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Mouse Anti-HDAC3 (AA 411-428) Recombinant Antibody (CBFYH-0848) (CBMAB-H0780-FY)

This product is mouse antibody that recognizes HDAC3. The antibody CBFYH-0848 can be used for immunoassay techniques such as: WB, IP, ICC, IF.
See all HDAC3 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
CBFYH-0848
Antibody Isotype
IgG2a
Application
WB, IP, ICC, IF

Basic Information

Immunogen
Human C-terminal peptide
Specificity
Human, Mouse
Antibody Isotype
IgG2a
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
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 411-428

Target

Full Name
Histone Deacetylase 3
Introduction
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. This protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. This gene is regarded as a potential tumor suppressor gene.
Entrez Gene ID
Human8841
Mouse15183
UniProt ID
HumanO15379
MouseO88895
Alternative Names
Histone Deacetylase 3; EC 3.5.1.98; RPD3-2; SMAP45; HD3; RPD3
Function
Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:23911289, PubMed:21030595, PubMed:21444723, PubMed:25301942, PubMed:28497810, PubMed:28167758).

Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:23911289).

Histone deacetylases act via the formation of large multiprotein complexes (PubMed:23911289).

Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression (PubMed:23911289).

Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (By similarity).

Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI3K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803).

Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner (By similarity).

During the activation phase, promotes the accumulation of ubiquitinated ARNTL/BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and ARNTL/BMAL1 (By similarity).

The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity).

Also functions as deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14 and RARA (PubMed:21030595, PubMed:21444723, PubMed:25301942, PubMed:28167758).

Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding (PubMed:28167758).

In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758).

In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:34608293).

Catalyzes decrotonylation of MAPRE1/EB1 (PubMed:34608293).
Biological Process
Cellular response to fluid shear stress Source: UniProtKB
Chromatin organization Source: UniProtKB
Circadian regulation of gene expression Source: UniProtKB
Histone H3 deacetylation Source: GO_Central
Histone H4 deacetylation Source: GO_Central
Negative regulation of apoptotic process Source: ProtInc
Negative regulation of JNK cascade Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of cold-induced thermogenesis Source: YuBioLab
Positive regulation of protein import into nucleus Source: UniProtKB
Positive regulation of protein phosphorylation Source: UniProtKB
Positive regulation of protein ubiquitination Source: UniProtKB
Positive regulation of TOR signaling Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Protein deacetylation Source: UniProtKB
Regulation of circadian rhythm Source: UniProtKB
Regulation of protein stability Source: UniProtKB
Spindle assembly Source: UniProtKB
Cellular Location
Cytoplasm; Cytosol; Nucleus. Colocalizes with XBP1 and AKT1 in the cytoplasm (PubMed:25190803). Predominantly expressed in the nucleus in the presence of CCAR2 (PubMed:21030595).
PTM
Sumoylated in vitro.

He, R., Liu, B., Geng, B., Li, N., & Geng, Q. (2023). The role of HDAC3 and its inhibitors in regulation of oxidative stress and chronic diseases. Cell Death Discovery, 9(1), 131.

Eshleman, E. M., Shao, T. Y., Woo, V., Rice, T., Engleman, L., Didriksen, B. J., ... & Alenghat, T. (2023). Intestinal epithelial HDAC3 and MHC class II coordinate microbiota-specific immunity. The Journal of Clinical Investigation, 133(4).

Li, W., Kou, J., Qin, J., Li, L., Zhang, Z., Pan, Y., ... & Du, W. (2021). NADPH levels affect cellular epigenetic state by inhibiting HDAC3–Ncor complex. Nature Metabolism, 3(1), 75-89.

Wu, S. E., Hashimoto-Hill, S., Woo, V., Eshleman, E. M., Whitt, J., Engleman, L., ... & Alenghat, T. (2020). Microbiota-derived metabolite promotes HDAC3 activity in the gut. Nature, 586(7827), 108-112.

Nguyen, H. C., Adlanmerini, M., Hauck, A. K., & Lazar, M. A. (2020). Dichotomous engagement of HDAC3 activity governs inflammatory responses. Nature, 584(7820), 286-290.

Kim, T. H., Yoo, J. Y., Choi, K. C., Shin, J. H., Leach, R. E., Fazleabas, A. T., ... & Jeong, J. W. (2019). Loss of HDAC3 results in nonreceptive endometrium and female infertility. Science translational medicine, 11(474), eaaf7533.

Ji, H., Zhou, Y., Zhuang, X., Zhu, Y., Wu, Z., Lu, Y., ... & Bu, H. (2019). HDAC3 deficiency promotes liver cancer through a defect in H3K9ac/H3K9me3 transition. Cancer research, 79(14), 3676-3688.

Janczura, K. J., Volmar, C. H., Sartor, G. C., Rao, S. J., Ricciardi, N. R., Lambert, G., ... & Wahlestedt, C. (2018). Inhibition of HDAC3 reverses Alzheimer’s disease-related pathologies in vitro and in the 3xTg-AD mouse model. Proceedings of the National Academy of Sciences, 115(47), E11148-E11157.

Adhikari, N., Amin, S. A., Trivedi, P., Jha, T., & Ghosh, B. (2018). HDAC3 is a potential validated target for cancer: An overview on the benzamide-based selective HDAC3 inhibitors through comparative SAR/QSAR/QAAR approaches. European journal of medicinal chemistry, 157, 1127-1142.

Whitt, J., Woo, V., Lee, P., Moncivaiz, J., Haberman, Y., Denson, L., ... & Alenghat, T. (2018). Disruption of epithelial HDAC3 in intestine prevents diet-induced obesity in mice. Gastroenterology, 155(2), 501-513.

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

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