COXIIb | Cytochrome oxidase subunit II b
AS06 151 | clonality: polyclonal | host: rabbit | reactivity: Chlamydomonas reinhardtii | cellular [compartment marker] of mitochondrial inner membrane
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1: 5000 with alkaline phosphatase (WB), 1: 25 000 with standard ECL (WB)
|Expected | apparent MW||
|Confirmed reactivity||Chlamydomonas reinhardtii|
|Not reactive in||
no confirmed exceptions from predicted reactivity known in the moment
|Selected references||Volgusheva et al. (2017). Comparative analyses of H2 photoproduction in magnesium- and sulfur-starved Chlamydomonas reinhardtii cultures. Physiol Plant. 2017 Apr 7. doi: 10.1111/ppl.12576.
Schulz-Raffelt et al. (2016). Hyper-accumulation of starch and oil in a Chlamydomonas mutant affected in a plant-specific DYRK kinase. Biotechnol Biofuels. 2016 Mar 8;9:55. doi: 10.1186/s13068-016-0469-2. eCollection 2016.
Kropat et al. (2015). Copper economy in Chlamydomonas: Prioritized allocation and reallocation of copper to respiration vs. photosynthesis. Proc Natl Acad Sci U S A. 2015 Feb 2. pii: 201422492.
Dang et al. (2014). Combined Increases in Mitochondrial Cooperation and Oxygen Photoreduction Compensate for Deficiency in Cyclic Electron Flow in Chlamydomonas reinhardtii. Plant Cell. 2014 Jul 2. pii: tpc.114.126375.
Johnson et al. (2014). Proton Gradient Regulation 5-Mediated Cyclic Electron Flow under ATP- or Redox-Limited Conditions: A Study of ΔATPase pgr5 and ΔrbcL pgr5 Mutants in the Green Alga Chlamydomonas reinhardtii. Plant Physiol. 2014 May;165(1):438-52. doi: 10.1104/pp.113.233593. Epub 2014 Mar 12.
Chlamydomonas reinhardtii membrane extract (A), Chlamydomonas reinhardtii total cell extract, prepared by sonication, loading 14 µl equivalent to 30 µg of total protein (B), Chlamydomonas reinhardtii total cell extract, rapid, prepared directly by spinning down the cells and lysis of cell pellet in SDS-PAGE sample buffer and loading 14 µl equivalent to 98 µg of total protein (C), denatured at 100°C for 5 min. were separated on 15 % SDS-PAGE and blotted 1h to PVDF using tank transfer. Blots were blocked with 1 % blocking buffer (2 ml blocking reagent stock solution ROCHE 11 520 709 001 in 20 ml TBS) for ON at 4°C without agitation. Blot was incubated in the primary antibody at a dilution of 1: 25 000 for 1h 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 TBS-T at RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from Agrisera AS09 602) diluted to 1:20 000 in for 1h at RT with agitation. The blot was washed as above and developed according to manufacture instructions. Exposure time was 8 seconds.
Courtesy of Nadine Coosemans, Laboratoire de génétique et physiologie des microalgues, Université de Liège, Belgium
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