Eg5 (also known as kinesin-5 and KIF11) is a homo-tetramer which cross-links anti-parallel microtubules in the mitotic spindle to maintain spindle bipolarity. Eg5, a member of the Kinesin-5 subclass of kinesins, is a plus-end-directed tetrameric kinesin-family protein that influences the assembly and organization of the mitotic spindle, a self-assembled and dynamic microtubule-based structure that orchestrates chromosome segregation in dividing cells. Eg5 action is essential: when it is depleted from the cytoplasm of meiotically-mature Xenopus laevis eggs, abnormal monopolar spindles form, preventing successful division. Eg5 is expressed in all cells during mitosis and in post-mitotic neurons during development. In developing neurons pharmacological inhibition and siRNA knockdown of Eg5 results in longer axons, more branches, fewer bouts of axon retraction and the inability of growth cones to turn on contact with repulsive substrates. In migratory neurons, inhibition of Eg5 causes neurons to migrate in a random pattern and form shorter leading processes. In adult neurons, Eg5 has a similar effect on inhibiting the rate of short microtubule transport so pharmacological inhibition of adult Eg5 (i.e Monastrol) may be a potential therapeutic tool for the augmentation of adult axon regeneration.
應(yīng)用類(lèi)型
ELISA,Immunohistochemistry,Western Blot,
免疫原
Eg5 was prepared from whole rabbit serum produced by repeated immunizations with a truncated Eg5 construct expressed in E. coli corresponding to human Eg5 protein.
來(lái)源宿主
Rabbit
反應(yīng)性
H. sapiens (Human)
保存建議
Store vial at -20° C or below prior to opening. This vial contains a relatively low volume of reagent (25 μL). To minimize loss of volume dilute 1:10 by adding 225 μL of the buffer stated above directly to the vial. Recap, mix thoroughly and briefly centrifuge to collect the volume at the bottom of the vial. Use this intermediate dilution when calculating final dilutions as recommended below. Store the vial at -20°C or below after dilution. Avoid cycles of freezing and thawing.