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anti-Human PHLPP2 Antibodies:
anti-Mouse (Murine) PHLPP2 Antibodies:
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Human Polyclonal PHLPP2 Primary Antibody for EIA, WB - ABIN1449986
Brognard, Newton: PHLiPPing the switch on Akt and protein kinase C signaling. in Trends in endocrinology and metabolism: TEM 2008
Show all 4 references for ABIN1449986
Human Polyclonal PHLPP2 Primary Antibody for IP, WB - ABIN151321
Sangai, Akcakanat, Chen, Tarco, Wu, Do, Miller, Arteaga, Mills, Gonzalez-Angulo, Meric-Bernstam: Biomarkers of response to Akt inhibitor MK-2206 in breast cancer. in Clinical cancer research : an official journal of the American Association for Cancer Research 2012
Show all 2 references for ABIN151321
Human Polyclonal PHLPP2 Primary Antibody for ELISA, WB - ABIN190753
Gao, Furnari, Newton: PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. in Molecular cell 2005
Human Polyclonal PHLPP2 Primary Antibody for EIA, IHC (p) - ABIN360110
Brognard, Sierecki, Gao, Newton: PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. in Molecular cell 2007
Our studies not only first time identify PHLPP2 downregulation by lung carcinogen B[a]P/B[a]PDE (show ALDH7A1 Antibodies), but also elucidate a novel molecular mechanisms underlying lung inflammation and carcinogenesis upon B[a]P/B[a]PDE (show ALDH7A1 Antibodies) exposure.
Results showed that PHLPP1 (show PHLPP1 Antibodies) and PHLPP2 gene expression are down-regulated in esophageal squamous cell carcinoma. Their promotor is a target for mir (show MLXIP Antibodies)-224.
Data show that both serine/threonine phosphatases PHLPP (show PHLPP1 Antibodies) and dephosphorylated the physiological substrates of Akt1 (show AKT1 Antibodies) and Akt3 (show AKT3 Antibodies) with similar efficiencies.
Aberrant expression of PHLPP1 (show PHLPP1 Antibodies) and PHLPP2 correlates with poor prognosis in patients with hypopharyngeal squamous cell carcinoma
miR (show MLXIP Antibodies)-135a promotes cell proliferation in bladder cancer by targeting PHLPP2 and FOXO1 (show FOXO1 Antibodies), and is performed as an onco-
Data show that miR (show MLXIP Antibodies)-372 modulated the expression of phosphoprotein phosphatase (show PPP1R2 Antibodies) PHLPP2 by directly targeting its 3'-untranslated region (3'-UTR (show UTS2R Antibodies)) and that miR (show MLXIP Antibodies)-372 expression was inversely correlated with PHLPP2 expression in glioma samples.
Results reveal PHLPP2 as a new biomarker of cancer progression, and implicate it as major negative regulator of NF-kappaB (show NFKB1 Antibodies) signaling.
miR (show MLXIP Antibodies)-141 and its targets PHLPP1 (show PHLPP1 Antibodies) and PHLPP2 play critical roles in NSCLC tumorigenesis
biochemical characterization of phosphatase domain of PHLPP1 (show PHLPP1 Antibodies) and PHLPP2;PHLPP1 (show PHLPP1 Antibodies) and PHLPP2 have similar in vitro activities and respond comparably to the presence of metallic ions; metallic ions affect structural stability of the domain;identified 3 residues likely involved in metal coordination and 2 that may be important for structural integrity
This study reveals functional and mechanistic links between miRNA-224 and the tumor suppressors PHLPP1 (show PHLPP1 Antibodies) and PHLPP2 in the pathogenesis of colorectal cancer
PHLPP (show PHLPP1 Antibodies) is a negative regulator of RAF1 (show RAF1 Antibodies), which reduces colorectal cancer cell motility and prevents tumor progression in mice.
Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser- 657' of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor.
PH domain leucine-rich repeat-containing protein phosphatase 2
, PH domain and leucine rich repeat protein phosphatase 2
, PH domain leucine-rich repeat-containing protein phosphatase 2-like
, GTPase activating protein and VPS9 domains 1