Immunohistochemical analysis of paraffin embedded LNCaP (left) and NIH/3T3 (right) cell pellets using PTEN (138G6) Rabbit mAb #9559.
Western blot analysis of extracts from LNCaP or NIH/3T3 cells using PTEN (138G6) Rabbit mAb #9559. NIH/3T3 cells express PTEN and LNCaP cells do not express PTEN. This assay serves to verify PTEN expression.
Each control slide contains formalin fixed, paraffin-embedded LNCaP and NIH/3T3 cell pellets. NIH/3T3 cells express PTEN while LNCaP cells do not express PTEN. Western blot analysis was performed on extracts derived from the same cells to verify PTEN expression.
To be used with antibodies: 9188, 9559.
PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).
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