106116 Results for: "Farnesyl+thiosalicylic+acid+amide"

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 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.

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: 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 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.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localised to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterised by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

FDPS is a 419 amino acid enzyme belonging to the FPP/GGPP synthetase family. Localized to cytoplasm and peroxisome, FDPS expression is regulated by phorbol esters and polyunsaturated fatty acids. FDPS assists in cholesterol biosynthesis, post-translational protein modifications and synthesis of steroid hormones in the isoprenoid pathway.FDPS catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FDPS is inactivated by interferon-induced RSAD2, which may result in the disruption of lipid rafts at the plasma membrane. Existing as a homodimer, FDPS may have anti-viral effects when inactivated by RSAD2. Reduced activity of FDPS in liver may partly be the cause of Zellweger syndrome and neonatal adrenoleukodystrophy, both of which are known to be peroxisomal deficiency diseases.

Supplier: Bioss

RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.