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Monoclonal Antibody Western Blotting Phosphoric Monoester Hydrolase Activity

$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 Na,K-ATPase α1 (D4Y7E) Rabbit mAb #23565.
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2,3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T- and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils, and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Prostatic Acid Phosphatase (ACPP or PAP) is a member of the histidine acid phosphatase family. It is a non-specific phosphatase that is capable of dephosphorylating tyrosine residues as well as phospholipids under mildly acidic conditions. ACPP has ecto-5'-nucleotidase activity in pain-sensing neurons where it converts AMP to adenosine, suppressing the pain response (1,2). ACPP occurs as two isoforms that are both heavily glycosylated. The secreted phosphatase (sPAP) is found predominantly in the prostate and seminal plasma, while the cellular isoform (cPAP) is broadly expressed at very low levels and is associated with the plasma and lysosomal membranes (3-5). Cellular PAP has been shown to dephosphorylate ErbB2 at various tyrosine residues effectively terminating signaling (6). Furthermore, the physical interaction between cPAP and ErbB2 appears to regulate androgen sensitivity in prostate cancer cells. Loss of cPAP in androgen-sensitive prostate cancer cells results in the development of a castration-resistant phenotype suggesting that ACPP plays a significant role in prostate cancer cell growth (7). ACPP is expressed in metastatic cells arising from prostate cancer - especially in prostate-derived bone metastasis - suggesting that it may be a relevant diagnostic indicator of prostate cancer re-emergence in bone (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: PTPN22 (Lyp/PEP) is a cytoplasmic phosphatase expressed by hematopoietic cells (1,2). PTPN22 associates with the tyrosine kinase Csk to inhibit T cell receptor signaling through inactivation of Src kinases (3,4). Csk phosphorylates Src kinases on an inhibitory tyrosine, while PTPN22 dephosphorylates an activating site (4). PTPN22(-/-) mice have higher levels of activated Lck than wild-type, resulting in greater T cell expansion and increased serum antibody levels (5). Research studies have shown that a single-nucleotide polymorphism, 1858T of the PTPN22 gene which encodes the amino acid substitution R620W, confers increased risk for multiple autoimmune diseases including type I diabetes, rheumatoid arthritis, systemic lupus erythematosus, and Graves disease (6-9). Interestingly, although the R620W substitution disrupts the interaction between Csk and PTPN22, it is actually a gain-of-function mutation resulting in increased phosphatase activity (6,10,11). Recent evidence suggests that the autoimmune phenotype associated with the R620W variant is the result of increased calpain-mediated degradation and decreased protein levels of PTPN22 (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein regulates the cellular response to multiple stresses, including DNA damage and oxidative stress. Activation of p53 can lead to cell cycle arrest and DNA repair, or apoptosis (1). Activated p53 transcription factor regulates the expression of multiple genes that regulate cell metabolism and the cell cycle. One p53-inducible gene is C12orf5, which encodes for a fructose-2,6-bisphosphatase known as TIGAR. TP53-inducible glycolysis and apoptosis regulator (TIGAR) protects cells from oxidative stress as it negatively regulates glycolysis and reduces the production of reactive oxygen species (ROS) in cells (2,3). Research studies demonstrate that knockdown of TIGAR expression induces autophagy and apoptosis (4,5), and its expression protects cells from ROS-related cell death (6,7). Additional studies show that TIGAR promotes cell cycle arrest and supports dephosphorylation of the retinoblastoma (Rb) protein (8).