Eg5 polyclonal, anti-human

Eg5 polyclonal, anti-human

€428.00
In stock
SKU
BS90447
Catalog Number: BS90447
Size: 100 µl
Other Size: 50 µl
Isotype: rabbit IgG
Applications: WB, IP
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Background:
Eukaryotes contain a superfamily of microtubule-based motor proteins comprising kinesin and a number of related proteins that are thought to participate in various forms of intracellular motility, including cell division and organelle transport. KIF11(also known as kinesin family member 11, Eg5 or TRIP5) is a slow, plus-end-directed microtubule-based motor of the BimC kinesin family that is essential for bipolar spindle formation during eukaryotic cell division. When the expression of KIF11 is blocked, centrosome migration halts and cells are arrested in mitosis with monoastral microtubule arrays. KIF11 is phosphorylated on serine during S phase and on both serine and Thr 927 during mitosis, which regulates the association of Eg5 with the spindle apparatus (probably during early prophase). KIF11 is also known to be a member of the thyroid receptor interacting protein (Trip) family, and interacts with the thyroid hormone receptor only in the presence of thyroid hormone.

Alternative Name:
TR-interacting protein 5, TRIP-5, KIF11, EG5, KNSL1, TRIP5, EG5, HKSP, KIF11, KIF11, Kinesin family member 11, Kinesin like protein 1, Kinesin-like protein 1, Kinesin-like protein KIF11, Kinesin-like spindle protein HKSP, Kinesin-related motor protein Eg5, KNSL1, MCLMR, Thyroid receptor-interacting protein 5, TR-interacting protein 5, TRIP-5, TRIP5,

Application Dilution:
WB:1:500-1:2,000
IP:1:10-1:50

Specificity: Eg5 polyclonal antibody detects endogenous levels of Eg5 protein.

Immunogen:
Recombinant protein

MW: 119 kDa

Swiss-Prot: P52732(Human)

Purification & Purity:
ProA affinity purified

Format:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Storage:
Store at +4°C after thawing. Aliquot store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

For research use only, not for use in diagnostic procedure.
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