-97-0. Molecular formula: C27H35N3O6S.HCl. Mole weight: 566.11. |  |
| γ-GT | γ-GT(63699-78-5) is a substrate for γ-glutamyl transferase in biochemical test. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 63699-78-5. Pack Sizes: 10 mM * 1 mL; 25 mg; 50 mg; 100 mg. Product ID: HY-15936. |  |
| gamma-L-Glutamic acid 7-amido-4-methylcoumarin | L-Glutamic acid γ-(7-amido-4-methylcoumarin) is a substrate for aminopeptidase or the assay of γ-glutamyl transferase producing a blue fluorescent solution upon cleavage. Synonyms: H-GLU(AMC)-OH; L-Glutamic Acid Gamma-(7-Amido-4-Methylcoumarin). Grades: ≥ 99% (HPLC). CAS No. 72669-53-5. Molecular formula: C15H16N2O5. Mole weight: 304.30. | |
| gamma-L-Glutamyl-alpha-naphthylamide | Gamma-L-Glutamyl-alpha-naphthylamide, a widely used enzymatic substrate, serves as a crucial tool in the identification of gamma-glutamyl transferase (GGT) activity in diverse physiological and pathological scenarios. Converging evidence has linked elevated levels of GGT to several diseases, spanning from liver and pancreatic cancer to alcoholism and cholestasis. By exploiting Gamma-L-Glutamyl-alpha-naphthylamide as a probe, scholars have unraveled new facets of GGT-related biochemistry, paving the way to the development of innovative therapeutic interventions. CAS No. 81012-91-1. Molecular formula: C16H18N2O5. Mole weight: 318.32. | |
| 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 | |
| L-Glutathione, Reduced | L-Glutathione, Reduced. Synonyms: γ-L-Glutamyl-L-cysteinyl-glycine, GSH. CAS No. 70-18-8. Product ID: CDC10-0057. Molecular formula: C10H17N3O6S. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; L-Glutathione, Reduced; CDC10-0057; 70-18-8; C10H17N3O6Sl; γ-L-Glutamyl-L-cysteinyl-glycine, GSH; 200-725-4; MFCD00065939; 70-18-8. Purity: ≥98.0%. Color: White. EC Number: 200-725-4. Physical State: Powder. Solubility: H2O: 50 mg/mL. Quality Level: 300. Storage: 2-8°C. Application: L-Glutathione (GSH) reduced has been used in the elution buffer to elute GST (glutathione S-transferase)-fused proteins using glutathione-agarose beads. It has been used to prepare a standard curve for GSH analyses. Boiling Point: 754.5±60.0 °C(Predicted). Melting Point: 192-195 °C (dec.) (lit.). Density: 1.4482 g/mL(rough estimate). |  |
| lipid II:glycine glycyltransferase | The enzyme from Staphylococcus aureus catalyses the transfer of glycine from a charged tRNA to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc (lipid II), attaching it to the N6 of the L-Lys at position 3 of the pentapeptide. This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S. aureus for the crosslinking of different glycan strands to each other. Four additional Gly residues are subsequently attached by EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase) and EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). Group: Enzymes. Synonyms: N-acetylmuramoyl-L-alanyl-D-glu. Enzyme Commission Number: EC 2.3.2.16. 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-2289; lipid II:glycine glycyltransferase; EC 2.3.2.16; N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase; femX (gene name); alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase. Cat No: EXWM-2289. | |
| Native Equine γ-Glutamyltranspeptidase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; . Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 5-12 units/mg solid. Storage: -20°C. Source: Equine kidney. Species: Equine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0791. | |
| Native Guinea pig Transglutaminase | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptide...h as huntington?s disease and alzheimer?s disease.transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tr | |
| Native Porcine γ-Glutamyltranspeptidase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellul...ase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 2.0-6.0 units/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0793. | |
| RTA-408 | RTA-408 is a member of the synthetic oleanane triterpenoid class of compounds and an activator of nuclear factor erythroid 2 [NF-E2]-related factor 2 (Nrf2, Nfe2l2), with potential chemopreventive activity. Upon administration, RTA 408 activates the cytoprotective transcription factor Nrf2. In turn, Nrf2 translocates to the nucleus, dimerizes with a small Maf protein (sMaf), and binds to the antioxidant response element (ARE). This induces the expression of a number of cytoprotective genes, including NAD(P)H quinone oxidoreductase 1 (NQO1), sulfiredoxin 1 (Srxn1), heme oxygenase-1 (HO1, HMOX1), superoxide dismutase 1 (SOD1), gamma-glutamylcysteine synthetase (gamma-GCS), thioredoxin reductase-1 (TXNRD1), glutathione S-transferase (GST), glutamate-cysteine ligase catalytic subunit (Gclc) and glutamate-cysteine ligase regulatory subunit (Gclm), and increases the synthesis of the antioxidant glutathione (GSH). Nrf2, a leucine zipper transcription factor, plays a key role in the maintenance of redox balance and cytoprotection against oxidative stress. Synonyms: RTA408; RTA408; RTA-408. Omaveloxolone; Propanamide, N-(2-cyano-3,12-dioxo-28-noroleana-1,9(11)-dien-17-yl)-2,2-difluoro-. Grades: >98%. CAS No. 1474034-05-3. Molecular formula: C33H44F2N2O3. Mole weight: 554.723. | |
| S- (2-Hydroxyethyl) glutathione | A glutathione derivative as inhibitor of glutathione S-transferase. Group: Biochemicals. Alternative Names: L-γ-Glutamyl-S-(2-hydroxyethyl)-L-cysteinylglycine; L-N-[1-[ (Carboxymethyl) carbamoyl]-2-[ (2-hydroxyethyl) thio]ethyl]glutamine; N-[N-L-γ-Glutamyl-S-(2-hydroxyethyl)-L-cysteinyl]glycine; S-( β -Hydroxyethyl) glutathione. Grades: Highly Purified. CAS No. 28747-20-8. Pack Sizes: 25mg. US Biological Life Sciences. |  Worldwide |
