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Polyclonal Antibody Protein Phosphatase 1 Binding

Also showing Polyclonal Antibody Western Blotting Protein Phosphatase 1 Binding

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: PAR-4 (prostate apoptosis response-4) was identified as a protein that is upregulated in prostate tumor cells undergoing apoptosis (1). Additionally, in parallel studies PAR-4 was found in the yeast two-hybrid system to bind to the Wilms' tumor suppressor protein WT1 and may modulate WT1-medated transcriptional activation (2). PAR-4 contains a leucine zipper domain and a death domain and has been implicated as an effector of apoptosis during tumorigenesis as well as in neurodegenerative disorders (3,4). PAR-4 is widely expressed in normal tissues but can be downregulated in some tumor types. The mechanism of PAR-4 mediated apoptosis regulation appears to be complex and dependent on the cellular context. Studies have indicated roles for PAR-4 in activation of the Fas-FADD-caspase-8 pathway as well as inhibition of the NF-κB pro-survival pathway (5-7). Its activity is likely to depend on the cellular context and post-translational modifications. For instance, phosphorylation of PAR-4 by Akt prevents its nuclear translocation thereby promoting cell surivival (8). In contrast, phoshorylation of rat PAR-4 at T155 by PKA appears to positively regulate its apoptotic activity (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PAR-4 (prostate apoptosis response-4) was identified as a protein that is upregulated in prostate tumor cells undergoing apoptosis (1). Additionally, in parallel studies PAR-4 was found in the yeast two-hybrid system to bind to the Wilms' tumor suppressor protein WT1 and may modulate WT1-medated transcriptional activation (2). PAR-4 contains a leucine zipper domain and a death domain and has been implicated as an effector of apoptosis during tumorigenesis as well as in neurodegenerative disorders (3,4). PAR-4 is widely expressed in normal tissues but can be downregulated in some tumor types. The mechanism of PAR-4 mediated apoptosis regulation appears to be complex and dependent on the cellular context. Studies have indicated roles for PAR-4 in activation of the Fas-FADD-caspase-8 pathway as well as inhibition of the NF-κB pro-survival pathway (5-7). Its activity is likely to depend on the cellular context and post-translational modifications. For instance, phosphorylation of PAR-4 by Akt prevents its nuclear translocation thereby promoting cell surivival (8). In contrast, phoshorylation of rat PAR-4 at T155 by PKA appears to positively regulate its apoptotic activity (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). It is a bifunctional signaling molecule that controls serine/threonine kinase and serine/threonine phosphatase activity (2). Dopamine stimulates phosphorylation of DARPP-32 through D1 receptors and activation of PKA. PKA phosphorylation of DARPP-32 at Thr34 converts it into an inhibitor of protein phosphatase 1 (1). DARPP-32 is converted into an inhibitor of PKA when phosphorylated at Thr75 by cyclin-dependent kinase 5 (CDK5) (2). Mice containing a targeted deletion of the DARPP-32 gene exhibit an altered biochemical, electrophysiological, and behavioral phenotype (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). It is a bifunctional signaling molecule that controls serine/threonine kinase and serine/threonine phosphatase activity (2). Dopamine stimulates phosphorylation of DARPP-32 through D1 receptors and activation of PKA. PKA phosphorylation of DARPP-32 at Thr34 converts it into an inhibitor of protein phosphatase 1 (1). DARPP-32 is converted into an inhibitor of PKA when phosphorylated at Thr75 by cyclin-dependent kinase 5 (CDK5) (2). Mice containing a targeted deletion of the DARPP-32 gene exhibit an altered biochemical, electrophysiological, and behavioral phenotype (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).