Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2005 Jun 20;169(6):929–939. doi: 10.1083/jcb.200412114

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2005, The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 6. — The COOH-terminal part of the CLASP-MT–binding domain is required for high affinity MT binding in vitro. (A) Immunoblot of a MT sedimentation assay of bacterially expressed His6-CLASP2(340–1084) at constant concentration incubated with increasing concentrations of MTs. Note the slightly smaller degradation product (∼70 kD), which does not bind to MTs. (B) Comparison of MT binding of His6-CLASP2(340–1084) and His6-CLASP2(340–875). 2.5 μM MTs were incubated with increasing amounts of expressed CLASP2 proteins. 1× corresponds to the concentration used in A. Gels were loaded with equivalent amounts of protein in each lane. Even at concentrations at which His6-CLASP2(340–1084) began to saturate MTs (8×), binding of His6-CLASP2(340–875) to MTs could not be detected. S, supernatant; P, pellet. Molecular masses are indicated in kilodaltons on the right.