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Product listing: PI3 Kinase Class III Antibody, UniProt ID Q8NEB9 #3811 to PLEKHM1 Antibody, UniProt ID Q9Y4G2 #66012

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Three distinct types of phosphoinositide 3-kinases (PI3K) have been characterized. Unlike other PI3Ks, PI3K class III catalyzes the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate (PIP3) (1). PI3K class III is the mammalian homolog of Vps34, first identified in yeast. PI3K class III interacts with the regular subunit p150, the mammalian homolog of Vps15, which regulates cellular membrane association through myristoylation (2,3). PIP3 recruits several proteins with FYVE or PX domains to membranes regulating vesicular transport and protein sorting (4). Moreover, PI3K class III has been shown to regulate autophagy, trimeric G-protein signaling, and the mTOR nutrient-sensing pathway (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).

$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, Mouse, Rat

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

Background: Inositol phospholipids have an important role in intracellular signaling in response to hormones, growth factors and neurotransmitters. Phosphatidylinositol 4-kinase phosphorylates phosphatidylinositol (PI) to phosphatidylinositol-4-phosphate (PIP). In a second step, PIP is further phosphorylated to phosphatidylinositol-4,5-bisphosphate (PIP2), and PIP2 is subsequently hydrolyzed by phospholipase C, producing the two intracellular second messengers, inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). PI4K230, PI4K92 and PI4K55 are three PI4 kinase isoforms that have been characterized and classified according to their molecular weights of 230, 92 and 55 kD. Previously, PI4 kinases were classified into type II and III enzymes (2). All isoforms are located on distinct membranes and cellular compartments suggesting various tasks. PI4K230 is located at the endoplasmatic reticulum and outer membranes of mitochondria, PI4K92 at the Golgi apparatus and endoplasmatic reticulum, and PI4K55 at the plasma membrane and endosomes (3-5). PI4K230 is predominantly expressed in brain and moderately sensitive to wortmannin as well as specifically and irreversibly inhibited by cyclitol derivatives (3, 6).

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

Application Methods: Western Blotting

Background: The protein inhibitor of activated Stat (PIAS) proteins, which include PIAS1, PIAS3, PIASx, and PIASy, were originally characterized based on their interaction with the Stat family of transcription factors (1,2). PIAS1, PIAS3, and PIASx interact with and repress Stat1, Stat3, and Stat4, respectively (1-3). Deletion of PIAS1 leads to inhibition of interferon-inducible genes and increased protection against infection (4). The PIAS family contains a conserved RING domain that has been linked to a function as a small ubiquitin-related modifier (SUMO) ligase, coupling the SUMO conjugating enzyme Ubc9 with its substrate proteins (5,6). Numerous studies have now shown that PIAS family members can regulate the activity of transcription factors through distinct mechanisms, including NF-κB (7,8), c-Jun, p53 (5,9), Oct-4 (10), and Smads (11,12). The activity of PIAS1 is regulated by both phosphorylation and arginine methylation. Inflammatory stimuli can induce IKK-mediated phosphorylation of PIAS1 at Ser90, which is required for its activity (13). In addition, PRMT1 induces arginine methylation of PIAS1 at Arg303 following interferon treatment and is associated with its repressive activity on Stat1 (14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The serine/threonine PI3 kinase regulatory subunit 4 (PIK3R4, Vps15) is the mammalian homologue of the yeast vacuolar protein sorting 15 (1). PIK3R4 regulates the kinase activity of PI3K class III and anchors the kinase to cellular membranes through myristoylation (2,3). Recruitment of PI3K class III to the site of early endosome fusion and docking is directly mediated by PIK3R4 binding to the small GTPase Rab5 through its HEAT and WD-40 domains (4,5). The PIK3R4/PI3K class III plays a role in late endosome function through PIK3R4 binding to the Rab7 GTPase (6). In addition to its role in trafficking, the PIK3R4/PI3K class III complex interacts with beclin-1 to play a role during several stages of autophagy. Autophagosome formation is stimulated when Atg14 complexes with PIK3R4, PI3K class III, and beclin-1. The UVRAG protein competes with Atg14 for beclin-1 binding, forming a mutually exclusive complex with PIK3R4, PI3K class III, and beclin-1 that regulates autophagosome maturation. Autophagosome maturation is impaired in the presence of the beclin-1-binding protein Rubicon (7,8). Co-expression of PIK3R4 is required for PI3K class III activation and regulation by both beclin-1/UVRAG and by nutrients (9). Overexpression of PIK3R4 protein has been associated with decreased survival in patients with ovarian tumors, while mutations of the corresponding PIK3R4 gene are associated with metastatic melanoma, suggesting that PIK3R4 functions in cancer (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Pim proteins (Pim-1, Pim-2 and Pim-3) are oncogene-encoded serine/threonine kinases (1). Pim-1, a serine/threonine kinase highly expressed in hematopoietic cells, plays a critical role in the transduction of mitogenic signals and is rapidly induced by a variety of growth factors and cytokines (1-4). Pim-1 cooperates with c-Myc in lymphoid cell transformation and protects cells from growth factor withdrawal and genotoxic stress-induced apoptosis (5,6). Pim-1 also enhances the transcriptional activity of c-Myb through direct phosphorylation within the c-Myb DNA binding domain as well as phosphorylation of the transcriptional coactivator p100 (7,8). Hypermutations of the Pim-1 gene are found in B-cell diffuse large cell lymphomas (9). Phosphorylation of Pim-1 at Tyr218 by Etk occurs following IL-6 stimulation and correlates with an increase in Pim-1 activity (10). Various Pim substrates have been identified; Bad is phosphorylated by both Pim-1 and Pim-2 at Ser112 and this phosphorylation reverses Bad-induced cell apoptosis (11,12).

