Figure 1
From: A mass spectrometry-based approach for the identification of Kpnβ1 binding partners in cancer cells
Immunoprecipitation of Kpnβ1. (A) Endogenous Kpnβ1 protein levels in non-cancer hTERT-RPE-1 cells, HeLa cervical cancer cells and WHCO5 and KYSE30 oesophageal cancer cells. GAPDH was used to control for protein loading. (B) Kpnβ1 was successfully immunoprecipitated using 50 µg of a Kpnβ1 agarose-conjugated antibody from hTERT-RPE-1, HeLa, WHCO5 and KYSE30 cell extracts. Kpnβ1 was not pulled down in lysates incubated with a non-specific IgG isotope control and protein A agarose beads. GAPDH was not pulled down with Kpnβ1, as expected.
