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Also for CENPU (NM_024629)
|This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids surrounding Thr78 of human MLF1IP protein.|
|human, dog, bovine, chimpanzee
||ELISA: 1:5,000 - 1:25,000, WB: 1:500- 1:2,000, IHC: User Optimized
|0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2|
|This antibody 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.
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Western blot using affinity purified anti-MLF1IP antibody shows detection of MLF1IP (arrowhead) in HeLa cells transfected with ZZ-tagged MLF1IP (Lane 1). Lane 2 is lysate from non-transfected HeLa cells, and Lane 3 is lysate from HeLa cells containing a knock-out mutation for PBIP1/MLF1IP. Personal Communication, Kyung S. Lee, CCR-NCI, Bethesda, MD.