p-p130 Anticuerpo(Ser 966): sc-16300

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The human retinoblastoma gene product plays an important role in the negative regulation of cell proliferation. Functional inactivation of Rb can be mediated either through mutation or as a consequence of interaction with DNA tumor virus encoded proteins (1). pRb and the structurally related p107 form complexes with E2F (2–7), a transcription factor originally identified through its role in transcriptional activation of the adenovirus E2 promoter (5,7). Moreover, pRB and p107 share a high degree of structural homology in the adenovirus E1A binding domain (i.e., “pocket region”) that is believed to play a primary role in the function of these proteins. A protein designated p130 shows a high degree of identity with pRb and p107 and also possesses a pocket region (8). p130 undergoes cell cycle dependent phosphorylation during the mid-G1 to S phase transition and this phosphorylation is dependent upon the activity of cyclin D/cdk4 (9). In contrast to pRB and p107, p130 is phosphorylated during G0 and the early G1 phase of the cell cycle (9). p130 is specifically phosphorylated on serine and threonine residues in cells arrested in G0 by serum deprivation or density arrest (9). Most of the phospho-serine and phospho-threonine residues are clustered within a short co-linear region unique to p130, defined as the Loop (9).