Synthesized peptide derived from human HMGB1 (Acetyl Lys3)

This antibody detects endogenous levels of Human,Mouse,Rat HMGB1 (Acetyl Lys3).The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):GkGDP

HMGB1 HMG1

HMG-1 (Acetyl Lys3)

High mobility group protein B1 ;
High mobility group protein 1 ;
HMG-1 ;

function:Binds preferentially single-stranded DNA and unwinds double stranded DNA.,similarity:Belongs to the HMGB family.,similarity:Contains 2 HMG box DNA-binding domains.,

negative regulation of transcription from RNA polymerase II promoter, DNA metabolic process, DNA replication, DNA-dependent DNA replication, DNA ligation, DNA unwinding during replication, DNA repair, base-excision repair, base-excision repair, DNA ligation, DNA recombination, chromatin organization, regulation of transcription, DNA-dependent,regulation of transcription from RNA polymerase II promoter, anti-apoptosis, response to DNA damage stimulus,negative regulation of biosynthetic process, negative regulation of macromolecule biosynthetic process, negative regulation of macromolecule metabolic process, negative regulation of gene expression, regulation of cell death,negative regulation of transcription, negative regulation of transcriptional preinitiation complex assembly, negative regulation of cellular biosynthetic process, DNA geometric change, DNA duplex unwinding, cellular response to stress,regulation of apoptosis, negative regulation of apoptosis, regulation of programmed cell death, negative regulation of programmed cell death, regulation of protein complex assembly, regulation of cellular component biogenesis,regulation of transcription, negative regulation of transcription, DNA-dependent, regulation of transcriptional preinitiation complex assembly, negative regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process, DNA ligation during DNA repair, negative regulation of cellular component organization, negative regulation of nitrogen compound metabolic process, regulation of RNA metabolic process, negative regulation of RNA metabolic process, chromosome organization, regulation of transcription initiation from RNA polymerase II promoter, negative regulation of cell death,

Nucleus . Chromosome . Cytoplasm . Secreted . Cell membrane ; Peripheral membrane protein ; Extracellular side . Endosome . Endoplasmic reticulum-Golgi intermediate compartment . In basal state predominantly nuclear. Shuttles between the cytoplasm and the nucleus (PubMed:12231511, PubMed:17114460). Translocates from the nucleus to the cytoplasm upon autophagy stimulation (PubMed:20819940). Release from macrophages in the extracellular milieu requires the activation of NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the extracellular milieu from necrotic cells by diffusion, involving the fully reduced HGMB1 which subsequently gets oxidized (PubMed:19811284). Also released from apoptotic cells (PubMed:16855214, PubMed:18631454). Active secretion from a variety of immune and non-immune cells such as macrophages, monocytes, neutrophils, dendritic cells and natural killer cells in response to various stimuli such as LPS and cytokines involves a nonconventional secretory process via secretory lysosomes (PubMed:12231511, PubMed:14532127, PubMed:15944249). Secreted by plasma cells in response to LPS (By similarity). Found on the surface of activated platelets (PubMed:11154118). An increased chromatin association is observed when associated with the adenovirus protein pVII (PubMed:27362237). .

>>Base excision repair ;
>>Autophagy - animal ;
>>Necroptosis ;
>>Neutrophil extracellular trap formation