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The phosphatidylethanolamine (PE)-binding proteins, including PEBP4, are an evolutionarily conserved family of proteins with pivotal biologic functions, such as lipid binding and inhibition of serine proteases (Wang et al., 2004 [PubMed 15302887]).[supplied by OMIM, Dec 2008].. Additionally we are shipping PEBP4 Antibodies (35) and PEBP4 Kits (4) and many more products for this protein.
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PEBP4 is a secreted protein and has multiple functions, including a role in Akt (show AKT1 Proteins) phosphorylation.
We describe the cloning and functional characterization of the mouse homolog of hPEBP4 (mPEBP4). We demonstrate that mPEBP4 promotes cellular migration and invasion by inhibiting ERK1/2 and JNK (show MAPK8 Proteins) activation and up-regulating the expression of COX-2.
PEBP4 was associated with the development and invasion of gastric cancer cells through activation of the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway
knockdown of PEBP4 inhibited hypoxia-induced epithelial-to-mesenchymal transition in prostate cancer cells.
this study suggested that PEBP4 might promote the progression of pancreatic ductal adenocarcinoma
Increased expression of phosphatidylethanolamine-binding protein 4 strongly associates with gliomas grade.
Increased miR (show MLXIP Proteins)-15b expression in lung adenocarcinoma patients treated with cisplatin-based chemotherapy was correlated with low expression of PEBP4, decreased sensitivity to cisplatin and poor prognosis.
concluded that hPEBP4, specifically expressed in rectal cancer cells, is associated with radioresistance of rectal cancer
overexpression of PEBP4, which we show to be a target of miR (show MLXIP Proteins)-34a, reduces the sensitivity of lung cancer cells to cisplatin
in human breast cancer hPEBP4 is a novel and clinically relevant metastasis accelerator gene
Human PEBP4 expression correlates negatively with estrogen and progesterone receptors in endometrial carcinoma.
The phosphatidylethanolamine (PE)-binding proteins, including PEBP4, are an evolutionarily conserved family of proteins with pivotal biologic functions, such as lipid binding and inhibition of serine proteases (Wang et al., 2004
phosphatidylethanolamine-binding protein 4
, cousin-of-RKIP 1 protein
, protein cousin-of-RKIP 1