Western blot using GeneTexs affinity purified anti-MLF1IP / PBIP1 antibody shows detection of endogenous MLF1IP protein (a tier of four modified protein bands indicated by the arrowheads) in lysates of Hela cells (- lane). Cells treated with MLF1IP / PBIP1 shRNA (+ lane) show no staining. The identities of the higher and lower molecular weight bands are unknown. Primary antibody was used at 1:1,000.
Western blot using GeneTexs affinity purified anti-MLF1IP / PBIP1 antibody shows detection of endogenous MLF1IP protein (a tier of four modified protein bands indicated by the arrowheads) in lysates of Hela cells (- lane). Cells treated with MLF1IP / PBIP1 shRNA (+ lane) show no staining. The identities of the higher and lower molecular weight bands are unknown. Primary antibody was used at 1:1,000.
Mlf1 Interacting Protein antibody - KO/KD Validated
GTX48709
ApplicationsWestern Blot, ELISA, ImmunoHistoChemistry
Product group Antibodies
ReactivityHuman
TargetCENPU
Overview
- SupplierGeneTex
- Product NameMlf1 Interacting Protein antibody - KO/KD Validated
- Delivery Days Customer9
- ApplicationsWestern Blot, ELISA, ImmunoHistoChemistry
- CertificationResearch Use Only
- ClonalityPolyclonal
- Concentration1.1 mg/ml
- ConjugateUnconjugated
- Gene ID79682
- Target nameCENPU
- Target descriptioncentromere protein U
- Target synonymsCENP50; CENPU50; centromere protein of 50 kDa; centromere protein U; interphase centromere complex protein 24; KLIP1; KSHV latent nuclear antigen interacting protein 1; MLF1 interacting protein; MLF1IP; PBIP1; polo-box-interacting protein 1
- HostRabbit
- IsotypeIgG
- Scientific DescriptionMyeloid 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.
- ReactivityHuman
- Storage Instruction2°C to 8°C,-20°C or -80°C
- UNSPSC12352203