266 Results for: "PP1"

Supplier: ProSci Inc.

The protein encoded by this gene is associated with the nuclear scaffold in proliferating cells. It was found to bind to the catalytic subunit of protein phosphatase-1 (PP1) and inhibit PP1 activity, suggesting that this protein may function as a regulatory subunit of PP1. Alternative splicing at this locus results in several transcript variants encoding different isoforms.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: US Biological

PROTEIN PHOSPHATASE 1 PP1 PAB CH XHU 1 * 1 mg

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Eukaryotic protein phosphorylation and dephosphorylation on serine and threonine residues regulates numerous cell functions, including division, homeostasis and apoptosis. A group of proteins that play a major role in this process are the serine/threonine protein phosphatases. Protein phosphatase (PP) holoenzyme is a trimeric complex that contains a regulatory subunit, a variable subunit and a catalytic subunit. Families of PP catalytic subunits include PP1, PP2A, PP2B, PP2C, PPX and PP5. Regulatory subunits include nuclear inhibitor of PP1 (NIPP1), PP1 nuclear targeting subunit (PNUTS), PP2A-A, PP2A-B, PP2A-B56, PP2A-C, PP2B-B and PR48. PNUTS, also designated CAT53 or FB19, is encoded by the gene PPP1R10. PNUTS acts as an inhibitor for the phosphatase activity of PP1 Alpha and PP1 Gamma. It is a nuclear protein primarily detected in nucleoplasmic bodies and within nucleoli. PNUTS expression levels are highest in brain, heart, lung, placenta, liver, kidney, pancreas and skeletal muscle.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: Bioss

Inhibitor subunit of the major nuclear protein phosphatase 1 (PP1). It has RNA binding activity but does not cleave RNA and may target PP1 to RNA associated substrates. May also be involved in pre mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.

Supplier: ProSci Inc.

SH3RF2 Antibody: Although the SH3 domain containing ring finger 2 protein (SH3RF2) has been identified as a marker of the nucleus accumbens in the human brain, little is known about this protein. Recent yeast two-hybrid experiments have shown that SH3RF2 associates with protein phosphatase 1 (PP1) and is expressed primarily in heart and testis tissue. Recombinant SH3RF2 enhanced PP1 enzymatic activity and antagonized the ability of phopho-inhibitor-1 or -2 to inhibit PP1, suggesting that SH3RF2 may play a role working with PP1 in cardiac functions.

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development. Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation. Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells. Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain. Neurabin II localizes to neuronal dentritic spines, which are the specialised protrusions from dendritic shafts that receive most of the excitatory input in the CNS. Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells. Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis. Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1.

Supplier: Bioss

Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta Signalling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development. Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation. Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells. Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain. Neurabin II localizes to neuronal dentritic spines, which are the specialised protrusions from dendritic shafts that receive most of the excitatory input in the CNS. Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells. Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis. Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1.

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta Signalling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.

Supplier: ANTIBODIES.COM

Rabbit polyclonal antibody to PP1-alpha for WB, IHC and ELISA with samples derived from Human, Mouse and Rat.

Supplier: ANTIBODIES.COM

Rabbit polyclonal antibody to PP1-alpha (phospho Thr320) for IHC and ELISA with samples derived from Human, Mouse and Rat.

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).

Supplier: Bioss

Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).