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Fig. 1 | BMC Molecular and Cell Biology

Fig. 1

From: Design and structural characterisation of olfactomedin-1 variants as tools for functional studies

Fig. 1

Purification of three novel Olfm1 constructs; Olfm1Olf, Olfm1coil-Olf and Olfm1BMY. a Overview of Olfm1 sequence and isoform differences. Indicated domain widths scale with amino acid sequence length. N-linked glycosylation sites and cysteines are indicated. b Architecture of tetrameric Olfm1BMZ (full-length) isoform as previously determined [6]. Colours correspond to domains as indicated in panel a. c Coomassie-stained SDS-PAGE analysis of purified Olfm1Olf, Olfm1coil-Olf and Olfm1BMY shows a high degree of purity and confirms correct formation of disulfides in Olfm1coil-Olf and Olfm1BMY as evidenced by the shift under non-reducing (−DTT) conditions. The multiple bands predominantly visible in the reduced samples, with apparent weight differences of a few kDa, are the result of heterogeneous N-linked glycosylation (Fig. 2)

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