CENPU / Unconjugated / Polyclonal

Product Details

Description	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.
Conjugate	Unconjugated
Clone	Polyclonal
Target Species	Bovine, Canine, Human
Applications	ELISA, WB, IHC
Supplier	Aviva Systems Biology
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About CENPU
The centromere is a specialized chromatin domain, present throughout the cell cycle, that acts as a platform on which the transient assembly of the kinetochore occurs during mitosis. All active centromeres are characterized by the presence of long arrays of nucleosomes in which CENPA (MIM 117139) replaces histone H3 (see MIM 601128). MLF1IP, or CENPU, is an additional factor required for centromere assembly (Foltz et al., 2006 [PubMed 16622419]).[supplied by OMIM, Mar 2008]

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