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- Table of Contents
Facts about High mobility group protein B2.
From the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and likely other processes. Binds DNA with a preference to non-canonical DNA structures like single-stranded DNA.
Human | |
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Gene Name: | HMGB2 |
Uniprot: | P26583 |
Entrez: | 3148 |
Belongs to: |
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HMGB family |
High mobility group protein 2; high mobility group protein B2; high-mobility group box 2; HMG-2; HMG2high-mobility group (nonhistone chromosomal) protein 2
Mass (kDA):
24.034 kDA
Human | |
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Location: | 4q34.1 |
Sequence: | 4; NC_000004.12 (173331376..173334358, complement) |
Expressed in gastric and intestinal tissues (at protein level).
Nucleus. Chromosome. Cytoplasm. Secreted. In basal state predominantly nuclear.
The HMGB2 marker is found in many biological samples and is used in many biochemical assays. There are many biological assays using HMGB2 and antibodies are a common method for detecting it. Boster Bio produces antibodies against HMGB2 from rabbits and mice. Whether you are looking for a specific antibody for research purposes or simply want a specific protein in your samples, the HMGB2 marker will help you do just that.
Human HMGB2 is a glycoprotein found in the blood of many species. In biological assays, it is detected by antibodies, either polyclonal or monoclonal. Boster Bio develops antibodies for this molecule using rabbit and mouse samples. The HMGB2 protein is expressed in many body tissues, including the heart. Here are the best uses of HMGB2.
High Mobility Group Box Proteins, or HMGBs, are a family of nonhistone proteins. These proteins are found in all higher animals and show remarkable conservation in their primary structures. These proteins are present in both the nuclei and cytoplasm. However, their biological roles are still unclear. HMGBs are thought to play an important role in DNA replication and transcription.
In addition, the present inventors studied the high-titer antibody derived from human HMGB1. They used birds as immune animals, and a peptide containing a particular amino acid sequence as the immunogen. Their method was also patent-pending. The present inventors have made these antibodies available for research in the field of cancer immunology. This antibody is the first of its kind to have human HMGB1 homology.
HMGB2 is a protein found in human blood. In cancer and other diseases, it has a role in the formation of angiogenesis and has anti-inflammatory properties. It is also an important marker for ovarian cancer. It is a highly sensitive diagnostic. It has many applications and can be used to detect cancer in humans and animals. If you are looking for a good anti-HMG2 antibody, it is time to check out Boster Bio.
Anti-human HMGB1 antibody is not a trivial task. It must have high binding capacity to human HMGB1. This antibody is generally obtained through an injection of the substance to be measured. However, the probability of obtaining a high-titer antibody is extremely low. Therefore, it is important to use anti-human HMGB1 antibody. The best use of anti-human HMGB1 antibody in research is in the field of cancer immunology.
HMGB-proteins are a family of small proteins that bind DNA. HMGB1-2 and -3 are expressed in eukaryotes and are highly conserved between species. They contain two HMGB-boxes, a sequence of amino acids that binds DNA, and an acidic tail. The HMGB4 protein is different from the other HMGB-proteins, lacking the acidic tail.
HMGB4 regulates the expression of over 800 genes in HEK 293T cells. HMGB4 is also associated with adhesion and histone H2A-processes. This protein is important in neuronal differentiation, where it inhibits the activity of other proteins. Furthermore, HMGB4 regulates the expression of several genes, including oligodendrocyte marker PPP1R14a.
The HMGB4L1 marker interacts with histone H2A and toposomerase II. It is a potential target for drug development, a biomarker for lung cancer, and an alternative marker for CLL. However, this marker is not yet available for routine research in cancer. Its best uses will be determined after it has been studied. This research will help in the development of more effective drugs and a more accurate diagnosis.
The HMGB4L1 protein has a polymorphic nature, and the polymorph rs10379 is a prominent marker of this gene. To detect this polymorphism, NIH-3T3 cells were transfected with expression vectors. The resulting HMGB4-EGFP fusion proteins were bleached with laser pulses, and fluorescence was measured. Failure to recover full fluorescent means that a portion of the HMGB4-EGFP is immobile in the nucleus.
Several studies have reported that HMGB4L1 promotes neuronal development in adult mice. In addition to brain and spinal cord cancer, it is also important for analyzing fetal kidney development and repair. Interestingly, the marker is expressed in neurons in many types of tumors, including glioma, gliomas, and testicular stem cells. A recent study from the University of Helsinki has revealed that the HMGB4L1 gene is involved in the development of neuronal tissues.
HMGB1b-Beclin 1 autophagy pathway is regulated by HSP70 and HMGB1b. Overexpression of these two proteins increased the levels of Beclin 1 protein. Knockdown of these proteins inhibited the expression of Beclin 1, synergistically restraining their expression. Inhibitors of HSP70, VER-155008, inhibit the interaction of Beclin 1 with HMGB1b.
