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

. 2015 Jun 29;10(6):e0130416. doi: 10.1371/journal.pone.0130416

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

© 2015 Singer et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

PMC Copyright notice

Fig 3 — A. Co-immunoprecipitation of transiently transfected ZBTB16 (Myc-tagged) and NLRP7 (Flag-tagged) in HEK293T cells. Immunoprecipitation was done using an anti-Flag specific antibody. Quantification of interaction between NLRP7 and ZBTB16 was determined relative to NLRP7 full-length. B. Co-immunoprecipitation of five ZBTB16 deletion constructs del1-5 (Myc-tagged) by immunoprecipitation of full-length NLRP7 (Lane 1) or one of four NLRP7 deletion constructs (lane 2–5; Flag-tagged) using an anti-Flag specific antibody. C. Blue Native gel electrophoresis of NLRP7 (Flag-tagged) and ZBTB16 (Myc-tagged) after transient transfection in HEK293T cells. Native protein extraction was performed using different concentrations of digitonin that is indicated above the picture. Upper panels: In the first dimension, the native Flag-NLRP7 appears as a smeary oligomer in a broad shift from 480–1000 kD (left side), while native ZBTB16-Myc was detected as a sharp band at 480 kD (right side). Lower panels: In the second dimension, the monomeric Flag-NLRP7 is visible as a thin line at 113kD, while ZBTB16-Myc occurs as individual spot at its expected size of 75 kD.