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. Author manuscript; available in PMC: 2022 Oct 10.
Published in final edited form as: J Mol Biol. 2020 Jul 6;432(17):4799–4814. doi: 10.1016/j.jmb.2020.06.024

Fig. 3. Addition of HA tags at the N-termini of the largest UNC-89 isoforms does not affect the normal M-line localization of UNC-89 in body wall muscle sarcomeres, but does moderately reduce the level of UNC-89 giant isoforms in whole animal extracts.

Fig. 3.

(A) Total Laemmli-soluble proteins from wild type and unc-89(syb797) were separated on a 5% SDS-PAGE, transferred to membrane and reacted with antibody EU30, a well-established rabbit polyclonal antibody to UNC-89. On the right is shown Ponceau S staining of the blots before reaction with antibodies. Note the presence of HA tags in unc-89(syb797) but not in wild type, and a moderate reduction in the level of UNC-89 giant isoforms in unc-89(sy797) compared with wild type. The asterisk indicates the position of the UNC-89 giant isoforms. The thin upper-most band is likely to be some UNC-89 that could not enter the separating gel. The positions of size markers are shown on the left-hand side. (B) Co-immunostaining of parts of two body wall muscle cells in unc-89(syb797) with anti-HA and MH42, a well-established monoclonal that recognizes UNC-89. Note the co-localization of each antibody to the M-lines of these muscle sarcomeres (merged image). Scale bar, 10 μm.