Anti-Human HDAC3 [Clone 3G6] – Purified No Carrier Protein

This monoclonal antibody was raised against a peptide sequence derived from the C-terminus of the human HDAC3 protein.

This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added.

Purified antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

Anti-Human HDAC3

Histone deacetylase 3 (HDAC3) is a 49kDa enzyme that removes acetyl groups from both histone and non-histone proteins, playing roles in gene expression and other key cellular processes. When HDAC3 removes acetyl groups from histones, the DNA in that region becomes more condensed, restricting access for transcription machinery and thereby suppressing gene transcription (1,2). HDAC3 also regulates cell cycle progression, cell proliferation, DNA repair, and apoptosis (3,4).

Ongoing research has suggested roles for HDAC3 in numerous diseases, including Alzheimer’s disease and cancer (1,3). In particular, HDAC3 has been shown to be a critical epigenetic regulator of immune evasion and tumor progression; multiple HDAC inhibitors have been approved for use in treatment of various lymphomas and multiple myeloma (1).

The hybridoma 3G6 was developed against a synthetic peptide corresponding to amino acids 411-428 of human HDAC3. 3G6 has been used in WB, IP, IF, and IHC applications.

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1. Han, R., Luo, Y., Gao, J., Zhou, H., Wang, Y., Chen, J., Zheng, G., & Ling, C. (2025). HDAC3: A Multifaceted Modulator in Immunotherapy Sensitization. Vaccines, 13(2), 182.

2. Yeo, D., Zars Fisher, E. L., Khosla, S., Farr, J. N., & Westendorf, J. J. (2024). Hdac3-deficiency increases senescence-associated distention of satellite DNA and telomere-associated foci in osteoprogenitor cells. Journal of Bone and Mineral Research, 39(7), 994-1007.

3. Zhang, X., Ozawa, Y., Lee, H., Wen, Y. D., Tan, T. H., Wadzinski, B. E., & Seto, E. (2005). Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes & development, 19(7), 827–839.

4. Nishimoto, K., Niida, H., Uchida, C., Ohhata, T., Kitagawa, K., Motegi, A., ... & Kitagawa, M. (2020). HDAC3 is required for XPC recruitment and nucleotide excision repair of DNA damage induced by UV irradiation. Molecular Cancer Research, 18(9), 1367-1378.