Anti-EC 3.1.3.16, Anti-PH domain leucine-rich repeat protein phosphatase, Anti-PH domain leucine-rich repeat-containing protein phosphatase, Pleckstrin homology domain-containing family E protein 1, Suprachiasmatic nucleus circadian oscillatory protein
Pleckstrin homology domain leucine-rich repeat protein phosphatase 1 (PHLPP1) is encoded by the gene mapped to human chromosome 18q21.33. The encoded protein belongs to the PHLPP family and is characterized with a PH domain followed by region of leucine-rich repeats (LRR), a PP2C phosphatase domain and a C-terminal PDZ ligand. PHLPP1 has two alternatively spliced transcript variants encoding different isoforms namely PHLPP1α with 1205 amino acids and PHLPP1β with 1717 amino acids. PHLPP1 is expressed in cytosolic, nuclear and membrane fraction of cells.
免疫原
PHLPP1 (NP_919431, 24-58) This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human PHLPP1.
生物化学的/生理学的作用
PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1) catalyzes the dephosphorylation of serine/threonine-protein kinases AKT2 and AKT3. The encoded protein might act as a tumor suppressor. Loss of gene expression is associated with the development of colon cancers. Overexpression of the gene has been observed in skeletal muscles of Type 2 diabetic patients. Thus, inhibition of PHLPP1 might enhance Akt2 activity and can be considered as a potent therapeutic target for the type II diabetes. Inhibition PHLPP1 through DNA methylation leads to the development of melanoma.
物理的形状
精製済みポリクローナル抗体のPBS溶液(0.09%(W/V)アジ化ナトリウム含有)
免責事項
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Akt is constitutively activated in up to 70% of human melanomas and has an important role in the pathogenesis of the disease. However, little is known about protein phosphatases that dephosphorylate and thereby inactivate it in melanoma cells. Here we