106113 Results for: "Farnesyl+thiosalicylic+acid+amide"

Supplier: Cayman Chemical

Farnesyl thiosalicylic acid amide

Supplier: Cayman Chemical

Association of Ras protein with the inner surface of the plasma membrane is required for Ras signaling activity. Farnesyl thiosalicylic acid (FTS) is an inhibitor of Ras-mediated signaling that functions by dislodging Ras from the cell membrane thereby rendering it susceptible to proteolytic degradation.

Supplier: TCI

Farnesyl thiosalicylic acid ≥96.0% (by HPLC, titration analysis)

Supplier: Merck

Thiosalicylic acid for synthesis, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific

Thiosalicylic acid ≥98%

Supplier: TCI

Thiosalicylic acid ≥90.0% (by titrimetric analysis)

Supplier: Thermo Fisher Scientific

Thiosalicylic acid 98%

Supplier: TCI

Sodium thiosalicylate ≥95.0% (by titrimetric analysis)

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Thermo Fisher Scientific

Methyl thiosalicylate 97%

Supplier: Bioss

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.

Supplier: Apollo Scientific

Methyl thiosalicylate 95%

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Thermo Fisher Scientific

Methyl thiosalicylate ≥97%

Supplier: TCI

Methyl thiosalicylate ≥98.0% (by GC)