STN7 | Serine/threonine-protein kinase STN7, chloroplastic

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AS10 1611 | clonality: polyclonal | host: rabbit | reactivity:Arabidopsis thaliana


28 st
Item No:
AS10 1611

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product information
Background STN7 (serine/threonine protein kinase) (EC= in Arabidopsis thaliana, and its Stt7 homologue in Chlamydomonas reinhardtii, is required for LHCII phosphorylation and for state transitions. The loss of this thylakoid-associated kinase blocked stn7 (stt7)-deficient mutants in state 1. Alternative names: Protein STATE TRANSITION 7, Stt7 homolog.
Immunogen KLH-conjugated synthetic peptide (amino acids 128 – 141) specific for Arabidopsis thaliana STN7 serine/threonine kinase At1g68830 (Q9S713)
Host Rabbit
Clonality Polyclonal
Purity Affinity purified serum
Format Lyophilized
Quantity 50 ĩg
Reconstitution For reconstitution please add 50 ĩl 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

AS10 1601 | anti-STN8 kinase | serine/threonine-protein kinase STN8, chloroplastic for Arabidopsis thaliana, rabbit antibodies

AS15 3080 | anti-STN7 | serine/threonine-protein kinase STN7, chloroplastic for Chlamydomonas reinhardtii, rabbit antibodies

Secondary antibodies

Additional information An extract from STN7 mutant needs to be used in pararel to determine specific band of STN7 protein on a western blot.
application information
Recommended dilution 1: 2000 with standard ECL (WB)
Expected | apparent MW

63.2 | 44 kDa (on urea gel), 55 kDa (no urea)

Confirmed reactivity

Arabidopsis thaliana, Nicotiana tabacum

Predicted reactivity Glycine max, Oryza sativa, Ricinus communis, Zea mays, Vitis vinifera
Not reactive in Chlamydomonas reinhardtii
Additional information

For best results with this antibody sample buffer needs to contain 6 M urea (138mM TrisHCl pH 6.8, 6M urea, 22.2% Glycerol, 4.3% SDS).

STN7 is a nuclear encoded protein which is localized in chloroplast, hence posses a chloroplastic target peptides (cTP) at the beginning of the amino acid sequence which is cut off. Accroding to TargetP (program that predicts the length of the cTP:s) the length of cTP for Stn7 is 45aa. STN7 portein mobility can be also affected by urea present in the gel.

Selected references Mekala et al. (2015). Plants actively avoid state-transitions upon changes in light intensity - role of light-harvesting complex II protein dephosphorylation in high light. Plant Physiol. 2015 Apr 22. pii: pp.00488.2015.
et al. (2014). Natural variation in phosphorylation of photosystem II proteins in Arabidopsis thaliana: is it caused by genetic variation in the STN kinases? Philos Trans R Soc Lond B Biol Sci. 2014 Mar 3;369(1640):20130499. doi: 10.1098/rstb.2013.0499. Print 2014.
Yin et al. (2012). Photosystem II Function and Dynamics in Three Widely Used Arabidopsis thaliana Accessions. PLOS ONE, open access.

application example

western blot using anti-STN7 antibodies

Thylakoids 3 ug of chlorophyll/lane from Arabidopsis thaliana were extracted according to Sirpiö et al (2011, Methods Mol Biol. 2011;775:19-30) and were separated on 12 % SDS-PAGE containing 6 M urea and blotted 1h to PVDF. Blots were blocked with 5% milk in TTBS for 1h at room temperature (RT) with slow agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 over night at 4°C with slow agitation in 1 % milk TTBS . The antibody solution was decanted and the blot was rinsed briefly only once, then washed once for 15 min only in TBS-T at RT with vigorous agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated ) diluted to 1:10 000 in 1% milk in TTBS for 2h at 4°C with slow agitation. The blot was washed as above and incubated for 5 min with ECL-solution according to the manufacturers instructions. Exposure time was 1 min.

To avoid cross-reactivity with LHC proteins a gel can be run further to let proteins below 25 kDa leave a gel.

Courtesy Dr. Maija Holmström, University of Turku, Finland

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