Table 3. In vitro microtubule gliding rates of Kinesin-5 proteins.

Using purified kinesin protein, bulk-measurement rates of microtubule motion were recorded in motility assays. Noted are the oligomeric state of the kinesin protein, buffer, pH, and salt/osmolyte concentration.

Kinesin-5isoform	Oligomeric State	Buffer (pH)	Salt/Other (Osmolyte)	Velocity (nm/s)	Reference
X. laevis	native tetramer	80 mM PIPES (6.8)	-	12.3	(Kwok et al., 2004)
	native tetramer	80 mM PIPES (6.8)	-	24.0	(Kapitein et al., 2005)
	native tetramer	70 mM PIPES (6.8)	80 mM KCl	34.4	(Weinger et al., 2011)
	native tetramer	70 mM PIPES (6.8)	-	16.8	(Weinger et al., 2011)
	native dimer (1-513)	70 mM PIPES (6.8)	-	30.1	(Weinger et al., 2011)
	chimeric dimer (1-373 with KHC 345-426)	80 mM PIPES (6.8)	-	61.0	(Duselder et al., 2012)
	chimeric dimer (1-373 with KHC 345-559)	80 mM PIPES (6.8)	-	64.0	(Shastry and Hancock, 2011)
H. sapiens	native dimer (1-513)	100 mM PIPES (6.8)	-	26.7	(Ma et al., 2011)
	native dimer (1-513)	80 mM PIPES (6.9)	150 mM sucrose	32.9	(Waitzman et al., 2011)
	native dimer (1-513)	10 mM PIPES (6.9)	-	47.2	(Krzysiak and Gilbert, 2006)
	native dimer (1-439)	80 mM PIPES (6.8)	-	37.0	(Yajima et al., 2008)
	chimeric dimer (1-370)* with KHC 337-432	80 mM PIPES (6.9)	100 mM K-acetate	104.0	(Kaseda et al., 2008)
	chimeric monomer (1-370)* with KHC 337-432	80 mM PIPES (6.9)	100 mM K-acetate	92.0	(Kaseda et al., 2008)
	native monomer (1-372)	80 mM PIPES (6.8)	-	42.0	(Yajima et al., 2008)
	native monomer (1-367)	80 mM PIPES (6.9)	150 mM sucrose	20.5	(Waitzman et al., 2011)
D. melanogaster	native tetramer	100 mM PIPES (6.9)	50-75 mM KCl	40.0	(Cole et al., 1994)
	native tetramer	80 mM PIPES (6.8)	-	32.0	(van den Wildenberg et al., 2008)
	native tetramer	20 mM Tris (8.0)	75 mM KCl	40.0	(Tao et al., 2006)