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. 2013 Feb;27(2):568–580. doi: 10.1096/fj.12-209445

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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/us/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — Cross-linking purified β3 Ig domain generates higher Mwt dimer and trimers. Purified native β3-Ig-6His protein (A) and purified β3-Ig-6His containing the selectively reduced and alkylated C_2–24 disulfide bond (B) were cross-linked with BS³ as described in Materials and Methods for the times indicated, then examined by denaturing PAGE. Higher-molecular-mass bands corresponding to dimer (D) and trimer (T) are indicated for the case of the native β3-Ig-6His protein. Mwt, molecular weight (mass).