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

. 2021 Jul 13;11(16):8112–8128. doi: 10.7150/thno.54961

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

© The author(s)

This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions.

PMC Copyright notice

CCDC65 interacts with ENO1. (A) Coomassie brilliant blue staining showed the proteins that interacted with CCDC65 in AGS cells and the molecular weight of CCDC65 and ENO1. (B) Co-IP detected the interaction of exogenous CCDC65 and ENO1. (C) Co-IP detected the interaction of endogenous CCDC65 and ENO1. (D) Colocalization of CCDC65 and ENO1 in HEK293T cells by immunofluorescence staining. (E) N-terminal deletion mutant domain (Flag-CCDC65-130-484) of CCDC65 is important for interaction with ENO1. The mutants of CCDC65 were transfected into HEK293T cells and analyzed by immunoprecipitation using anti-Flag antibody. (F) The C-terminal TIM barrel domain (Myc-ENO1-140-434) of ENO1 is required for its interaction with CCDC65. The mutants of ENO1 were transfected into HEK293T cells and analyzed by immunoprecipitation using anti-Myc antibody.