Kinesins are nano-sized biological motors which are responsible for active transport in cells. A single kinesin molecule is able to transport its cargo about 1 μm in the absence of external loads. However, kinesins perform much longer range transport in cells by working collectively. One of the most important mechanisms involved in this long transport are the binding and unbinding of kinesins to microtubules. Kinesins realize the transport by a repetitive mechanochemical cycle. In this study, the unbinding probabilities corresponding to each mechanochemical state of kinesin are calculated. The statistical characterization of the instants and locations of binding are captured by computing the probability of unbound kinesin being at given locations. The forces acting on kinesins affect binding and unbinding. This effect is also considered in this study. It reveals that the length of the transport is significantly longer when multiple proteins cooperatively transport the same cargo.