Horseradish conjugated goat α rabbit immunoglobulin g

Samples were prepared by harvesting exponentially growing M. xanthus cultures and subsequent resuspension in SDS lysis buffer to an equal concentration of cells. Western blot analyses were performed as described⁶⁵ with rabbit polyclonal α-PomX (1:10000)^{31 (link)}, α-PomY (1:10000)^{31 (link)}, α-PilC (1:3000)^{68 (link)}, or α-mCh (1:10000; Biovision) primary antibodies together with horseradish-conjugated goat α-rabbit immunoglobulin G (1:25000) (Sigma-Aldrich) as the secondary antibody. For PomY blots, protein transfer was performed with a Tris/CAPS buffer system (BioRad). Protein transfer was done with Trans-Blot Turbo buffer (BioRad) for all other blots. Blots were developed using Luminata Forte Western HRP Substrate (Millipore) and visualized using a LAS-4000 luminescent image analyzer (Fujifilm).

Western blot analyses were performed as described (Sambrook and Russell, 2001 ) with rabbit polyclonal α-PomX (1:15000), α-PomY (1:15000), α-PomZ (1:10000) (Schumacher et al., 2017 (link)), α-PilC (1:3000) (Bulyha et al., 2009 (link)), or α-mCh (1:10000; Biovision) primary antibodies together with horseradish-conjugated goat α-rabbit immunoglobulin G (Sigma-Aldrich) as secondary antibody (1:25000). Blots were developed using Luminata Forte Western HRP Substrate (Millipore) and visualized using a LAS-4000 luminescent image analyzer (Fujifilm).