FtsZ | Procaryotic cell division GTPase (cyanobacterial)
AS07 217 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Cyanobacteria
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|Recommended dilution||1 : 200 (IL) Immunogold-TEM, 1 : 500 (IF), 1 : 2000-1 : 5000 (WB)|
|Expected | apparent MW||
44.5 | 50 kDa
|Confirmed reactivity||Cylindrospermopsis raciborskii CS-505, Listeria monocytogenes (weak reaction), Synechococcus elongatus|
Phaeodactylum tricornutum, Prochlorococcus sp.
|Not reactive in||No confirmed exceptions from predicted reactivity are currently known.|
This antibody can be used as a loading control antibody in cyanobacteria.
Immunofluorescence has been done by labelling Synechococcus elongatus cells at 30°C for 2 hours with FtsZ antibodies diluted to 1: 500 in blocking buffer. Detection images can be found in Kabeya et al (2010).
|Selected references||MacCready et al. (2016). Robust Min-System Oscillation in the Presence of Internal Photosynthetic Membranes in Cyanobacteria. Molecular Microbiology November 5 2016. doi: 10.1111/mmi.13571
Probst et al. (2014). Biology of a widespread uncultivated archaeon that contributes to carbon fixation in the subsurface. Nat Commun. 2014 Nov 26;5:5497. doi: 10.1038/ncomms6497.
Miyagishima et al. (2014). DipM is required for peptidoglycan hydrolysis during chloroplast division. BMC Plant Biol. 2014 Mar 6;14(1):57. (immunofluorescence)
Plominsky et al. (2013). Dinitrogen Fixation Is Restricted to the Terminal Heterocysts in the Invasive Cyanobacterium Cylindrospermopsis raciborskii CS-505. PLOS ONE, Open Access.
Kabeya et al (2010). The YlmG protein has a conserved function related to the distribution of nucleoids in chloroplasts and cyanobacteria. BMC Plant Biology 10:57.
Total protein samples (5 or 10 µg) from: Arabidopsis thaliana, leaf (1), Synechocystis 6803 motile (2), Synechocystis 6803 GT (glucose tolerant strain) (3), Synechococcus elongates 7942 (4), Marker - Pierce™ Prestained Protein MW Marker (kat #26612) were extracted with buffer (10mM Tris HCl, pH 8.0, 0.5% LDS, 4% glycerol, 0.1 mM EDTA ) were mixed with sample buffer and denatured for 5 min at 95°C. Samples were separated on 10% SDS -PAGE and blotted 1h to nitrocellulose membrane (Amersham Protran) using sem i-dry transfer (Bio -Rad) in standard transfer buffer in presence of 10% methanol. Transfer of proteins to the membrane was checked using 0,5% Ponceau S staining before the blocking step. Blots were blocked in buffer (2% low -fat milk in 1xPBS, 0,1% Tween) for 1h at room temperature (RT) with agitation. Blots were incubated in the primary antibody at a dilution of 1: 1000 at RT with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in PBS -T at RT with agitation. Blot was incubated in secondary antibody ( goat anti -rabbit IgG, AS09 602, Agrisera) diluted to 1:30 000 for 1h at RT with agitation. The blot was washed as above and developed for 5 min with C larity Western ECL Substrate and ChemiDoc detection system.
Courtesy Dr. Elena Pojidaeva, Laboratory of Plant Gene Expression, Timiryazev Institute of Plant Physiology RAS, 127276 Moscow Russia
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