Bethyl Laboratories, Inc.
Antibodies to Kinesins
March 2010
Overview

 
The kinesins (KIFs) make up a large superfamily of motor proteins that function in intracellular transport along microtubules. Kinesin activity has been linked to various cellular functions such as organelle and vesicle transport, mitotic spindle formation, chromosome segregation, and cytokinesis. Structurally, all kinesins contain a motor domain with microtubule and nucleotide binding sites that utilize ATP to target cargo along microtubule filaments. The kinesin motor proteins have been implicated in human disease. A mutation in the KIF1B locus is associated with Charcot-Marie-Tooth disease (CMT2A) which is characterized by a progressive dysfunction of peripheral neurons and a lack of synaptic vesicle transport in nerve endings and axons. Over forty members of the KIF family have been identified and well characterized. However, when one considers the multitude of cellular tasks involving the intracellular transport of cargo, many questions concerning KIF regulation remain unanswered.






Detection of Human and Mouse KIF1B by WB and IP.

Samples: Whole cell lysate from HeLa (5, 15 and 50 mcg for WB; 1 mg for IP, 20% of IP loaded), 293T (T; 50 mcg) and mouse NIH3T3 (M; 50 mcg) cells.  Antibodies:  Affinity purified rabbit anti-KIF1B antibody A301-055A used for WB at 0.1 mcg/ml (A) and 1 mcg/ml (B) and used for IP at 3 mcg/mg lysate.  KIF1B was also immunoprecipitated by rabbit anti-KIF1B antibody A301-056A, which recognizes a downstream epitope.  For blotting immunoprecipitated KIF1B, ReliaBLOT® Reagents and Procedures WB120 were used. Detection:  Chemiluminescence with exposure times of 30 seconds (A) and 10 seconds (B).
Detection of KIF14 by Immunocytochemistry.

Samples:
Formaldehyde-fixed asynchronous HeLa cells.  Antibodies: Affinity purified rabbit anti-KIF14 Antibody IHC-00475 used at a dilution of 1:100.  Detection: Red-fluorescent goat anti-rabbit IgG highly cross-adsorbed Antibody Hilyte Plus 555 A120-501E used at a dilution of 1:100.
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