QUICK SEARCH:

[advanced]

	Author:		Keyword(s):

Home Help Feedback Subscriptions Archive Search Table of Contents

	Help viewing high resolution images
	Return to article

(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.

Fig. 6. Binding of filamin isoforms and variants to GST-myotilin and GST-FATZ-1 fusion proteins. (A) HA-tagged recombinant form of filamin-A (FLN-A), filamin-B (FLN-B), filamin-ß_Var-1 (FLN-B_var-1) and filamin-C (FLN-C), containing repeats 19-24 were generated by coupled in vitro transcription/translation and analyzed by SDS-PAGE and autoradiography. The positions of FLN-A, FLN-B and FLN-B_var-1 (arrowhead), and FLN-C (arrow) are indicated. (B,C) GST-fusion proteins immobilized on glutathione-agarose beads were incubated with the various radiolabeled filamin recombinants. After washing, bound proteins were analyzed by SDS-PAGE and autoradiography. Filamin-A, filamin-B, filamin-B_var-1 as well as filamin-C containing repeats 19-24 bind to GST-myotilin but not to GST alone (B). Filamin-A, filamin-B, filamin-B_var-1 as well as filamin-C containing repeats 19-24 bind to FATZ-1 but not to GST alone (C). The grouping of images was arranged from two different gels in B and in C. Note that filamin-B in the presence of FATZ-1 showed a tendency to proteolytic degradation under the conditions of the GST pull down experiments. Molecular mass markers are indicated in kDa.

Return to article