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AOX1 | alternative oxidase 1

320 €

AS06 152  |  clonality: polyclonal  |  host: rabbit  |  reactivity: Chlamydomonas reinhardtii  |  cellular [compartment marker] of mitochondrial inner membrane

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Item No:
AS06 152

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product information
background  

The mitochondrial AOX (alternative oxidase) of the unicellular green alga Chlamydomonas reinhardtii is encoded by two different genes, the Aox1 and Aox2. The  alternative respiratory pathway is comprised of a single homodimeric protein – AOX – and functions as a mechanism to decrease the formation of reactive oxygen species (ROS) produced during respiratory electron transport.  Alternative oxidase expression is  influenced by different stress stimuli.

immunogen  

whole presumed mature AOX1 protein from from Chlamydomonas reinhardtii O65000 fused to GST

antibody format  

rabbit

polyclonal

serum

lyophilized

quantity  

100 µl

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 tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

tested applications  

western blot (WB)

related products  

AS04 054 | anti-plant alternative oxidase 1 and 2 polyclonal antibody

AS10 699 | AOX | alternative oxidase monoclonal antibody

Collection of antibodies to Chlamydomonas proteins

additional information  

cellular [compartment marker] of Chlamydomonas reinhardtii mitochondrial inner membrane

application information
recommended dilution  

1: 10 000 with alkaline phosphatase (WB)

expected | apparent MW  

36 | 36 kDa (Chlamydomonas reainhardii)

confirmed reactivity  

Chlamydomonas reinhardtii

predicted reactivity  

Ostreococcus lucimarinus, Aspergilus niger

 

not reactive in  

no confirmed exceptions from predicted reactivity known in the moment

additional information  

to be added when available

selected references  

Bohne et al. (2013). Reciprocal Regulation of Protein Synthesis and Carbon Metabolism for Thylakoid Membrane Biogenesis. PLOS, Open Access.



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