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. 2015 Jun 17;10(6):e0127993. doi: 10.1371/journal.pone.0127993

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© 2015 Panwar 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.

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Fig 2 — SDS-PAGE profiles of buffalo KGF (A) and KITLG (B) proteins showing their resolved chromatographic fractions. M, Un, In and P denote marker, uninduced, induced and purified protein samples. The purified KGF and KITLG proteins were validated using western blot (WB) with anti-His (panel A) and anti-GST antibodies (panel B), respectively. The 23 and 57 kDa bands correspond to the purified KGF (His-tagged) and KITLG (GST tagged) proteins. (C and D) Co-immunoprecipitation of KGF and KITLG proteins. (C) The buffalo KGF and KITLG protein interactions were confirmed by immunoprecipitation of the tissue (ovary) lysate with anti-KGF antibody followed by immunoblotting with anti-KITLG IgG and detected a specific band of 31 kDa corresponding to KITLG protein. (D) In the reciprocal assay, a band of 22 kDa was detected on immunoprecipitation with anti-KITLG antibody followed by western blotting with anti-KGF IgG. The tissue lysate and resin in both C and D panels denote the positive and negative controls, respectively.