Aging continues to be a central theme in biomedical research, and HMGB1 has emerged as a critical player in the chronic, low-grade inflammation that underpins many age-related conditions. To study HMGB1 contribution with greater precision, we now have a new tool: BoxAB, a tailless, LPS-free form of HMGB1.
Composed of both BoxA and BoxB DNA-binding domains, BoxAB replicates the core structure of HMGB1 while lacking the acidic C-terminal tail—a region known to modulate HMGB1’s activity via electrostatic autoinhibition and flexible interactions.
This tailless variant is LPS-free and optimized for high-sensitivity applications in: in vitro signaling studies, cell-based assays and receptor-ligand binding analysis.
BoxAB enables targeted HMGB1 analysis
BoxAB has already been successfully employed in independent peer-reviewed studies.
In a study by Mantonico et al, BoxAB from HMGB1 protein has been used to dissect the structural complexity of the frHMGB1•CXCL12 heterocomplex, demonstrating that the acidic tail—absent in BoxAB—is a key mediator of the “fuzzy” and dynamic interactions with CXCL12 and cell-surface CXCR4.
The absence of the tail in BoxAB allowed precise mapping of interaction regions and highlighted the tail’s role in heterocomplex formation.
Moreover in a research by Wang et al, HMGB1 was shown to be proteolytically cleaved by neutrophil elastase in NETs, specifically removing the C-terminal D/E-rich tail. This tail truncation significantly increased HMGB1’s binding affinity to TLR4•MD-2, DNA G-quadruplexes, and Holliday junctions.
At HMGBiotech Srl, we provide comprehensive information to facilitate informed decision-making for researches with HMGB1.
Discover more about our BoxAB from HMGB1 protein
Read the full articles about the studies:
https://pmc.ncbi.nlm.nih.gov/articles/PMC10853541/
https://pubmed.ncbi.nlm.nih.gov/36220391/
