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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
lyophilized powder
Assay:
≥95% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in HEK 293 cells
Mol wt:
calculated mol wt 25.7 kDa, observed mol wt 28 kDa (DTT-reduced. Protein migrates due to glycosylation. Phe17 is the predicted N-terminus.), observed mol wt 32 kDa
biological source
human
recombinant
expressed in HEK 293 cells
tag
6-His tagged (C-terminus)
assay
≥95% (SDS-PAGE)
form
lyophilized powder
potency
0.22 μg/mL
mol wt
calculated mol wt 25.7 kDa, observed mol wt 28 kDa (DTT-reduced. Protein migrates due to glycosylation. Phe17 is the predicted N-terminus.), observed mol wt 32 kDa
packaging
pkg of 10 μg
impurities
<1 EU/μg endotoxin (LAL test)
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... HMGB1(3146)
General description
High-mobility group protein B1 (HMGB1), also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a member of the HMGB family consisting of three members, HMGB1, HMGB2 and HMGB3. HMGB1 is a non-histone architectural chromosomal protein ubiquitously present in all vertebrate nuclei and binds double-stranded DNA without sequence specificity. However, it can shuttle between the nucleus and cytoplasm. The protein is secreted by activated monocytes and macrophages. HMGB1 is from the high mobility group protein super family. The gene is mapped to human chromosome 13q12.
Application
HMGB1 (high-mobility group protein B1) has been used to identify factors masking HMGB1 in human serum and plasma. It has been used to study HMGB1-mediated growth and motility in papillary thyroid cancer cells.
HMGB1/HMG1 human has been used as a positive control to analyse the expression of purified HMGB1 gene.
Biochem/physiol Actions
In the nucleus, HMGB1 (high-mobility group protein B1) works as a nucleosome stabilizer and transcriptional regulator. It also exhibits chaperone-like activity and suppresses aggregation of polyglutamine. It is also involved in inflammation and autophagy. HMGB1 can interacts with toll-like receptor (TLR) 2 and 4, interleukin-1β, chemokine (C-X-C motif) ligand 12 (CXCL12) and pathogen-associated molecular pattern (PAMP) molecules. It also works as a damage-associated molecular pattern molecule (DAMP). The mechanism of inflammation and damage is binding to TLR4, which mediates HMGB1-dependent activation of macrophage cytokine release. This positions HMGB1 at the intersection of sterile and infectious inflammatory responses. HMGB1 has been studied as a DNA vaccine adjuvant and a target for cancer therapy. In presence of Epstein-Barr virus (EBV) infection, HMGB1 is upregulated and is responsible for the proliferation of human nasopharyngeal carcinoma cells. It is involved in cancer cell migration and invasion.
Physical form
Lyophilized from 0.22 μm filtered solution in PBS. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Preparation Note
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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MiR-142-3p functions as a potential tumor suppressor directly targeting HMGB1 in non-small-cell lung carcinoma.
Xiao P and Liu WL
International Journal of Clinical and Experimental Pathology, 8, 10800-10807 (2015)
Molecular adjuvant HMGB1 enhances anti-influenza immunity during DNA vaccination.
Fagone P
Gene Therapy, 18, 1070-1077 (2011)
High mobility group box 1 (HMGB1) is upregulated by the Epstein-Barr virus infection and promotes the proliferation of human nasopharyngeal carcinoma cells.
Zhu X
Acta Oto-Laryngologica, 136, 87-94 (2016)
N-linked glycosylation plays a crucial role in the secretion of HMGB1.
Kim YH
Journal of Cell Science, 129, 29-38 (2016)
Factors masking HMGB1 in human serum and plasma.
Urbonaviciute V
Journal of Leukocyte Biology, 81, 67-74 (2007)
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