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Guinea Pig Polyclonal PPAP2A Primary Antibody for IHC, WB - ABIN2775553
Tanyi, Hasegawa, Lapushin, Morris, Wolf, Berchuck, Lu, Smith, Kalli, Hartmann, McCune, Fishman, Broaddus, Cheng, Atkinson, Yamal, Bast, Felix, Newman, Mills: Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer. in Clinical cancer research : an official journal of the American Association for Cancer Research 2003
Show all 2 Pubmed References
the first of the two transmembrane regions in human SAC1 (TM1) functions in Golgi localization
Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association
this enzyme regulates interleukin-4-mediated STAT6 signaling.
This protein and phosphoprotein SET regulate androgen production by P450c17.
lipid phosphate phosphatase-1 has a role in regulating accumulation of lysophosphatidic acid in ovarian cancer
Lipopolysaccharide-induced up-regulation of cyclooxygenase-2 depends on the activity of the Mg(+2)-dependent phosphatidic acid phosphohydrolase 1 (PAP-1)
LPP1 and LPP3 are distributed in distinct lipid rafts that may provide unique microenvironments defining their non-redundant physiological functions.
These results suggest that the expression of PAP2a is directly regulated by p73.
These results suggest that LPP1a is important for the determination of plasma FTY720-P levels.
Data identify a novel role for phospholipid phosphate phosphatase type 1 activity and hepatocyte lysophosphatidic acid levels in glucagon sensitivity via a mechanism involving STAT3.
Decreased peritoneal ovarian cancer growth in mice lacking expression of lipid phosphate phosphohydrolase 1.
increasing the LPP1 activity in three lines of aggressive cancer cells decreases their abilities to produce tumors and metastases
Authors demonstrated for the first time that lipin-1 and PAP2a contribute to macrophage inflammation in response to Francisella tularensis.
there are marked differences in biochemical activity between fly Wun and mammalian lipid phosphate phosphatase (LPPs), with Wun having a narrower activity range than has been reported for the mammalian LPPs
Lipid phosphate phosphatase 1 (LPP-1) is presumed to regulate the balance between lipid phosphates and their dephosphorylated counterparts
LPP1 is a catabolic enzyme for lysophosphatidic acid in vivo.
The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.
phosphatidic acid phosphatase type 2A
, phosphatidic acid phosphatase 2a
, lipid phosphate phosphohydrolase 1
, lipid phosphate phosphohydrolase 1a
, phosphatidate phosphohydrolase type 2a
, phosphatidic acid phosphohydrolase type 2a
, type-2 phosphatidic acid phosphatase alpha
, 35 kDa PAP
, hydrogen peroxide inducible protein 53
, hydrogen peroxide-inducible protein 53
, lipid phosphate phosphatase 1