You Searched For: Isoamyl+acrylate

Description: Anti-Methionine adenosyltransferase Rabbit Polyclonal Antibody (FITC (Fluorescein))

Catalog Number: BIRBORB9208-100

UOM: 1 * 100 µG

Supplier: Biorbyt

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localisation of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the Signalling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-A680

UOM: 1 * 100 µl

Supplier: Bioss

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-A350

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: BOSSBS-9548R-A750

UOM: 1 * 100 µl

Supplier: Bioss

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-FITC

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: BOSSBS-9548R-A350

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: BOSSBS-9548R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: BOSSBS-9548R-FITC

UOM: 1 * 100 µl

Supplier: Bioss

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Description: MAT1A 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.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.

Catalog Number: PRSI29-561

UOM: 1 * 100 µG

Supplier: ProSci Inc.

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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.

Catalog Number: BOSSBS-13025R

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Fmoc-Met(O)-OH ≥98% (by HPLC), Novabiochem®

Catalog Number: 04-12-1112-5

UOM: 1 * 5 g

Supplier: Novabiochem (Part of Merck)

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-CY5

UOM: 1 * 100 µl

Supplier: Bioss

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Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-CY5.5

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: BOSSBS-9548R-CY5

UOM: 1 * 100 µl

Supplier: Bioss

Sale

Description: FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.

Catalog Number: BOSSBS-9547R-A488

UOM: 1 * 100 µl

Supplier: Bioss

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