|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
sumo1 was immunoprecipitated using:
Lane A:0.5 mg Hela Whole Cell Lysate
Lane B:0.5 mg A431 Whole Cell Lysate2 µL anti-sumo1 rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-sumo1 rabbit polyclonal antibody,at 1:500 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: 12 kDa
Observed band size: 18 kDa
Anti-sumo1 rabbit polyclonal antibody at 1:1000 dilution
Lane A: Hela Whole Cell Lysate
Lane B: A431 Whole Cell Lysate
Lane C: NIH-3T3 Whole Cell Lysate
Lane D: HL60 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:12 kDa
Observed band size:15 kDa
(We are unsure as to the identity of these extra bands.)
Small ubiquitin-like modifier protein (SUMO) modification is a highly dynamic process, catalyzed by SUMO-specific activating (E1), conjugating (E2) and ligating (E3) enzymes, and reversed by a family of SUMO-specific proteases (SENPs). Small ubiquitin-like modifier 1 (SUMO1) is a member of the superfamily of ubiquitin-like proteins. Despite its structural similarity with ubiquitin, SUMO1 does not seem to play any role in protein degradation. SUMO1 plays an important role in modulation of NOX activity required for ROS generation. SUMO1 haploinsufficiency results in cleft lip and palate in animal models. SUMO1 gene variation in human non-syndromic cleft lip with or without cleft palate (NSCLP) development. SUMO-1 may be useful as a novel target for therapy in oral squamous cell carcinoma (SCC) as well as a clinical indicator for tumor recurrence together with Mdm2.