MLF1IP / PBIP1 Antibody

Background

This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. Myeloid leukemia factor-1 (MLF1) Interacting Protein (also known as PBIP1, MLF1IP1, KLIP1 or KSHV latent nuclear antigen interacting protein 1) is a novel polo-like kinase 1 (Plk1) substrate.  Plk1 phosphorylation of MLF1IP induces ubiquitination and degradation of MLF1IP prior to the metaphase/anaphase transition.  Several Plk1-dependent phosphorylation sites have been identified on MLF1IP by mass spectrometry.  Mutations of these sites stabilize MLF1IP and inhibit mitotic progression.  Subsequent in vitro and in vivo MLF1IP phosphorylation and stability assays have revealed that phosphorylation of Thr78 is critical for triggering Plk1-dependent MLF1IP degradation.  Expression of a non-degradable Thr78Ala mutant was sufficient to induce a mitotic block.  Timely phosphorylation of MLF1IP on Thr78 by Plk1 is critical for eliminating the MLF1IP-imposed mitotic block prior to anaphase onset.  MLF1IP is speculated to be a novel tumor suppressor, whose function is required for proper sister-chromatid separation.  Loss of MLF1IP function may result in improper segregation of chromosomes and genomic instability, thus promoting tumorigenesis.