HMG1 (HMGB1, High Mobility Group, HMG Transcription Factor Box1, Amphoterin, Sulfoglucuronyl Carbohydrate Binding Protein, SBP-1, HMG3)

HMG box domains recognize DNA structure such as prebent, supercoiled or four way junction DNA, and non-specific DNA sequences. Both HMG-1 and HMG-2 contain an N-terminal HMG box, a central HMG box, and an acidic carboxy terminus. The acidic tails of these proteins contain multiple serine residues which match the phosphorylation consensus sites of casein kinase II. Phosphorylation of this domain appears to be important for proper functioning of these proteins. HMG-1/-2 have been shown to facilitate the binding of various sequence-specific transcription factors to their respective DNA binding sites such as steroid hormone receptors, p53, and Oct. HMG-1/-2 may serve as architectural factors that recognize and mediate DNA structural changes that accompany various events such as DNA repair, transcription and replication. Chromosomal HMG proteins have a global fold of three helices stabilized in an `L-shaped' configuration by two hydrophobic cores. The HMG domain binds to an AT rich DNA sequence using a large surface on the concave face of the protein, to bind the minor groove of the DNA. This bends the DNA helix axis away from the site of contact. The first and second helices contact the DNA. Their N-termini fitting into the minor groove. Helix 3 is primarily exposed to solvent. Partial intercalation of aliphatic and aromatic residues in helix 2 occurs in the minor groove.\n\nApplications: \nSuitable for use in ELISA, Western Blot, Immunohistochemistry (paraffin). Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 1:250\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nFor long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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