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Polyclonal Antibody Phosphoinositide Binding

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). PLD1 is phosphorylated at Ser2, Ser561, and Thr147 by PKC (2,3). Phosphorylation at Thr147 and Ser561 regulates PLD1 activity (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). PLD1 is phosphorylated at Ser2, Ser561, and Thr147 by PKC (2,3). Phosphorylation at Thr147 and Ser561 regulates PLD1 activity (3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). PLD1 is phosphorylated at Ser2, Ser561, and Thr147 by PKC (2,3). Phosphorylation at Thr147 and Ser561 regulates PLD1 activity (3).

$303
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster

Application Methods: Western Blotting

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The actin-binding protein girdin (CCDC88A, GIV) is a non-receptor guanine nucleotide exchange factor (GEF) and part of a scaffold that mediates key signaling pathways during cell migration (1). Girdin protein structure includes an amino-terminal Hook domain for microtubule interaction, a coiled-coil dimerization domain, a Gα binding domain, a PI(4)P-binding domain, and a carboxy-terminal receptor-binding domain within a GEF motif (1-5). Akt kinase phosphorylates girdin at Ser1416, which promotes PI(4)P binding, localization of girdin to the membrane leading edge, and regulation of actin organization and cell motility (3). After growth factor receptor activation, girdin binds both G-protein and receptor to form an activation complex at the receptor cytoplasmic tail. The activation complex enhances receptor autophosphorylation and promotes downstream signaling that results in actin organization and cell migration (5). An activated growth factor phosphorylates girdin at its carboxy-terminal Tyr1764 and Tyr1798 residues to form an SH2 docking site for PI3K binding (6). The girdin GEF motif interacts with Gα and leads to release of Gβγ, resulting in further PI3K activation and the completion of signal transduction from receptor to cytoskeleton (7). The cytoskeletal reorganization and cell migration properties of girdin are important in regulating several biological processes, including wound healing, angiogenesis, and cancer progression (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TKS5 (SH3PXD2A, FISH) is a scaffold protein expressed on invadosomes of both normal and transformed cell lines. Research studies suggest that TKS5 is functionally required for both the formation and invasive behavior of invadosomes (1, 2). TKS5 has an N-terminal PX domain that mediates invadosome initiation and localization of MMP-rich vesicles to the invadosome (3). TKS5 also has five SH3 domains, which recruit ADAM family proteinases to the invadosome to degrade extracellular matrix. These SH3 domains interact with adaptor proteins to facilitate F-actin polymerization during invadosome formation (4-6). Src tyrosine kinase has been shown to phosphorylate TKS5 at Tyr557 and Tyr619, which was shown to be necessary and sufficient for TKS5-mediated invadopia formation and invasion (7). Elevated TKS5 expression is positively associated with invasive behavior of cancer cells, suggesting TKS5 may have prognostic potential in cancer (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The phagocytic NADPH oxidase is a multiprotein enzyme that catalyzes the reduction of oxygen to superoxide in response to pathogenic invasion. The NADPH oxidase consists of 6 subunits, including the membrane-bound p91 phox and p22 phox heterodimers (also known as cytochrome b558), the cytosolic complex of p40phox, p47phox and p67phox, and the small GTPase Rac2. Activation of NADPH oxidase is initiated by cytosolic complex phosphorylation, which induces a conformational change that leads to the translocation of the cytosolic complex to the membrane and formation of an active enzyme with cytochrome b558 (1). Defects in p47phox, often resulting from recombination between p47phox and a nearby homologous pseudogene, cause chronic granulomatous disease (2-4). Elevated oxidative stress due to increased myocardial NADPH oxidase activity may be a contributing factor in heart failure (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fes/Fps and Fer are the only two members of a unique family of cytoplasmic protein tyrosine kinases (1,2). Fes and Fer contain a central Src homology-2 (SH2) domain and a carboxy-terminal tyrosine kinase catalytic domain. They are structurally distinguished from other members of cytoplasmic protein tyrosine kinase subfamilies by the presence of amino-terminal Fer/CIP4 homology and coiled-coil domains (3). Fes/Fps was originally identified as an oncogene from avian (Fps) and feline (Fes) retroviruses. Human c-Fes has been implicated in myeloid, vascular endothelial and neuronal cell differentiation. Mutations may activate the Fps kinase and thereby contribute to cancer (4). However, recent data strongly suggests that the c-Fes protein-tyrosine kinase is a tumor suppressor rather than a dominant oncogene in colorectal cancer (5).

$122
20 µl
$303
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-PLCgamma2 (Tyr1217) Antibody #3871.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: 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).

$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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: OCRL1 is an inositol 5-phosphatase that selectively dephosphorylates the 5 position of the inositol ring. Its substrates include phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate, and inositol 1,3,4,5-tetrakisphosphate (1). Research studies indicate that mutations in OCRL1 are linked to Oculocerebrorenal syndrome or Lowe syndrome, an X-linked disorder distinguished by mental retardation and congenital cataracts, as well as Dent's disease (2,3). OCRL1 interacts with several endocytic proteins, including clathrin, AP-2, and RabGTPases (4-7). OCRL1 is localized to the Golgi complex, endosomes, and late stage clathrin-coated pits (6,8). OCRL1 controls early endosome function (8), regulating membrane traffic from endosomes to the Golgi. It is also involved in cytokinesis (9) and cilia assembly (10).

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).