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{{/_source.additionalInfo}}Anti-FtsH3 + FtsH10 | ATP-dependent zinc metalloprotease FtsH3 + FtsH10 (mitochondrial)
(Cat#: AS07 204)
Description
- Immunogen: KLH-conjugated peptide dereived from sequences of Arabidopsis thaliana FtsH3 and FtsH10 with localization to mitochondria Q84WU8, At2g29080 and Q8VZI8, At1g07510
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Immunogen affinity purified serum in PBS pH 7.4.
- Format: Lyophilized
- Quantity: 200 µg
- Reconstitution: For reconstitution add 100 µl of sterile water
- Storage: Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
- Tested applications: Blue Native PAGE (BN-PAGE), Western blot (WB)
- Recommended dilutions: 1 : 500-1 : 1000 (WB)
- Expected | apparent MW: 80 kDa
- Confirmed reactivity: Arabidopsis thaliana
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- One of the several classes of mitochondrial proteases is membrane bound, ATPdependent FtsH protease. Their function is very important for the control of protein quality and quantity by degradation of unassembled subunits. Other names: AtFtsH3, cell division protease ftsH homolog 3, mitochondrial, AtFtsH10, cell division protease ftsH homolog 10, mitochondrial
- Kolodziejczak et al. (2018). m-AAA Complexes Are Not Crucial for the Survival of Arabidopsis Under Optimal Growth Conditions Despite Their Importance for Mitochondrial Translation. Plant Cell Physiol. 2018 May 1;59(5):1006-1016. doi: 10.1093/pcp/pcy041.Piechota et al. (2010). Identification and characetization of high-molecular-weight complexes fromed by m-AAA proteases and prohibitins in mitochondria of Arabidopsis thaliana. J Biol Chem. 2010 Apr 23;285(17):12512-21. doi: 10.1074/jbc.M109.063644.
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