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Agrisera
DHAR2/Dehydroascorbate Reductase 2 Polyclonal Antibody
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FIGURE: 1 / 1
DHAR2/Dehydroascorbate Reductase 2 Antibody (AS11-1747) in WB
1 cm 2 of a leaf from Arabidopsis thaliana Col-0 (1) and or t-DNA insertion lines dhar 1-1 (2), dhar 1-2 (3), dhar 1-3 (4), dhar 2-1 (5), dhar 2-2 (6), dhar 1-3 EOS-DHAR 1 (7), was extracted using 200 µL Lyse& Load-Buffer (Grefen et al. 2009). 10 µL were separated on a 15% SDS-PAGE and blotted 1 h to PVDF (using Bjerrum Buffer in a semidry blot). Blots were blocked with 5% Milk in 1 x TBS-Tween 20 (1%) for ... View More
Product Details
AS11-1747
Product Specifications
Species Reactivity
Plant
Host/Isotype
Rabbit
Class
Polyclonal
Type
Antibody
Immunogen
KLH-conjugated synthetic peptide derived from known DHAR1 sequence of Arabidopsis thaliana.
Conjugate
Form
Lyophilized
Amount
200 µg
Purification
Antigen affinity chromatography
Storage buffer
PBS, pH 7.4
Contains
no preservative
Storage conditions
-20°C, Avoid Freeze/Thaw Cycles
Shipping conditions
Ambient (domestic); Wet ice (international)
Product Specific Information
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.
For reconstitution add 200 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana
Target Information
DHAR2 encodes a soluble, predominantly cytosolic dehydroascorbate reductase that functions in the ascorbate-glutathione cycle to maintain cellular redox homeostasis by catalyzing the glutathione-dependent reduction of dehydroascorbate back to ascorbate, thereby supporting antioxidant capacity during oxidative stress. The protein belongs to the glutathione transferase superfamily and adopts the canonical GST-like architecture, comprising an N-terminal thioredoxin-like domain that contributes to glutathione binding and a largely all-helical C-terminal domain; structural and mechanistic analyses indicate it acts as a monomer and relies on a conserved catalytic cysteine that undergoes reversible redox chemistry during turnover, consistent with a ping-pong-type mechanism involving sequential interaction with glutathione and dehydroascorbate. Genetic and cell biology studies support a role for DHAR2 in shaping glutathione/ascorbate redox states in vivo, with loss-of-function combinations affecting oxidative stress-linked signaling outputs, including salicylic acid pathway activation under elevated oxidative load.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: AT1G75270; dehydroascorbate reductase 2; F22H5.1; F22H5_1
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