Beclin1 overexpression inhibited cell proliferation, reducing Bcl-2 protein expression levels and promoting caspase-3 and PARP expression, but had no effect on the expression of Bax. Beclin1 overexpression decreased cell viability and was associated with a reduced mean clone diameter. However, the number of clones formed remained unaffected.
During the initiation of autophagy, HMGB1b-Beclin 1 interacts with Bcl-2, a protein that regulates autophagy. HMGB1b-Beclin 1 interaction is induced by H2O2-treatment and increased with overexpression of HSP70. VER-155008 inhibits the association of HMGB1b with Beclin 1, suggesting that HSP70 and Beclin 1 may be involved in the association.
HMGB1b-Beclin 1 interactions have been reported in mice. HMGB1b-Beclin 1 interaction is regulated by HSP70 and the PI3K/Akt signaling pathways. The results of this study suggest that HMGB1b-Beclin 1 interaction is necessary for apoptosis in breast cancer cells. This interaction may help understand the process of autophagy and its role in mammary tumor development and resistance.
Activated GPR30 is an important regulatory protein in cancer cells. This protein promotes autophagy in cancer cells by inhibiting ERK/MAPK signaling. This interaction may be a crucial link in breast cancer progression. The implication of this study is that GPR30 is important in the regulation of autophagy. But HMGB1b is crucial for the development of anticancer drugs.
HMGB4 is a transcriptional repressor, highly expressed in adult mouse testis but not in brain or other tissues. Its distribution in human tissues is unknown. This study reports the development of a specific anti-hHMGB4 polyclonal antibody. We have characterized the antibody by ELISA, western blotting, and immunohistochemical techniques. We also used it to evaluate the expression level of HMGB4 in Boster Bio cells.
HMGB4 expression levels in Boster Bio cells are highly variable. It is important to note that HMGB4 expression is low in the stroma of boster bio cells. This may reflect low levels of expression. However, overexpression of this protein can increase the activity of the pPtaLHY2/3 reporter at the cytoplasmic membrane, allowing the mRNA to reach the right levels.
Interestingly, the HMGB4-EGFP protein modulates the expression of about 800 genes. HMGB4-EGFP also induced the expression of several histone variants. H2a and H2b were most affected, while HMGB1 and HMGB4L1 showed only a mild effect. In addition, HMGB4-EGFP inhibits the translation of PPP1R14a.
In addition to its role in tumorigenesis, HMGB3 has been associated with carcinogenic effects. Depletion of HMGB3 in ovarian cancer cells results in cisplatin resistance. While this is promising, further studies are needed to determine its role in NB. If the protein does have a role in the progression of tumors, it may represent an important new target for treatment.
The mechanism of HMGB4 gene regulation remains unclear. The active histone methylation mark of HMGB4 promoter is present in haploid sperm cells. However, HMGB4 and HMGB4L1 are not co-expressed in boster bio cells. However, they are still involved in the regulation of the expression of histones in transformed cells. And HMGB1 and HMGB4L1 play a crucial role in post-translational modification of histones.
Compared to other members of the HMGB-family, HMGB4 regulates gene expression in a variety of different ways, including by regulating transcription and histone variants. Interestingly, this protein also regulates the expression of over 800 genes, including those involved in neuronal differentiation and oligodendrocyte formation. Moreover, HMGB4 expression correlated with gene expression levels of a variety of cellular types, including glial cells.
The pET28a cell line was used to produce polyclonal antibodies against human HMGB4 and express a fusion protein containing full-length HMGB4 with His6-tags and thrombin at the terminal. HMGB4-FLAG-tagged fusion proteins were identified as hHMGB4 by MS/MS analysis. Further studies are planned to examine the mechanisms involved in HMGB4 regulation in Boster Bio.
The plasmid pBluescriptR/hHMGB4 was used to produce the recombinant pET28a expression vector for expressing hHMGB4. The recombinant plasmid was digested with EcoRI and SalI and transformed into hybrid poplar cells. To examine the resulting pET28a/hHMGB4 construct, BL21 cells were transduced with binary plasmid carrying pUPD.
hHMGB4 is an important part of the immune system, and antibodies that recognize it are necessary to combat the disease. The antibodies to HMGB4 and HMGB4L1 may help researchers understand how to regulate the activity of these proteins. They may also be useful as reagents for functional studies of the molecule. If you have an anti-hHMGB4 antibody, it is worth considering purchasing it to further investigate how it regulates histones.
HMGB4 is expressed in a very restricted number of tissues. Most notably, it is highly expressed in the testes and decidual tissue of adult mice. However, despite its limited expression in uterine and prostate tissue, the protein's location remains unknown. This study reports the development of a specific anti-hHMGB4 polyclonal antibody to detect hHMGB4. This antibody was characterized by immunohistochemical techniques and ELISA.
PMID: 1754403 by Majumdar A., et al. Sequence of human HMG2 cDNA.
PMID: 1551873 by Shirakawa H., et al. Structure of a gene coding for human HMG2 protein.