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Mouse Anti-HDAC3 Recombinant Antibody (7G6-C5-D8) (CBMAB-Z0340-LY)

The product is antibody recognizes HDAC3. The antibody 7G6-C5-D8 immunoassay techniques such as: WB, ICC, IP.
See all HDAC3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
7G6-C5-D8
Antibody Isotype
IgG2a
Application
WB, ICC, IP

Basic Information

Immunogen
Purified recombinant fragment of human HDAC3 (aa224-428) expressed in E. Coli.
Specificity
Human
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
Buffer
Ascitic fluid containing 0.03% sodium azide.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Histone Deacetylase 3
Entrez Gene ID
8841
UniProt ID
O15379
Alternative Names
HD3; RPD3; RPD3-2
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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