|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Mouse GLO1 was immunoprecipitated using:
Lane A:0.5 mg 293T Whole Cell Lysate
Lane B:0.5 mg A549 Whole Cell Lysate
Lane C:0.5 mg HepG2 Whole Cell Lysate2 µL anti-Mouse GLO1 rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-Mouse GLO1 rabbit polyclonal antibody,at 1:200 dilutionSecondary antibody:
Dylight 800-labeled antibody to rabbit IgG (H+L), at 1:5000 dilutionDeveloped using the odssey technique.
Performed under reducing conditions.Predicted band size: 24 kDa
Observed band size: 24 kDa
Anti-GLO1 rabbit polyclonal antibody at 1:500 dilution
Lane A: 293T Whole Cell Lysate
Lane B: MCF7 Whole Cell Lysate
Lane C: A549 Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:21 kDa
Observed band size:23 kDa
(We are unsure as to the identity of these extra bands.)
Lactoylglutathione lyase, also known as Methylglyoxalase, Aldoketomutase, Glyoxalase I, Ketone-aldehyde mutase, S-D-lactoylglutathione methylglyoxal lyase and GLO1, is a member of the glyoxalase I family. GLO1 / Glyoxalase I is a ubiquitous cellular defense enzyme involved in the detoxification of methylglyoxal, a cytotoxic byproduct of glycolysis. Accumulative evidence suggests an important role of GLO1 expression in protection against methylglyoxal-dependent protein adduction and cellular damage associated with diabetes, cancer, and chronological aging. GLO1 / Glyoxalase I has been implicated in anxiety-like behavior in mice and in multiple psychiatric diseases in humans. GLO1 / Glyoxalase I catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. GLO1 / Glyoxalase I exists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties. GLO1 upregulation may play a functional role in glycolytic adaptations of cancer cells.