552 resultater for: "Rapamycin"

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: ProSci Inc.

FKBP3 contains 1 PPIase FKBP-type domain, belongs to the FKBP-type PPIase family. FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. FKBP3 is a cis-trans prolyl isomerase enzyme that binds the immunosuppressants FK506 and rapamycin, as well as histone deacetylases, the transcription factor YY1, casein kinase II, and nucleolin. It has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Bioss

mTOR is one of a family of proteins involved in cell cycle progression, DNA recombination, and DNA damage detection. In rat, it is a 289-kDa protein (symbolized RAFT1) with significant homology to the Saccharomyces cerevisiae protein TOR1 and has been shown to associate with the immunophilin FKBP12 in a rapamycin dependent fashion. The FKBP12-rapamycin complex is known to inhibit progression through the G1 cell cycle stage by interfering with mitogenic signaling pathways involved in G1 progression in several cell types, as well as in yeast. The binding of FRAP to FKBP12-rapamycin correlated with the ability of these ligands to inhibit cell cycle progression.

Supplier: Agrisera

TOR (Target of rapamycin) is an essential cell growth regulator that controls development from early embryo to seed production in response to nutrient availability in envoronmental stress conditions. It belongs to the family of phosphatidylinositol 3-kinase and are targets of the antiproliferative drug rapamycin. AtTOR is expressed in embryos, endosperm and meristems. Acts through the phosphorylation of downstream effectors that are recruited by the binding partner RAPTOR. Acts by activating transcription, protein synthesis and ribosome biogenesis, and inhibiting mRNA degradation and autophagy.,TOR (Target of rapamycin) is an essential cell growth regulator that controls development from early embryo to seed production in response to nutrient availability in envoronmental stress conditions. It belongs to the family of phosphatidylinositol 3-kinase and are targets of the antiproliferative drug rapamycin. AtTOR is expressed in embryos, endosperm and meristems. Acts through the phosphorylation of downstream effectors that are recruited by the binding partner RAPTOR. Acts by activating transcription, protein synthesis and ribosome biogenesis, and inhibiting mRNA degradation and autophagy.

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene.

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene.

Supplier: ProSci Inc.

TOR Antibody: The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. It was initially discovered as a kinase whose ability to stimulate T cell proliferation in response to IL-2 could be inhibited by the immunosuppressive drug rapamycin. Rapamycin inhibits TOR in other cell types resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. TOR is normally associated with the regulatory proteins RAPTOR and GbetaL. Its downstream targets are thought to be the ribosomal protein S6 kinases and the eukaryotic initiation factor 4E binding proteins (4EBPs). Regulation of these protein families allows TOR to control protein biosynthesis.

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The protein encoded by this gene belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNA damage and nutrient deprivation. This protein acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. The ANGPTL7 gene is located in an intron of this gene. [provided by RefSeq, Sep 2008]

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11?s peptidyl-prolyl isomerase activity.

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11?s peptidyl-prolyl isomerase activity.

Supplier: Bioss

The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.