Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, M||WB, ICC, IP||R||Purified||Monoclonal Antibody|
|Presentation||Purified rat monoclonal IgG2aκ in buffer containing PBS.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at 2-8°C from date of receipt.|
|Material Size||100 µg|
|Anti-EB1, EB2 and EB3, clone KT65 - QVP1310183||QVP1310183|
|Reference overview||Pub Med ID|
|SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase. |
van der Vaart, Babet, et al.
J. Cell Biol., 193: 1083-99 (2011) 2011
The ends of growing microtubules (MTs) accumulate a set of diverse factors known as MT plus end-tracking proteins (+TIPs), which control microtubule dynamics and organization. In this paper, we identify SLAIN2 as a key component of +TIP interaction networks. We showed that the C-terminal part of SLAIN2 bound to end-binding proteins (EBs), cytoplasmic linker proteins (CLIPs), and CLIP-associated proteins and characterized in detail the interaction of SLAIN2 with EB1 and CLIP-170. Furthermore, we found that the N-terminal part of SLAIN2 interacted with ch-TOG, the mammalian homologue of the MT polymerase XMAP215. Through its multiple interactions, SLAIN2 enhanced ch-TOG accumulation at MT plus ends and, as a consequence, strongly stimulated processive MT polymerization in interphase cells. Depletion or disruption of the SLAIN2-ch-TOG complex led to disorganization of the radial MT array. During mitosis, SLAIN2 became highly phosphorylated, and its interaction with EBs and ch-TOG was inhibited. Our study provides new insights into the molecular mechanisms underlying cell cycle-specific regulation of MT polymerization and the organization of the MT network.