Anti-NtrC thioredoxin reductase

Anti-NtrC thioredoxin reductase | Gentaur

Gentaur

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SKU :
451-AS07 243-GEN
Disponibilité :
IN STOCK
Size:
100 µg
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Anti-NtrC thioredoxin reductase

Immunogen KLH-conjugated peptide derived from N-terminal domain of NtrC of Chlamydomonas reinhardtii A8HNQ7
 
Host Rabbit Clonality Polyclonal
 
Purity Immunogen affinity purified serum in PBS pH 7.4. Format Lyophilized
 
Quantity 200 µg Reconstitution 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 the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
 
Tested applications Western blot (WB)
 
Recommended dilution 1 : 500 (WB)
 
Expectedapparent MW 55,349 kDa (following processing)

Genevestigator analysis has indicated heat shock induction of transcripts for NADPH-thioredoxin reductase, type C (NTRC) in the light. Here we show overexpression of NTRC in Arabidopsis (NTRC°E) resulting in enhanced tolerance to heat shock, whereas NTRC knockout mutant plants (ntrc1) exhibit a temperature sensitive phenotype. To investigate the underlying mechanism of this phenotype, we analyzed the protein’s biochemical properties and protein structure.

NTRC assembles into homopolymeric structures of varying complexity with functions as a disulfide reductase, a foldase chaperone, and as a holdase chaperone. The multiple functions of NTRC are closely correlated with protein structure. Complexes of higher molecular weight (HMW) showed stronger activity as a holdase chaperone, while low molecular weight (LMW) species exhibited weaker holdase chaperone activity but stronger disulfide reductase and foldase chaperone activities.

Heat shock converted LMW proteins into HMW complexes. Mutations of the two active site Cys residues of NTRC into Ser (C217/454S-NTRC) led to a complete inactivation of its disulfide reductase and foldase chaperone functions, but conferred only a slight decrease in its holdase chaperone function. The overexpression of the mutated C217/454S-NTRC provided Arabidopsis with a similar degree of thermotolerance compared with that of NTRC°E plants.

However, after prolonged incubation under heat shock, NTRC°E plants tolerated the stress to a higher degree than C217/454S-NTRC°E plants. The results suggest that the heat shock-mediated holdase chaperone function of NTRC is responsible for the increased thermotolerance of Arabidopsis and the activity is significantly supported by NADPH.

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