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- Product number
- ABIN151319 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-PH Domain and Leucine Rich Repeat Protein Phosphatase 1 (PHLPP1) (AA 1050-1100) antibody
- Antibody type
- Polyclonal
- Description
- Immunogen affinity purified
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- AA 1050-1100
- Vial size
- 100 μL
- Storage
- Store at 4°C. Do not freeze.
- Handling
- Do not freeze.
Submitted references Mislocalization of the E3 ligase, β-transducin repeat-containing protein 1 (β-TrCP1), in glioblastoma uncouples negative feedback between the pleckstrin homology domain leucine-rich repeat protein phosphatase 1 (PHLPP1) and Akt.
mTOR-dependent regulation of PHLPP expression controls the rapamycin sensitivity in cancer cells.
Purinergic receptor-mediated rapid depletion of nuclear phosphorylated Akt depends on pleckstrin homology domain leucine-rich repeat phosphatase, calcineurin, protein phosphatase 2A, and PTEN phosphatases.
IGF-I activation of the AKT pathway is impaired in visceral but not subcutaneous preadipocytes from obese subjects.
Common polymorphism in the phosphatase PHLPP2 results in reduced regulation of Akt and protein kinase C.
The phosphatase PHLPP controls the cellular levels of protein kinase C.
PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms.
Warfel NA, Niederst M, Stevens MW, Brennan PM, Frame MC, Newton AC
The Journal of biological chemistry 2011 Jun 3;286(22):19777-88
The Journal of biological chemistry 2011 Jun 3;286(22):19777-88
mTOR-dependent regulation of PHLPP expression controls the rapamycin sensitivity in cancer cells.
Liu J, Stevens PD, Gao T
The Journal of biological chemistry 2011 Feb 25;286(8):6510-20
The Journal of biological chemistry 2011 Feb 25;286(8):6510-20
Purinergic receptor-mediated rapid depletion of nuclear phosphorylated Akt depends on pleckstrin homology domain leucine-rich repeat phosphatase, calcineurin, protein phosphatase 2A, and PTEN phosphatases.
Mistafa O, Ghalali A, Kadekar S, Högberg J, Stenius U
The Journal of biological chemistry 2010 Sep 3;285(36):27900-10
The Journal of biological chemistry 2010 Sep 3;285(36):27900-10
IGF-I activation of the AKT pathway is impaired in visceral but not subcutaneous preadipocytes from obese subjects.
Cleveland-Donovan K, Maile LA, Tsiaras WG, Tchkonia T, Kirkland JL, Boney CM
Endocrinology 2010 Aug;151(8):3752-63
Endocrinology 2010 Aug;151(8):3752-63
Common polymorphism in the phosphatase PHLPP2 results in reduced regulation of Akt and protein kinase C.
Brognard J, Niederst M, Reyes G, Warfel N, Newton AC
The Journal of biological chemistry 2009 May 29;284(22):15215-23
The Journal of biological chemistry 2009 May 29;284(22):15215-23
The phosphatase PHLPP controls the cellular levels of protein kinase C.
Gao T, Brognard J, Newton AC
The Journal of biological chemistry 2008 Mar 7;283(10):6300-11
The Journal of biological chemistry 2008 Mar 7;283(10):6300-11
PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms.
Brognard J, Sierecki E, Gao T, Newton AC
Molecular cell 2007 Mar 23;25(6):917-31
Molecular cell 2007 Mar 23;25(6):917-31
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