|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant human protein purified from E.coli.|
|Purification||Ammonium sulfate precipitation|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||Assay Dependent|
|Western Blot (WB)||1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
A suggested positive control for this product is HeLa cells.
Glutathione reductase (GR) is a member of pyridine nucleotide-disulfide oxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG) : GSSG + NADPH + H+ to 2GSH + NADP+. In most eukaryotic cells, GR maintains the ratio of [GSH]/[GSSG] elevated, and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment.
LF-PA0056 was used in western blot to investigate pyridine nucleotide redox state in the endoplasmic reticulum lumen
|Piccirella S,Czegle I,Lizák B,Margittai E,Senesi S,Papp E,Csala M,Fulceri R,Csermely P,Mandl J,Benedetti A,Bánhegyi G||The Journal of biological chemistry (281:4671)||2006|