UIC researchers, Scott Brady and Gerardo Morfini, created anti-KLC (63-90) with purified rat brain KLC1 as the initial immunogen1. The antibody maps within the N-terminal region. The 63-90 antibody has no effect on the axonal transport or membrane association of kinesin. The antibody also does not affect the ability of kinesin to bind microtubules or microtubule-activated ATPase activity. Phosphorylation of the epitope by CK2 and GSK3beta removes kinesin light chains from membrane bound vesicles and destroys its immunoreactivity to this antibody. Anti-KLC (63-90) has been used to confirm the homodimerization of KLC and the non-specificity of KLC interaction with kinesin-1 homodimers. Further UIC research utilized anti-KLC (63-90) to investigate links between Alzheimer’s associated mutations and kinesin function. Anti-KLC (63-90) has contributed to additional studies investigating such topics as the nuclear envelope, nesprin, myogenesis and Na,K-ATPase-containing vesicles. Nelson Grihalde grihalde@otm.uic.edu 312-996-4129
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