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Mouse Anti-DNMT3B Recombinant Antibody (15B83) (CBMAB-D1428-YC)

Provided herein is a Mouse monoclonal antibody, which binds to DNA Methyltransferase 3 Beta (DNMT3B). The antibody can be used for immunoassay techniques, such as ICC, IF, IHC-Fr, IP, WB.
See all DNMT3B antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
15B83
Antibody Isotype
IgG
Application
ICC, IF, IHC-Fr, IP, WB

Basic Information

Immunogen
Recombinant protein corresponding to mouse DNMT3b, expressed in bacteria
Specificity
Human, Mouse
Antibody Isotype
IgG
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!]

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
DNA Methyltransferase 3 Beta
Introduction
DNMT3B is a DNA methyltransferase which is thought to function in de novo methylation, rather than maintenance methylation. DNMT3B localizes primarily to the nucleus and its expression is developmentally regulated. Mutations in DNMT3B cause the immunodeficiency-centromeric instability-facial anomalies (ICF) syndrome.
Entrez Gene ID
Human1789
Mouse13436
UniProt ID
HumanQ9UBC3
MouseO88509
Alternative Names
DNA Methyltransferase 3 Beta; DNA (Cytosine-5-)-Methyltransferase 3 Beta; DNA Methyltransferase HsaIIIB; DNA MTase HsaIIIB; EC 2.1.1.37; M.HsaIIIB;
Function
Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity).

In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Functions as a transcriptional corepressor by associating with ZHX1. Required for DUX4 silencing in somatic cells (PubMed:27153398).
Biological Process
Cellular response to dexamethasone stimulus Source: Ensembl
Cellular response to hyperoxia Source: Ensembl
DNA methylation Source: UniProtKB
Negative regulation of histone H3-K9 methylation Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of gene expression Source: UniProtKB
Positive regulation of histone H3-K4 methylation Source: UniProtKB
Positive regulation of neuron differentiation Source: Ensembl
Response to activity Source: Ensembl
Response to caffeine Source: Ensembl
Response to cocaine Source: Ensembl
Response to drug Source: Ensembl
Response to estradiol Source: Ensembl
Response to hypoxia Source: Ensembl
Response to ionizing radiation Source: Ensembl
Response to toxic substance Source: Ensembl
Response to vitamin A Source: Ensembl
Cellular Location
Nucleus
Involvement in disease
Immunodeficiency-centromeric instability-facial anomalies syndrome 1 (ICF1):
A rare disorder characterized by a variable immunodeficiency resulting in recurrent infections, facial anomalies, and branching of chromosomes 1, 9, and 16. Other variable symptoms include growth retardation, failure to thrive, and psychomotor retardation. Laboratory studies show limited hypomethylation of DNA in a small fraction of the genome in some, but not all, patients.
Facioscapulohumeral muscular dystrophy 2 (FSHD2):
The gene represented in this entry may act as a disease modifier. DNMT3B mutations lead to DUX4 expression in somatic tissues, including muscle cells, when an haplotype on chromosome 4 is permissive for DUX4 expression. Ectopic expression of DUX4 in skeletal muscle activates the expression of stem cell and germline genes, and, when overexpressed in somatic cells, DUX4 can ultimately lead to cell death. A degenerative muscle disease characterized by slowly progressive weakness of the muscles of the face, upper-arm, and shoulder girdle. The onset of symptoms usually occurs in the first or second decade of life. Affected individuals usually present with impairment of upper extremity elevation. This tends to be followed by facial weakness, primarily involving the orbicularis oris and orbicularis oculi muscles.
PTM
Sumoylated.
Citrullinated by PADI4.

Zhu, L., Jia, L., Liu, N., Wu, R., Guan, G., Hui, R., ... & Wang, J. (2022). DNA Methyltransferase 3b Accelerates the Process of Atherosclerosis. Oxidative medicine and cellular longevity, 2022.

Qin, W., Brands, X., Van’t Veer, C., F. de Vos, A., Sirard, J. C., JTH Roelofs, J., ... & Van Der Poll, T. (2021). Bronchial epithelial DNA methyltransferase 3b dampens pulmonary immune responses during Pseudomonas aeruginosa infection. PLoS pathogens, 17(4), e1009491.

Yan, Y., He, Y. Y., Jiang, X., Wang, Y., Chen, J. W., Zhao, J. H., ... & Jing, Z. C. (2020). DNA methyltransferase 3B deficiency unveils a new pathological mechanism of pulmonary hypertension. Science Advances, 6(50), eaba2470.

Lin, C. C., Chen, Y. P., Yang, W. Z., Shen, J. C., & Yuan, H. S. (2020). Structural insights into CpG-specific DNA methylation by human DNA methyltransferase 3B. Nucleic acids research, 48(7), 3949-3961.

Iguchi, E., Takai, A., Takeda, H., Kumagai, K., Arasawa, S., Eso, Y., ... & Seno, H. (2020). DNA methyltransferase 3B plays a protective role against hepatocarcinogenesis caused by chronic inflammation via maintaining mitochondrial homeostasis. Scientific reports, 10(1), 1-15.

Su, J. F., Zhao, F., Gao, Z. W., Hou, Y. J., Li, Y. Y., Duan, L. J., ... & Zhou, F. Y. (2020). piR-823 demonstrates tumor oncogenic activity in esophageal squamous cell carcinoma through DNA methylation induction via DNA methyltransferase 3B. Pathology-Research and Practice, 216(4), 152848.

Shiah, S. G., Hsiao, J. R., Chang, H. J., Hsu, Y. M., Wu, G. H., Peng, H. Y., ... & Chang, J. Y. (2020). MiR-30a and miR-379 modulate retinoic acid pathway by targeting DNA methyltransferase 3B in oral cancer. Journal of biomedical science, 27(1), 1-13.

Zo, R. B., & Long, Z. (2019). MiR‐124‐3p suppresses bladder cancer by targeting DNA methyltransferase 3B. Journal of cellular physiology, 234(1), 464-474.

Shen, J., Wang, C., Li, D., Xu, T., Myers, J., Ashton, J. M., ... & O’Keefe, R. J. (2017). DNA methyltransferase 3b regulates articular cartilage homeostasis by altering metabolism. JCI insight, 2(12).

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

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