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| Product | Description | |
|---|---|---|
| Zinc Methionine | Zinc Methionine. |  |
| 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase | Requires phosphate and contains zinc. The enzyme from Escherichia coli also requires a reducing system. Unlike EC 2.1.1.13, methionine synthase, this enzyme does not contain cobalamin. Group: Enzymes. Synonyms: tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Enzyme Commission Number: EC 2.1.1.14. CAS No. 9068-29-5. 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-1735; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase; EC 2.1.1.14; 9068-29-5; tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Cat No: EXWM-1735. |  |
| betaine-homocysteine S-methyltransferase | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively. Group: Enzymes. Synonyms: betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase. Enzyme Commission Number: EC 2.1.1.5. CAS No. 9029-78-1. 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-1953; betaine-homocysteine S-methyltransferase; EC 2.1.1.5; 9029-78-1; betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase. Cat No: EXWM-1953. | |
| Betaine Homocysteine S-methyltransferase, Recombinant | In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) ? dimethylglycine (hydrogen receiver) + methionine (methyl receiver). Group: Enzymes. Synonyms: Betaine-homocysteine S-methyltransferase; Betaine homocysteine S-methyltransferase; Betaine-homocysteine S methyltransferase; Betaine homocysteine S methyltransferase; betaine-homocysteine methyltransferase; BHMT; 9029-78-1; EC 2.1.1.5. Enzyme Commission Number: EC 2.1.1.5. CAS No. 9029-78-1. Purity: 90% (SDS-PAGE test). Mole weight: About 47 kDa ?SDS-PAGE?. Storage: 4°C,store at -20°C for long-term preservation. Form: White powder, lyophilized. Betaine-homocysteine S-methyltransferase; Betaine homocysteine S-methyltransferase; Betaine-homocysteine S methyltransferase; Betaine homocysteine S methyltransferase; betaine-homocysteine methyltransferase; BHMT; 9029-78-1; EC 2.1.1.5. Cat No: NATE-1684. | |
| D-Gluconic acid zinc (II) salt | D-Gluconic acid zinc (II) salt, an invaluable biomedical resource, demonstrates immense potential for therapeutic efficacy across diverse conditions. Meticulous studies have unveiled its profound implications in mitigating zinc insufficiency and its associated ailments. As a remarkable zinc supplement, it seamlessly facilitates the preservation of cellular homeostasis while fortifying immune resilience. Uses: Cattle dermatomycosis, caused by trichophyton verrucosum (trichophytosis) was treated by oral admin of prepn containing 20-70% zinc gluconate, 2-10% sulfur, 0.2-1% vitamin a (106 iu), 2-6% methionine, & inert carrier such as calcium carbonate or flour. Synonyms: Zinc Gluconate dihydrate. CAS No. 4468-2-4. Molecular formula: C12H22O14Zn. Mole weight: 455.68. |  |
| methionine synthase | Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin-NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase, which acts only on the triglutamate. Group: Enzymes. Synonyms: 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethy. Enzyme Commission Number: EC 2.1.1.13. CAS No. 9033-23-2. 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-1727; methionine synthase; EC 2.1.1.13; 9033-23-2; 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethylase; N-methyltetrahydrofolate:L-homocysteine methyltransferase; N5-methyltetrahydrofolate methyltransferase; N5-methyltetrahydrofolate- | |
| protein farnesyltransferase | This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, γ-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity. Group: Enzymes. Synonyms: FTase. Enzyme Commission Number: EC 2.5.1.58. CAS No. 131384-38-8. 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-2795; protein farnesyltransferase; EC 2.5.1.58; 131384-38-8; FTase. Cat No: EXWM-2795. | |
| protein geranylgeranyltransferase type I | This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most γ-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding. Group: Enzymes. Synonyms: GGTase-I; GGTaseI. Enzyme Commission Number: EC 2.5.1.59. CAS No. 135371-29-8. 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-2796; protein geranylgeranyltransferase type I; EC 2.5.1.59; 135371-29-8; GGTase-I; GGTaseI. Cat No: EXWM-2796. | |
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