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Rabbit Anti-KIF20B/FITC Conjugated antibody
background:
The Kinesins constitute a large family of microtubule-dependent motor proteins which are responsible for the distribution of numerous organelles, vesicles and macromolecular complexes throughout the cell. Individual Kinesin members play crucial roles in cell division, intracellular transport and membrane trafficking events, including endocytosis and transcytosis. MPP1 (M-phase phosphoprotein 1), also known as KIF20B (kinesin family member 20B), MPHOSPH1 or KRMP1, is a 1,820 amino acid protein that localizes to both the nucleus and the cytoplasm and contains one kinesin-motor domain. Expressed in kidney, brain, testis and ovary, MPP1 functions as a plus-end directed motor enzyme that interacts with Pin1 and is required for the completion of cytokinesis. MPP1, which exists as multiple alternatively spliced isoforms termed 1-5, is subject to post-translational phosphorylation, probably by ATM or ATR.
Function:
Plus-end-directed motor enzyme that is required for completion of cytokinesis.
Subcellular Location:
Cytoplasm. Nucleus. Cytoplasm > cytoskeleton > spindle. Localizes mainly in the nucleus during interphase although it is also detected in the cytoplasm without clear association with microtubules. A 2-3 fold expression increase is seen as cells progress from G1 to G2/M phase. During prophase and metaphase it is found throughout the cytoplasm and at anaphase accumulates at the midplan of the cell and forms a distinct band extending across the spindle midzone. At anaphase it is concentrated in the mid-body.
Tissue Specificity:
Brain, ovary, kidney and testis.
Post-translational modifications:
Phosphorylated upon DNA damage, probably by ATM or ATR.
Similarity:
Belongs to the kinesin-like protein family.
Contains 1 kinesin-motor domain.
Database links:
Entrez Gene: 9585 Human
Omim: 605498 Human
SwissProt: Q96Q89 Human
Unigene: 48 Human
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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