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

Application Methods: Western Blotting

Background: Pin1, a member of the parvulin family of peptidyl-prolyl isomerases (PPIase), has been implicated in the G2/M transition of the mammalian cell cycle (1-6). Pin1 is a small (18 kDa) protein with two distinct functional domains: an amino-terminal WW domain and a carboxy-terminal PPlase domain. Pin1 interacts with several mitotic phosphoproteins, including Plk1, cdc25C and cdc27, and is thought to act as a phosphorylation-dependent PPlase for these target molecules (7-9).

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

Application Methods: Flow Cytometry, Western Blotting

Background: Phosphatidylinositol-5-phosphate 4-kinases (PIP4K) synthesize phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), a key precursor in phosphoinositide signaling that directly modulates the activity of signaling proteins and cellular processes. There are two subfamilies of PIP kinases, type I and II, that generate PtdIns(4,5)P2 from distinct substrate pools. PIP4 type I kinases use PtdIns5P as a substrate, whereas PIP5 type II kinases use PtdIns4P (1,2). In mammalian cells, three isoforms of each PIP4K and PIP5K subfamily, encoded by distinct genes, have been characterized (3-7). All PIP kinases are stimulated by phosphatidic acid, extensively regulated by ARF and Rho GTPases, and inhibited by protein kinase A and PI-stimulated autophosphorylation (8).

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

Application Methods: Western Blotting

Background: Phosphatidylinositol-5-phosphate 4-kinases (PIP4K) synthesize phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), a key precursor in phosphoinositide signaling that directly modulates the activity of signaling proteins and cellular processes. There are two subfamilies of PIP kinases, type I and II, that generate PtdIns(4,5)P2 from distinct substrate pools. PIP4 type I kinases use PtdIns5P as a substrate, whereas PIP5 type II kinases use PtdIns4P (1,2). In mammalian cells, three isoforms of each PIP4K and PIP5K subfamily, encoded by distinct genes, have been characterized (3-7). All PIP kinases are stimulated by phosphatidic acid, extensively regulated by ARF and Rho GTPases, and inhibited by protein kinase A and PI-stimulated autophosphorylation (8).

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

Application Methods: Western Blotting

Background: Phosphatidylinositol-5-phosphate 4-kinases (PIP4K) synthesize phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), a key precursor in phosphoinositide signaling that directly modulates the activity of signaling proteins and cellular processes. There are two subfamilies of PIP kinases, type I and II, that generate PtdIns(4,5)P2 from distinct substrate pools. PIP4 type I kinases use PtdIns5P as a substrate, whereas PIP5 type II kinases use PtdIns4P (1,2). In mammalian cells, three isoforms of each PIP4K and PIP5K subfamily, encoded by distinct genes, have been characterized (3-7). All PIP kinases are stimulated by phosphatidic acid, extensively regulated by ARF and Rho GTPases, and inhibited by protein kinase A and PI-stimulated autophosphorylation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Pitrilysin metalloproteinase 1 (PITRM1 or PreP) is a mitochondria-enriched presequence peptidase that processes the mitochondrial targeting sequence (MTS) of proteins imported across the inner mitochondrial membrane (1). Mitochondria normally function to regulate many cellular processes such as energy production and apoptosis, and its dysfunction may contribute indirectly or directly to human neurodegenerative diseases like Alzheimer’s and Parkinson’s disease (2, 3; AD and PD, respectively). Interestingly, Aβ, the pathological hallmark of AD, accumulates in mitochondria and inhibits Cym1, the PITRM1 yeast ortholog, leading to impaired MTS processing and accumulation of unprocessed mitochondrial proteins, suggesting an indirect role of Aβ and mitochondrial dysfunction via PITRM1 (4). In addition to biochemical association of PITRM1 with Aβ-dependent mitochondrial dysfunction, human genetics suggest a more direct link as PITRM1 genetic variants have been associated with AD (5, 6). The specific mechanism is currently poorly understood, but may involve impairment of PITRM1-dependent degradation of Aβ, directly resulting in pathological accumulation of Aβ in mitochondria (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Praja-2 (PJA2/RNF131) is a RING-H2-type E3 ubiquitin ligase. PJA2 is highly expressed in neural tissue and research studies have shown that PJA2 plays a role modulating synaptic archictecture and long-term memory by promoting the ubiquitin-dependent proteolysis of NOGO-A and PKA regulatory subunits (1,2). Research studies have also shown that PJA2 sustains gliobastoma growth by driving the ubiquitin-dependent proteasomal degradation of MOB, which inactivates the LATS tumor suppressor kinase of the Hippo pathway (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).