| S- (2-Hydroxyethyl) glutathione-d4 Hydrochloride | A labeled glutathione derivative as inhibitor of glutathione S-transferase. Group: Biochemicals. Alternative Names: L-γ-Glutamyl-S-(2-hydroxyethyl-d4)-L-cysteinylglycine Hydrochloride; N-[1-[ (Carboxymethyl) carbamoyl]-2-[ (2-hydroxyethyl-d4) thio]ethyl]tamine Hydrochloride; S-( β-Hydroxyethyl-d4)glutathione Hydrochloride. Grades: Highly Purified. Pack Sizes: 1mg. US Biological Life Sciences. | Worldwide |
| S-(2-Hydroxyethyl)glutathione-d4 Hydrochloride | A labelled glutathione derivative. It acts as an inhibitor of glutathione S-transferase. Synonyms: L-γ-Glutamyl-S-(2-hydroxyethyl-d4)-L-cysteinylglycine Hydrochloride; N-[1-[(Carboxymethyl)carbamoyl]-2-[(2-hydroxyethyl-d4)thio]ethyl]-L-glutamine Hydrochloride; S-(β-Hydroxyethyl-d4)glutathione Hydrochloride. Molecular formula: C12H18D4ClN3O7S. Mole weight: 391.86. | |
| S- (2-Hydroxyethyl) glutathione Hydrochloride | A glutathione derivative as inhibitor of glutathione S-transferase. Group: Biochemicals. Alternative Names: L-γ-Glutamyl-S-(2-hydroxyethyl)-L-cysteinylglycine Hydrochloride; N-[1-[ (Carboxymethyl) carbamoyl]-2-[ (2-hydroxyethyl) thio]ethyl]. Grades: Highly Purified. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| S, S'-Ethylenebis (glutathione) | S, S'-Ethylenebis (glutathione) is a haloethane-glutathione conjugate formed via GSH transferases. S, S'-Ethylenebis (glutathione) formation is used to study the polymorphism in glutathione conjugation activity of human erythrocytes towards ethylene dibromide. Group: Biochemicals. Alternative Names: 2,2'-(1,2-Ethanediyl)bis[L-γ-glutamyl-L-cysteinylglycine. Grades: Highly Purified. Pack Sizes: 2.5mg. US Biological Life Sciences. | Worldwide |
| Transglutaminase 2 from Cynomolgus, Recombinant | Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation. Applications: Labeling, immobilisation, conjugation and modification of proteins. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; trans...l., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20°C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The purified transglutaminase is lyophilized from 10 mM Tris-HCl pH 7.4, 300 mM NaCl, 1 mM DTT, 1 mM EDTA, contains maltodextrin. Source: HEK-293F. Species: Cynomolgus. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine & | |
| Transglutaminase 2 from Dog, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor X...1). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Dog. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μ | |
| Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa...e: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. | |
| Transglutaminase 7 from Human, Recombinant | Transglutaminase 7 is based on the TGM7-gene on plasmid pCRII-hTGz cl.14 (isolated by Daniel Aeschlimann), corrected by the insertion of a C at position 1169. It is N-terminally fused to a hexahistidine-tag. Applications: The transglutaminase 7 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 7 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; ...nd et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at ≤ -20?°C.Store working aliquots at ≤ -20?°C. Avoid repeated freezing and thawing.Delivery at ambient temperature is possible. Form: The Transglutaminase is lyophilized from 50 mM Tris-HCl pH 8. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg. Cat No: | |
| Transglutaminase from guinea pig liver, Recombinant | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chai...tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg. Storage: at -20°C. Form: Lyophilized powder from 5.0 mM Tris, pH 7.5, 0.5 mM DTE and 1 mM CaCl2. Source: Sf9 cells. Species: Guinea pig liver. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Cat No: NATE-1247. | |
| Transglutaminase from Mouse, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant mouse transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutaminase; EC ...ng to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Biotinylated-transglutaminase is a Ca2+-dependent enzyme. Source: Insect cells. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltra | |
| Transglutaminase from Streptoverticillium mobaraense (food grade) | Transglutaminase from Streptoverticillium mobaraense consists of 331 amino acid residues. The molecular mass is approximately 38 kDa. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. Transglutaminase. Activity: 100 U/g. Source: Streptoverticillium mobaraense. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Cat No: NATE-0879. | |
| UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase | Also acts on L-seryl-tRNASer. Group: Enzymes. Synonyms: alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase; UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase; uridine diphosphoacetylmuramoylpentapeptide lysine N6-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine 6-N-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase. Enzyme Commission Number: EC 2.3.2.10. CAS No. 37257-26-4. 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-2283; UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase; EC 2.3.2.10; 37257-26-4; alanyl-transfer ribonucleate-uridine diphosphoacetylmuramoylpentapeptide transferase; UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase; uridine diphosphoacetylmuramoylpentapeptide lysine N6-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine 6-N-alanyltransferase; L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine N6-alanyltransferase. Cat No: EXWM-2283. | |
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