You Searched For: L-Methionine+sulphoximine

Catalog Number: (BOSSBS-13025R-A680)

Supplier: Bioss

Description: Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4256R-CY5)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4256R-FITC)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4256R-CY3)

Supplier: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Catalog Number: (PRSIXW-RP3143)

Supplier: ProSci Inc.

Description: Methionine adenosyltransferase (EC 2.5.1.6) catalyzes the biosynthesis of S-adenosylmethionine (AdoMet) from methionine and ATP. AdoMet is the major methyl donor for many of the transmethylation reactions in the body. The MAT2A promoter is highly GC rich, especially in the first 300 bp. The promoter contains several potential SP1-, v-myb-, and GATA-binding sites, as well as potential binding sites for C/EBP, HSF2, c-myb, and STATx. It can efficiently drive expression from a reporter gene in both Jurkat and 293 cells.

UOM: 1 * 100 µG

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Supplier: Merck Millipore (Calbiochem‎)

Description: It increases the expression of glutathione peroxidase.

Catalog Number: (PRSI26-100)

Supplier: ProSci Inc.

Description: CTH is a cytoplasmic enzyme in the trans-sulfuration pathway that converts cystathione derived from methionine into cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in its gene cause cystathioninuria.This gene encodes a cytoplasmic enzyme in the trans-sulfuration pathway that converts cystathione derived from methionine into cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in this gene cause cystathioninuria. Alternative splicing of this gene results in two transcript variants encoding different isoforms.

UOM: 1 * 50 µG

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Supplier: MP Biomedicals

Description: Iodoacetamide is a thiol reagent; alkylating reagent for cysteine and histidine residues in proteins. In the alkylation reaction, it reacts with histidine (such as in RNase), methionine and sulfhydryl groups of many proteins.

Catalog Number: (PRSI55-116)

Supplier: ProSci Inc.

Description: This gene encodes the auxiliary subunit of the heteromeric N-terminal acetyltransferase B complex. This complex acetylates methionine residues that are followed by acidic or asparagine residues.

UOM: 1 * 400 µl

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Catalog Number: (USBI038097)

Supplier: US Biological

Description: Anti-METAP1D Rabbit Polyclonal Antibody

UOM: 1 * 200 µl

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Catalog Number: (PRSI30-465)

Supplier: ProSci Inc.

Description: NSUN3 belongs to the methyltransferase superfamily. RsmB/NOP family. It may have S-adenosyl-L-methionine-dependent methyl-transferase activity.

UOM: 1 * 50 µG

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Catalog Number: (PRSI55-106)

Supplier: ProSci Inc.

Description: N-methylation is one method by which drug and other xenobiotic compounds are metabolized by the liver. NNMT is the protein responsible for this enzymatic activity, which uses S-adenosyl methionine as the methyl donor.

UOM: 1 * 400 µl

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Catalog Number: (PRSI55-680)

Supplier: ProSci Inc.

Description: Probable S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNA. May also have a role in tRNA stabilization or maturation (By similarity).

UOM: 1 * 400 µl

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Catalog Number: (PRSI26-321)

Supplier: ProSci Inc.

Description: TRMT11 belongs to the methyltransferase superfamily. It is a catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.

UOM: 1 * 50 µG

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Catalog Number: (786-13)

Supplier: G-Biosciences

Description: SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It is therefore recommended to always use the shortest digestion time possible.

UOM: 1 * 2 items

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Catalog Number: (PRSI26-362)

Supplier: ProSci Inc.

Description: TRMT2B (CXorf34) is probable S-adenosyl-L-methionine-dependent methlytransferase that catalyzes the formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNA. And it may also have a role in tRNA stabilization or maturation.

UOM: 1 * 50 µG

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