Anti-Human/Mouse HDAC2 (Clone 3f3) – Purified No Carrier Protein

KLH-conjugated, synthetic peptide corresponding to the carboxy terminus of human HDAC2, amino acids 473-488

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.

Liquid

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.

This antibody may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.

Research Use Only

2 – 8° C Wet Ice

3F3 activity is directed against human and mouse HDAC2.

Histone modifications are essential to cellular differentiation and proliferation throughout growth and development¹. Histone deacetylases induce changes in chromatin structure that enable epigenetic control and modulation of gene expression patterns. Histone deacetylase 2 (HDAC2) is a class I histone deacetylase that, along with HDAC1, regulates gene expression as part of a corepressor complex. HDAC2 catalyzes the deacetylation of lysine residues on the N-terminus of core histones H2A, H2B, H3 and H4². HDAC2 can also perform noncatalytic activities¹. Additionally, HDAC2 associates with F-actin in mitotic cells³. HDAC inhibitors are being investigated for the treatment of neurological diseases and cancer¹.

3F3 was generated by immunizing mice with a KLH-conjugated, synthetic peptide corresponding to the carboxy terminus of human HDAC2, amino acids 473-488.

HDAC2 is widely expressed, with lower levels present in the brain and lung.

HDAC1, MAD, SIN3, YY1, N-COR, RBBP4, RBBP7, among many others

Human: Q92769
Mouse: P70288

1 Hagelkruys A, Mattes K, Moos V, et al. Mol Cell Biol. 36(3):462-474. 2015.
2 https://www.uniprot.org/uniprotkb/Q92769/entry
3 He S, Khan DH, Winter S, et al. J Cell Physiol. 228(7):1525-1535. 2013.
4 Li P, Wang D, Yao H, et al. Oncogene. 29(21):3153-3162. 2010.
5 Hagelkruys A, Lagger S, Krahmer J, et al. Development. 141(3):604-616. 2014.
6 Huang Y, Tang Q, Nguyen M, et al. Virol J. 8:151. 2011.
7 Preglej T, Hamminger P, Luu M, et al. JCI Insight. 5(4):e133393. 2020.
8 Kiweler N, Schwarz H, Nguyen A, et al. Cell Biol Toxicol. 39(5):2401-2419. 2023.