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Monoclonal Antibody Western Blotting Phospholipase Activity

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (1,2) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (3). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.

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

Application Methods: Western Blotting

Background: Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (1,2) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (3). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ABHD6 (α/β-Hydrolase domain-containing 6) is a monoacylglycerol lipase, ubiquitously expressed with the highest expression in brown adipose tissue, small intestine, and brain (1). A high-fat diet upregulates ABHD6 mRNA expression in small intestine and liver, and ABHD6 knockdown protects against high-fat diet-induced obesity, hepatic steatosis, and systemic insulin resistance (2). In addition, it has been shown that ABHD6 is a negative modulator of glucose-stimulated insulin secretion (3). In the central nervous system, ABHD6 is expressed postsynptically and degrades the endocannabinoid 2-arachidonoylglycerol (2-AG), an endogenous activator of cannabinoid receptors (4,5). Inhibitors of α/β-hydrolase domain 6 (ABHD6) have been actively pursued as a promising approach to treat inflammation, metabolic disorders, and epilepsy (2,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (1,2) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (3). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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). The PLD2 isoform is highly expressed in many cancers, such as colorectal and breast cancers (2,3). PLD2 also acts as a guanine nucleotide exchange factor for the small GTPase Rac2 independent of its phospholipase activity (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), 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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$348
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 PLCc1 (D9H10) XP® Rabbit mAb #5690.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, 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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), 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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

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

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, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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
Mouse, Rat

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, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The annexin superfamily consists of 13 calcium or calcium and phospholipid binding proteins with high biological and structural homology (1). Annexin-1 (ANXA1) is the first characterized member of the annexin family of proteins and is able to bind to cellular membranes in a calcium-dependent manner, promoting membrane fusion and endocytosis (2-4). Annexin A1 has anti-inflammatory properties and inhibits phospholipase A2 activity (5,6). Annexin A1 can accumulate on internalized vesicles after EGF-stimulated endocytosis and may be required for a late stage in inward vesiculation (7). Phosphorylation by PKC, EGFR, and Chak1 results in inhibition of annexin A1 function (8-10). Annexin A1 has also been identified as one of the 'eat-me' signals on apoptotic cells that are to be recognized and ingested by phagocytes (11). Annexin A1, as an endogenous anti-inflammatory mediator, has roles in many diverse cellular functions, such as membrane aggregation, inflammation, phagocytosis, proliferation, apoptosis, and tumorigenesis and cancer development (12-14).

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

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Lamin B1 (D9V6H) Rabbit mAb #13435.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (4,5). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (6-8). Lamin B1 is also cleaved by caspases during apoptosis (9). Research studies have shown that duplication of the lamin B1 gene LMNB1 is correlated with pathogenesis of the neurological disorder adult-onset leukodystrophy (10).