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

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

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

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

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Phospholipase A2 (PLA2) is a superfamily of enzymes that hydrolyze glycero-3-phosphocholines and release fatty acids and lysophospholipids (1). PLA2G1B is a member of this superfamily in the 1B group that is expressed most highly in the pancreatic acinar cells (2). Evidence suggests that PLA2G1B plays a role in the absorption and storage of extra energy as fats are metabolized (1,2). Lysophospholipids generated by PLA2G1B inhibit fatty acid oxidation in the liver and reduce energy expenditure, leading to diet-induced obesity and type 2 diabetes with a high fat diet (1). Therefore, a potential intervention of obesity and diabetes could target PLA2G1B in the digestive tract (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Plasminogen is the inactive, proenzyme precursor to the serine protease plasmin that degrades fibrin within blood clots, promotes cell migration through proteolytic degradation of extracellular matrix proteins, and regulates angiogenesis and wound healing through activation of matrix metalloproteases (1-4). Inactive plasminogen is produced and secreted by liver cells and is found in the circulatory system and extracellular fluids (1). The plasminogen protein is composed of an amino terminal preactivation peptide followed by five kringle domains and a serine proteinase domain (5). The plasminogen zymogen binds to sites on the cell surface and is subsequently cleaved to release the active serine proteinase plasmin. Identified plasminogen cell surface receptors (including S100A10, enolase and PLGRKT) share carboxy-terminal lysine residues that interact with plasminogen kringle domains, resulting in cell surface localization of plasminogen (6-8). Cleavage of plasminogen can be catalyzed by a number of distinct enzymes, including tissue specific plasminogen activator (tPA), urokinase plasminogen activator (uPA), and kallikrein (1). An additional plasminogen cleavage product is the angiogenesis inhibitor angiostatin, which is derived from the first four kringle domains (9). A number of related angiogenesis inhibitors, derived from various parts of the plasminogen kringle region, have been shown to inhibit endothelial cell growth and proliferation (10). Mutations in the corresponding PLG gene have been linked to plasminogen deficiencies, characterized by decreased plasmin expression and ligneous conjunctivitis in some individuals (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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).

$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).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Plectin is a large, widely expressed protein that crosslinks the intermediate filament and actin cytoskeleton, mechanically stabilizing cells and tissues. Plectin also plays a role in the regulation of actin dynamics and acts as a scaffold for signaling molecules (1). Plectin is important in the stabilization of hemidesmosomes, crosslinking them to the intermediate filament network. Research studies have shown that mutations in plectin and other genes coding for hemidesmosomal proteins can cause epidermolysis bullosa, a condition manifested by fragile skin and frequent blistering (1,2). Plectin modulates signals to PKC through binding and sequestration of RACK1, the receptor for activated C kinase 1 (3,4). Plectin is also involved in the regulation of cytokeratin architecture and cell stress response (4), signaling through the chemokine receptor CXCR4 (5) and regulation of AMP-activated protein kinase (AMPK) activity and signaling in mouse myotubes (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Pleckstrin homology domain-containing protein family member 1 (PLEKHM1) is a multivalent endolysosomal adaptor protein that contains an N-terminal RUN domain, two internal PH domains, and a C-terminal C1 domain/zinc-finger-like motif. Research studies have shown that PLEKHM1 plays a role in bone resorption by regulating the acidification of endosomal vesicles of osteoclasts. Loss-of-function mutations in PLEKHM1 promote osteoclast failure and impair bone resorption, which leads to osteopetrosis (1-3). Recent studies have shown that PLEKHM1 serves as a nexus for different trafficking pathways of the endolysosomal network by serving as the platform for the recruitment of Rab7, HOPS complex, and LC3/GABARAP family members. Indeed, loss of PLEKHM1 impairs the lysosomal degradation of cell-surface receptors and autophagic clearance of protein aggregates (4,5).