FtsH2 + FtsH8 | ATP-dependent zinc metalloprotease FtsH2 + FtsH8 (chloroplastic)

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AS16 3929 | clonality: polyclonal | host: rabbit | reactivity: Arabidopsis thaliana, Nicotiana tabacum, Spinacia oleracea


28 st
Item No:
AS16 3929

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product information

FtsH belong to a family of ATP dependent peptidases. Localized in a chloroplast are following isoforms: FTSH1 (synonymes AAA, FTSH, FTSH Protease 1), Ftsh2 (VAR2, VARIEGATED 2), FtsH5 (VAR1, VARIEGATED 1), FtsH6 (FTSH PROTEASE 6), FtsH7, FtsH8. FtsH9. Localized in mitochondria are following isoforms: FtsH3, FtsH4, FtsH10, FtsH11.

FtsH2 (VAR2) is a component of the ATP-dependent zinc metallopeptidase. It is involved in the thylakoids biogenesis and in the repair of damaged D1 subunit of photosystem II, a process that protects against cell death under high light conditions. VAR1 transcript and protein levels increase with light intensity and it forms a complex with VAR1. Mutants show a variegated phenotype, which decreases during development.
Immunogen Recombinant Arabidopsis thaliana FtsH2, UniProt: O80860; TAIR: At2g30950


Clonality Polyclonal
Purity Serum
Format Lyophilized

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)
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AS11 1789S | FtsH2 positive control/quantitation standard
AS11 1789 | anti-FtsH1-11 | ATP-dependent zinc metalloprotease FtsH1-11
AS16 3930 | anti-FtsH1 + FtsH5 | ATP-dependent zinc metalloprotease FtsH1 + FtsH5 (chloroplastic)
AS07 204 | anti-FtsH3 + FtsH10 | ATP-dependent zinc metalloprotease FtsH3 + FtsH10 (mitochondrial)
AS07 205 | anti-FtsH4 | ATP-dependent zinc metalloprotease FtsH4 (mitochondrial)
AS05 094A | anti-FtsH6 | ATP-dependent zinc metalloprotease FtsH6 (chloroplastic)
AS06 130 | anti-FtsH9 | ATP-dependent zinc metalloprotease FtsH9 (chloroplastic)
AS07 251 | anti-FtsH10 | ATP-dependent zinc metalloprotease FtsH10 (mitochondrial)

Antibodies to other proteins involved in photosynthesis

Plant and algal protein extraction buffer

Secondary antibodies

Additional information

To be added when available.

application information
Recommended dilution

1: 5000

Expected | apparent MW

65.6 kD (Arabidopsis thaliana)

Confirmed reactivity

Arabidopsis thaliana, Nicotiana tabacum, Spinacia oleracea

Predicted reactivity
Not reactive in

No confirmed exceptions from predicted reactivity known in the moment.

Additional information Both FtsH2 (VAR2) and FtsH8 share high degree of homology therefore this antibody recognizes both proteins.
Selected references

Application example

Western blot using anti-FtsH2 antibodies on Arabidopsis thaliana wt and var2 mutant

Total proteins were isolated from Arabidopsis (Arabidopsis thaliana) wild type (Col) and mutant lacking FtsH2 (yellow variegated2 [var2]). Samples were immediately frozen in liquid nitrogen and pulverized with a microtube homogenizer. Proteins were extracted by adding appropriate extraction buffer. Proteins were extracted by adding appropriate extraction buffer. After measurement of chlorophyll concentration, equally loaded supernatants (based on chlorophyll [0.5 µg chlorophyll/lane]). Proteins were separated on 12% SDS-PAGE gel and blotted 1h to PVDF membrane. Blots were blocked in 1% BSA in PBST buffer for 1 h at room temperature. Then, blots were incubated in the primary antibody (anti-VAR2) at a dilution of 1:5000 for 1 h. After washing 2 times for 10 min in PBST buffer, blots were incubated in the secondary antibody (anti Rabbit IgG) at a dilution of 1:5000 for 1 h. Blots were washed 2 times for 10 min in PBST buffer. Luminata crescendo (Millipore) was used for signal detection. Images of the blots were obtained using ChemiDoc™ XRS (Bio-rad). Exposure time was 2 seconds.
Detected signal in var2 mutant is attributed to high homology of FtsH2 with FtsH8 (another type-B subunit).
Courtesy of Dr. Yusuke Kato, Plant Light Acclimation Research Group, Okayama University, Japan

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