You Searched For: S-Farnesyl-L-cysteine+methyl+ester

Supplier: Enzo Life Sciences

Description: Multidrug resistance transporter activator.

Catalog Number: (10100-398)

Supplier: Prosci

Description: Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. NARF binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. NARF is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases.Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.

Supplier: Enzo Life Sciences

Description: Methyltransferase inhibitor

Catalog Number: (10491-238)

Supplier: Bioss

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: (10491-214)

Supplier: Bioss

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: (10491-220)

Supplier: Bioss

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: (10491-248)

Supplier: Bioss

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: (10491-242)

Supplier: Bioss

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: (10491-246)

Supplier: Bioss

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: (10491-202)

Supplier: Bioss

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: (76107-878)

Supplier: Bioss

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: (76107-876)

Supplier: Bioss

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: (10491-216)

Supplier: Bioss

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: (10491-218)

Supplier: Bioss

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: (10491-224)

Supplier: Bioss

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: (76107-872)

Supplier: Bioss

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.