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GLN2 | GS2, chloroplastic form of glutamine synthetase

345 €

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

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Item No:
AS08 296

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product information
Background

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.

Immunogen

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
Clone
Purity Serum
Format Lyophilized
Quantity 400 µl
Reconstitution For reconstitution add 400 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

AS08 295 GLN1 GLN2 | GS1 glutamine synthetase global antibody

Additional information
application information
Recommended dilution 1 : 5000 on 0.5-5 ug protein/lane detection (WB)
Expected | apparent MW

47 | 44-45 kDa

Confirmed reactivity Arabidopsis thaliana, Oryza sativa, Pisum sativum, Spinacia oleracea
Predicted reactivity Brassica napus, Glycine max, Hordeum vulgare, Pinus sylvestris, Phaseolus vulgaris, Physcomitrella patens, Populus sp., Triticum, aestivum, Zea mays
Not reactive in Diatoms
Additional information
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) 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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