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4-(2-Hydroxyhexafluoroisopropyl)benzoic+acid


52,444  results were found

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Supplier:  Bioss
Description:   Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade.

Supplier:  Bioss
Description:   In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the synthesis of either guanine or adenine nucleotides. In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the oxidation of IMP to XMP, and GMP synthetase, which catalyzes the amination of XMP to GMP. [provided by RefSeq, Jul 2008].
Catalog Number: (10298-456)

Supplier:  Bioss
Description:   In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the synthesis of either guanine or adenine nucleotides. In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the oxidation of IMP to XMP, and GMP synthetase, which catalyzes the amination of XMP to GMP. [provided by RefSeq, Jul 2008].

Supplier:  Bioss
Description:   Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF through replacement of GDP with GTP.
Catalog Number: (10298-634)

Supplier:  Bioss
Description:   GTPases from the MMR1/HSR1 GTP-binding protein subfamily are circularly rearranged G-motifs that play a critical role in maintaining normal cell growth. Deletion of these genes results in severe growth defects with a marked reduction in mature rRNA species and a concomitant accumulation of the 35S pre-rRNA transcript. Deletion also causes the ribosomal protein Rpl25a to fail exportation from the nucleolus. Deletion of any of the G-domain motifs will result in a null phenotype and nuclear/nucleolar localization that lacks the nucleolar export of preribosomes and is accompanied by a distortion of the nucleolar structure. GNL3L (guanine nucleotide binding protein-like 3 (nucleolar)-like) is a 582 amino acid nuclear protein that belongs to the MMR1/HSR1 GTP-binding protein family. Containing one G (guanine nucleotide-binding) domain, GNL3L is required for normal processing of ribosomal pre-rRNA and for cell proliferation.

Supplier:  Bioss
Description:   Members of the RAS subfamily of GTPases function in signal transduction as GTP/GDP-regulated switches that cycle between inactive GDP- and active GTP-bound states. Guanine nucleotide exchange factors (GEFs), such as Repac, serve as RAS activators by promoting acquisition of GTP to maintain the active GTP-bound state and are the key link between cell surface receptors and RAS activation. Repac, also known as Rap guanine nucleotide exchange factor 5 (RAPGEF5), is a 580 amino acid protein that is expressed in brain and testis, with weaker expression in heart, placenta, lung, pancreas and small intestine. Existing as two alternatively spliced isoforms, the Repac gene is conserved in cow, mouse and rat. The gene that encodes Repac maps to human chromosome 7p15.3, with high expression of this region linking to positive response to erlotinib therapy for those with non-small-cell lung cancer.

Supplier:  Bioss
Description:   GTPases from the MMR1/HSR1 GTP-binding protein subfamily are circularly rearranged G-motifs that play a critical role in maintaining normal cell growth. Deletion of these genes results in severe growth defects with a marked reduction in mature rRNA species and a concomitant accumulation of the 35S pre-rRNA transcript. Deletion also causes the ribosomal protein Rpl25a to fail exportation from the nucleolus. Deletion of any of the G-domain motifs will result in a null phenotype and nuclear/nucleolar localization that lacks the nucleolar export of preribosomes and is accompanied by a distortion of the nucleolar structure. GNL3L (guanine nucleotide binding protein-like 3 (nucleolar)-like) is a 582 amino acid nuclear protein that belongs to the MMR1/HSR1 GTP-binding protein family. Containing one G (guanine nucleotide-binding) domain, GNL3L is required for normal processing of ribosomal pre-rRNA and for cell proliferation.

Supplier:  Bioss
Description:   Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade.
Supplier:  Bioss
Description:   Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade.
Supplier:  Bioss
Description:   Rho GTPases are GTP binding proteins that regulate a wide spectrum of cellular functions. These cellular processes include cytoskeletal rearrangements, gene transcription, cell growth and motility. Activation of Rho GTPases is under the direct control of guanine nucleotide exchange factors (GEFs). The protein encoded by this gene is a guanine nucleotide exchange factor and belongs to the Rho GTPase GFE family. Family members share a common feature, a Dbl (DH) homology domain followed by a pleckstrin (PH) homology domain. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Oct 2008].
Catalog Number: (10751-510)

Supplier:  Prosci
Description:   EPAC2 Antibody: EPAC2, also known as Rap guanine nuclear exchange factor 4 and cAMPGEF-II, is belongs to a family of cyclic adenosine monophosphate (cAMP) binding proteins with guanine nucleotide exchange factor. Like the related protein EPAC1, EPAC2 signaling plays a role in numerous cellular processes such as integrin-mediated cell adhesion, muscle contraction, learning and memory, cell proliferation, and inflammation. Recent evidence suggests that EPAC2 induces synapse remodeling and depression, with mutations in its gene being found in patients with autism.
Catalog Number: (89358-030)

Supplier:  Genetex
Description:   Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human, Mouse Tested Applications: ICC/IF, IHC-P, WB Pkg Size: 100 ul
Supplier:  Bioss
Description:   Members of the RAS subfamily of GTPases function in signal transduction as GTP/GDP-regulated switches that cycle between inactive GDP- and active GTP-bound states. Guanine nucleotide exchange factors (GEFs), such as Repac, serve as RAS activators by promoting acquisition of GTP to maintain the active GTP-bound state and are the key link between cell surface receptors and RAS activation. Repac, also known as Rap guanine nucleotide exchange factor 5 (RAPGEF5), is a 580 amino acid protein that is expressed in brain and testis, with weaker expression in heart, placenta, lung, pancreas and small intestine. Existing as two alternatively spliced isoforms, the Repac gene is conserved in cow, mouse and rat. The gene that encodes Repac maps to human chromosome 7p15.3, with high expression of this region linking to positive response to erlotinib therapy for those with non-small-cell lung cancer.
Supplier:  Bioss
Description:   HERC1 is a stimulates guanine nucleotide exchange on ARF1 and Rab proteins. This protein may be involved in membrane transport processes.

Supplier:  Bioss
Description:   GTPases from the MMR1/HSR1 GTP-binding protein subfamily are circularly rearranged G-motifs that play a critical role in maintaining normal cell growth. Deletion of these genes results in severe growth defects with a marked reduction in mature rRNA species and a concomitant accumulation of the 35S pre-rRNA transcript. Deletion also causes the ribosomal protein Rpl25a to fail exportation from the nucleolus. Deletion of any of the G-domain motifs will result in a null phenotype and nuclear/nucleolar localization that lacks the nucleolar export of preribosomes and is accompanied by a distortion of the nucleolar structure. GNL3L (guanine nucleotide binding protein-like 3 (nucleolar)-like) is a 582 amino acid nuclear protein that belongs to the MMR1/HSR1 GTP-binding protein family. Containing one G (guanine nucleotide-binding) domain, GNL3L is required for normal processing of ribosomal pre-rRNA and for cell proliferation.

Supplier:  Bioss
Description:   Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
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