protein

Animal-Free HMGB1/HMG-1 Protein, Mouse (His)

HY-P700182AF

10 μg;50 μg

215;600 USD

Animal-Free HMGB1/HMG-1 Protein, Mouse (His)

proteins

E. coli

10 μg;50 μg

215;600 USD

HMGB1, or high mobility group box 1, is a protein that plays a role in various cellular processes. It has different functionalities depending on its redox state and location within the cell. Animal-Free HMGB1/HMG-1 Protein, Mouse (His) is the recombinant mouse-derived animal-FreeHMGB1/HMG-1 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free HMGB1/HMG-1 Protein, Mouse (His) is 215 a.a., with molecular weight of ~25.56 kDa.This product is for cell culture use only.

Mouse

HMGB1/HMG-1 protein, a multifunctional redox-sensitive molecule, assumes diverse roles across different cellular compartments. Within the nucleus, it stands as a major chromatin-associated non-histone protein, functioning as a DNA chaperone pivotal in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair, and genome stability. Proposed as a universal biosensor for nucleic acids, HMGB1 also plays a crucial role in promoting host inflammatory responses to both sterile and infectious signals, contributing to the coordination and integration of 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. Operating as a danger-associated molecular pattern (DAMP) molecule, HMGB1 amplifies immune responses during tissue injury. Upon release into the extracellular environment, it binds to a spectrum of molecules such as DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS), and lipoteichoic acid (LTA), activating cells through engagement with multiple surface receptors. The extracellular HMGB1 exhibits distinct functionalities, with fully reduced HMGB1 acting as a chemokine, disulfide HMGB1 functioning as a cytokine, and sulfonyl HMGB1 from apoptotic cells promoting immunological tolerance. Beyond its immunomodulatory roles, HMGB1 demonstrates proangiogenic activity and may be involved in platelet activation. It engages in various cellular functions, including binding to phosphatidylserine and phosphatidylethanolamide, mediating signaling for neuronal outgrowth via RAGE, and potentially contributing to the accumulation of expanded polyglutamine (polyQ) proteins. In the nucleus, its nuclear functions are attributed to fully reduced HMGB1, associating with chromatin, binding DNA with a preference for non-canonical DNA structures, and participating in DNA repair pathways, including nucleotide excision repair (NER), mismatch repair (MMR), base excision repair (BER), and double-strand break repair such as non-homologous end joining (NHEJ). HMGB1 also acts as a cofactor of the RAG complex in V(D)J recombination, displaces histone H1 from highly bent DNA in vitro, and can restructure the canonical nucleosome, leading to relaxation of structural constraints for transcription factor binding. Furthermore, it enhances the binding of sterol regulatory element-binding proteins (SREBPs) like SREBF1 to their cognate DNA sequences, increases their transcriptional activities, and facilitates the binding of TP53 to DNA. While proposed to be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion, this function has been subject to debate. Additionally, HMGB1 can modulate the activity of the telomerase complex and may be implicated in telomere maintenance. Overall, HMGB1 emerges as a versatile protein with intricate roles in cellular processes across diverse cellular compartments.

HMG-1; Hmg1; SBP; SBP-1; amph; p3; p30

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a solution containing 1X PBS, pH 7.4, trehalose.

Room temperature in continental US; may vary elsewhere.