Form
Liquid
Buffer
PBS
Preservative
0.02% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
Batch dependent (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
purified recombinant human HMG-1.
Purification
Purified immunoglobulin
Conjugation
Unconjugated
RRID
AB_367629
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
high mobility group box 1 , HMG-1 , HMG1 , HMG3 , SBP-1
Cellular Localization
Nucleus,Cytoplasm,Secreted,Cell membrane,Endosome
Background
HMG1 and HMG2, chromatin non-histone high mobility group proteins 1 and 2, are 27 and 25 kDa members of a family of proteins containing multiple HMG-boxes, conserved domains of 80 amino acids which mediate DNA binding of many proteins. HMG box domains recognize DNA structure, such as prebent, supercoiled or four way junction DNA, and non- specific DNA sequences. Both HMG1 and HMG2 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, and phosphorylation of this domain appears to be important for proper functioning of these proteins. HMG1/2 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. HMG1/2 may serve as architectural factors that recognize and mediate DNA structural changes that accompany various events such as DNA repair, transcription and replication.
Database
Research Area