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HAF018). A specific band was detected for HMGB1/HMG-1 at approximately 26 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox" target="_blank">
MAB004) for 15 minutes in an ultrasonic bath, followed by Biotinylated Anti-Mouse IgG Secondary Antibody (Catalog # BAF007). Immunocomplexes were captured using 50 µL of MagCellect Streptavidin Ferrofluid (Catalog # MAG999) and DNA was purified using chelating resin solution. TheAFPpromoter was detected by standard PCR." class="big_lightbox" target="_blank">
MAB0041, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG F(ab')2Secondary Antibody (Catalog # F0102B). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules." class="big_lightbox" target="_blank">
NL007) and counterstained with DAPI (blue, lower panel). Specific staining was localized to nuclei. View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_lightbox" target="_blank">
CTS013). Tissue was stained using the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (brown; Catalog # VC001) and counterstained with hematoxylin (blue). Specific staining was localized to cell nuclei. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_lightbox" target="_blank">
HMGB1 and HMGB2 are part of the chromatin non-histone high mobility group proteins 1 and 2. HMGB1 and HMGB2 (containing multiple HMG-boxes) are conserved domains of 80 amino acids which mediate the DNA binding of many proteins. HMG box domains recognize DNA structure. Both HMGB1 and HMGB2 contain a N-terminal HMG box, a central HMG box, and an acidic carboxy terminus. The acidic tails of HMGB1 and HMGB2 contain multiple serine residues which match the phosphorylation consensus sites of casein kinase II, and phosphorylation of this domain appears to be important for proper functioning of these proteins. HMGB1 and HMGB2 have been shown to facilitate the binding of various sequence-specific transcription factors to their respective DNA binding sites. HMGB1 and HMGB2 may also serve as architectural factors that recognize and mediate DNA structural changes that accompany various events such as DNA repair, transcription, and replication.