HMGB1/HMG-1 Protein, Human

The multifunctional and redox-sensitive HMGB1/HMG-1 protein plays multiple roles in cellular compartments. In the nucleus, it serves as a major chromatin-associated non-histone protein involved in key processes such as replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair, and genome stability. HMGB1/HMG-1 Protein, Human is the recombinant human-derived HMGB1/HMG-1 protein, expressed by E. coli , with tag free.

HMGB1/HMG-1, a multifunctional redox-sensitive protein, exhibits diverse roles across different cellular compartments. Within the nucleus, it stands as a major chromatin-associated non-histone protein, functioning as a DNA chaperone involved in crucial processes such as replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair, and genome stability. Proposed as a universal biosensor for nucleic acids, HMGB1/HMG-1 plays a pivotal role in promoting the host inflammatory response to both sterile and infectious signals, coordinating innate and adaptive immune responses. In the cytoplasm, it serves as a sensor and/or chaperone for immunogenic nucleic acids, activating TLR9-mediated immune responses and mediating autophagy. Released to the extracellular environment, HMGB1/HMG-1 engages with various molecules such as DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS), and lipoteichoic acid (LTA), activating cells through multiple surface receptors. The extracellular HMGB1 exists in different redox states, with fully reduced HMGB1 acting as a chemokine, disulfide HMGB1 as a cytokine, and sulfonyl HMGB1 promoting immunological tolerance. Beyond its immunomodulatory roles, HMGB1/HMG-1 is implicated in proangiogenic activity, platelet activation, neuronal outgrowth signaling via RAGE, and potential involvement in the accumulation of expanded polyglutamine proteins. Its nuclear functions, attributed to fully reduced HMGB1, include association with chromatin, DNA bending, and enhancement of DNA flexibility through looping, facilitating various gene promoter activities. Additionally, HMGB1/HMG-1 may play roles in nucleotide excision repair, mismatch repair, base excision repair, double-strand break repair, V(D)J recombination, displacement of histone H1, restructuring nucleosomes, enhancing transcription factor binding, and modulating the telomerase complex. The intricate functions of HMGB1/HMG-1 highlight its significance in diverse cellular processes.

Measured by its ability to down regulate the expression of TNF-α by THP-1 cells treated with 2 μg/mL LPS.

Human

E. coli

Tag Free

P09429 (M1-F89)

3146  [NCBI]

Partial

MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKF

Approximately 14 kDa

• 
  ≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 50 mM HEPES, 500 mM NaCl, 0.5 mM DTT, pH 7.9.
2.Lyophilized from a 0.22 μm filtered solution of 50 mM HEPS, 500 mM NaCl, 0.5 mM DTT, pH 8.0.
3.Lyophilized from a 0.22 μm filtered solution of PBS, pH 6.5, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.