You Searched For: Erythrosin+B

Catalog Number: (BOSSBS-13025R-FITC)

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-A647)

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-13026R-CY5)

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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13026R)

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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13026R-HRP)

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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13025R-A488)

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

Sale

Catalog Number: (BOSSBS-4256R-A488)

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

Sale

Catalog Number: (BOSSBS-4256R-A750)

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 centres can be oxidised to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidised Trx is catalysed 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

Sale

Catalog Number: (BOSSBS-13026R-CY7)

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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (PRSI29-562)

Supplier: ProSci Inc.

Description: MAT1A catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. MAT1A is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in its gene are associated with methionine adenosyltransferase deficiency.This gne encodes methionine adenosyltransferase I (alpha isoform), which catalyzes the formation of S-adenosylmethionine from methionine and ATP. Methionine adenosyltransferase deficiency is caused by recessive and dominant mutations, the latter identified in autosomal dominant persistant hypermethioninemia.

UOM: 1 * 100 µG

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Catalog Number: (PRSI55-466)

Supplier: ProSci Inc.

Description: The N-terminal methionine excision pathway is an essential process in which the N-terminal methionine is removed from many proteins, thus facilitating subsequent protein modification. In mitochondria, enzymes that catalyze this reaction are celled methionine aminopeptidases (MetAps, or MAPs; EC 3.4.11.18) (Serero et al., 2003 [PubMed 14532271]).

UOM: 1 * 400 µl

New Product Sale

Catalog Number: (BOSSBS-13026R-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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (PRSI55-674)

Supplier: ProSci Inc.

Description: May have S-adenosyl-L-methionine-dependent methyl-transferase activity (Potential).

UOM: 1 * 400 µl

New Product Sale

Catalog Number: (PRSI55-760)

Supplier: ProSci Inc.

Description: May have S-adenosyl-L-methionine-dependent methyl-transferase activity (Potential).

UOM: 1 * 400 µl

New Product Sale

Catalog Number: (BOSSBS-13026R-A488)

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, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-13025R-CY7)

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

Sale