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Rabbit Anti-HMGB2 Recombinant Antibody (D1P9V) (CBMAB-H2501-FY)

This product is rabbit antibody that recognizes HMGB2. The antibody D1P9V can be used for immunoassay techniques such as: WB.
See all HMGB2 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat, Monkey, Hamster, Cattle, Dog, Guinea pig, Horse
Clone
D1P9V
Application
WB

Basic Information

Specificity
Human, Mouse, Rat, Monkey, Hamster, Cattle, Dog, Guinea pig, Horse
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
high mobility group box 2
Introduction
This gene encodes a member of the non-histone chromosomal high mobility group protein family. The proteins of this family are chromatin-associated and ubiquitously distributed in the nucleus of higher eukaryotic cells. In vitro studies have demonstrated that this protein is able to efficiently bend DNA and form DNA circles. These studies suggest a role in facilitating cooperative interactions between cis-acting proteins by promoting DNA flexibility. This protein was also reported to be involved in the final ligation step in DNA end-joining processes of DNA double-strand breaks repair and V(D)J recombination.
Entrez Gene ID
Human3148
Mouse97165
Rat29395
Monkey697057
Cattle540444
Hamster101831500
Dog486068
Guinea pig100727388
Horse100061162
UniProt ID
HumanP26583
MouseP30681
RatP52925
MonkeyH9EQP8
CattleP40673
HamsterA0A1U7QXL1
DogE2QY30
Guinea pigH0V150
HorseF6R5B2
Alternative Names
High Mobility Group Box 2; High-Mobility Group (Nonhistone Chromosomal) Protein 2; High Mobility Group Protein 2; HMG-2; HMG2; High Mobility Group Protein B2; High-Mobility Group Box 2
Function
Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (PubMed:7797075, PubMed:11909973, PubMed:19522541, PubMed:18413230, PubMed:19965638, PubMed:20123072).

Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity).

Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (By similarity).

In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (PubMed:19811285).

Has antimicrobial activity in gastrointestinal epithelial tissues (PubMed:23877675).

Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity (By similarity).

Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (By similarity).

Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (By similarity).
Biological Process
Cell chemotaxis Source: UniProtKB
Cellular response to lipopolysaccharide Source: UniProtKB
Chromatin organization Source: UniProtKB
Defense response to Gram-negative bacterium Source: AgBase
Defense response to Gram-positive bacterium Source: AgBase
DNA geometric change Source: AgBase
DNA topological change Source: UniProtKB
Double-strand break repair via nonhomologous end joining Source: UniProtKB
Inflammatory response to antigenic stimulus Source: AgBase
Innate immune response Source: UniProtKB-KW
Male gonad development Source: Ensembl
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
Negative regulation of gene expression Source: Ensembl
Negative regulation of transcription, DNA-templated Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Nucleosome assembly Source: UniProtKB
Positive regulation of DNA binding Source: UniProtKB
Positive regulation of endothelial cell proliferation Source: UniProtKB
Positive regulation of erythrocyte differentiation Source: UniProtKB
Positive regulation of innate immune response Source: Ensembl
Positive regulation of interferon-beta production Source: Ensembl
Positive regulation of megakaryocyte differentiation Source: UniProtKB
Positive regulation of nuclease activity Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of neurogenesis Source: AgBase
Regulation of stem cell proliferation Source: AgBase
Regulation of transcription by RNA polymerase II Source: UniProtKB
Response to lipopolysaccharide Source: AgBase
Response to steroid hormone Source: Ensembl
Spermatid nucleus differentiation Source: Ensembl
V(D)J recombination Source: UniProtKB
Cellular Location
Secreted; Nucleus; Cytoplasm; Chromosome. In basal state predominantly nuclear.
PTM
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
Acetylation enhances nucleosome binding and chromation remodeling activity.

Wang, Y., Yang, Y., Zhang, T., Jia, S., Ma, X., Zhang, M., ... & Ma, A. (2022). LncRNA SNHG16 accelerates atherosclerosis and promotes ox-LDL-induced VSMC growth via the miRNA-22–3p/HMGB2 axis. European Journal of Pharmacology, 915, 174601.

Wang, F., Luo, Y., Zhang, L., Younis, M., & Yuan, L. (2022). The LncRNA RP11-301G19. 1/miR-582-5p/HMGB2 axis modulates the proliferation and apoptosis of multiple myeloma cancer cells via the PI3K/AKT signalling pathway. Cancer gene therapy, 29(3-4), 292-303.

Yano, K., Choijookhuu, N., Ikenoue, M., Fidya, Fukaya, T., Sato, K., ... & Hishikawa, Y. (2022). Spatiotemporal expression of HMGB2 regulates cell proliferation and hepatocyte size during liver regeneration. Scientific Reports, 12(1), 11962.

Pu, J., Tan, C., Shao, Z., Wu, X., Zhang, Y., Xu, Z., ... & Wei, H. (2020). Long noncoding RNA PART1 promotes hepatocellular carcinoma progression via targeting miR-590-3p/HMGB2 axis. OncoTargets and therapy, 9203-9211.

Zhang, X., Dang, Y., Liu, R., Zhao, S., Ma, J., & Qin, Y. (2020). MicroRNA‐127‐5p impairs function of granulosa cells via HMGB2 gene in premature ovarian insufficiency. Journal of Cellular Physiology, 235(11), 8826-8838.

Fang, J., Ge, X., Xu, W., Xie, J., Qin, Z., Shi, L., ... & Wang, H. (2020). Bioinformatics analysis of the prognosis and biological significance of HMGB1, HMGB2, and HMGB3 in gastric cancer. Journal of cellular physiology, 235(4), 3438-3446.

Cui, G., Cai, F., Ding, Z., & Gao, L. (2019). HMGB2 promotes the malignancy of human gastric cancer and indicates poor survival outcome. Human pathology, 84, 133-141.

Han, Q., Xu, L., Lin, W., Yao, X., Jiang, M., Zhou, R., ... & Zhao, L. (2019). Long noncoding RNA CRCMSL suppresses tumor invasive and metastasis in colorectal carcinoma through nucleocytoplasmic shuttling of HMGB2. Oncogene, 38(16), 3019-3032.

Fu, D., Li, J., Wei, J., Zhang, Z., Luo, Y., Tan, H., & Ren, C. (2018). HMGB2 is associated with malignancy and regulates Warburg effect by targeting LDHB and FBP1 in breast cancer. Cell Communication and Signaling, 16, 1-10.

Zirkel, A., Nikolic, M., Sofiadis, K., Mallm, J. P., Brackley, C. A., Gothe, H., ... & Papantonis, A. (2018). HMGB2 loss upon senescence entry disrupts genomic organization and induces CTCF clustering across cell types. Molecular cell, 70(4), 730-744.

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For research use only. Not intended for any clinical use.

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