GLN2 | GS2, chloroplastic form of glutamine synthetase

345 €

AS08 296  |  clonality: polyclonal  |  host: rabbit  | reactivity: A. thaliana, O. sativa, P. sativum, S. oleracea


20 st
Item No:
AS08 296

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product information

Glutamine synthetase (GLN or GS) is one of the key enzymes involved in nitrogen metabolism of plants. It catalyses the synthesis of glutamine from glutamate and ammonia in an ATP-dependent reaction. There are two general classes of glutamine synthetase in plants: GLN1, a cytosolic form and GLN2, a chloroplastic form. GLN2 is encoded by a single gene and is highly abundant in mesophyll cells of leaves for the assimilation of ammonia produced from photorespiration and the reduction of nitrate in the chloroplasts. GLN2 is a target for thioredoxin.


KLH-conjugated synthetic peptide which is a part of part of the glutamine synthetase/guanido kinase superfamily catalytic region chosen from various available sequences, including Arabidopsis thaliana GLN2, UniProt: Q43127, TAIR: AT5G35630

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 400 ĩl
Reconstitution For reconstitution add 400 ĩl of sterile water.

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

AS08 295 GLN1 GLN2 | GS1 glutamine synthetase global antibody

Additional information
application information
Recommended dilution

1:5000 on 0.5-5 ug protein/lane with ECL Advance detection (WB)

Expected | apparent MW

47 | 44-45 kDa

Confirmed reactivity

Arabidopsis thaliana, Oryza sativa, Pisum sativum, Spinacia oleracea

Predicted reactivity

dicots including: Brassica napus, Glycine max,  Phaseolus vulgaris, monoctos including: Hordeum vulgare, Triticum, aestivum,Zea mays,trees: Pinus sylvestris, Populus sp.,  moss: Physcomitrella patens,

Not reactive in


Additional information

to be added when available

Selected references Dixit (2015). Sulfur alleviates arsenic toxicity by reducing its accumulation and modulating proteome, amino acids and thiol metabolism in rice leaves. Sci Rep. 2015 Nov 10;5:16205. doi: 10.1038/srep16205.
Lee et al. (2013). Stromal protein degradation is incomplete in Arabidopsis thaliana autophagy mutants undergoing natural senescence. BMC Res Notes, Jan 17.
Hu and Li
(2012). The amino-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo. Plant Physiol. Apr;158(4):1656-65. doi: 10.1104/pp.112.193300. Epub 2012 Feb 21.

application example

0.5 µg of protein from Arabidopsis thaliana total leaf fraction (1), 5 µg of protein fromSpinacia oleracea chlorplast enriched fraction (2), molecular weight markers (MagicMarkTM,Invitrogen) (M), the same samples as in 1 and 2 but after peptide neutralisation assay, e.g.  incubation of the antibody with 100 mM excess of peptide used to elicit andt-GLN2 antibody (4,5), extracted with PEB (AS08 300), were separated on  4-12% NuPage (Invitrogen) LDS-PAGE and blotted 1h to PVDF (Millipore). Filters were blocked 1h with 2% low-fat milk powder in TBS-T (0.1% TWEEN 20) and probed with anti-GLN2 antibody (AS08 296, 1:5 000, 1h) and secondary anti-rabbit (1:20000, 1 h) antibody (HRP conjugated, Abcam) in TBS-T containing 2% low fat milk powder. Antibody incubations were followed by washings in TBS-T. All steps were performed at RT with agitation. Blots were developed for 5 min with ECL Advance detection reagent according the manufacturers instructions (GE Healthcare). Images of the blots were obtained using a CCD imager (FluorSMax, Bio-Rad) and Quantity One software (Bio-Rad). 


  Western blot detection using anti-GLN2 antibodies

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