Anti-Human/Mouse HDAC1 (Clone 10E2) – Purified No Carrier Protein

N/A

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

10E2 activity is directed against human and mouse HDAC1.

HDAC1 is a histone deacetylase that plays an important role in transcriptional regulation, cell cycle progression, and development¹ as well as regulates major endothelial functions such as angiogenesis, inflammatory signalling, redox homeostasis, and nitric oxide signalling². As part of a large multiprotein complex, HDAC1 deacetylates lysine residues on the N-terminal portion of core histones H2A, H2B, H3 and H4¹. In this capacity, HDAC1 is involved in chromatin remodelling, histone acetylation, and RNA polymerase II progression in transcribed regions. Additionally, HDAC1 deacetylates non-histone targets (NR1D2, RELA, SP1, SP3, STAT3, RELA, TSHZ3, SP proteins), and thereby regulates their function. HDAC1 is also required for repression of circadian genes (CLOCK-BMAL-1, PER1, and CRY1). Knockout of HDAC1 in mice causes impairment to cellular proliferation and death at embryonic day 9.5³.

HDAC1 expression is ubiquitous, with higher levels in heart, pancreas, and testis tissues. Levels are lower in kidney and brain. HDAC1 primarily localizes to the nucleus.

HDAC2, RBBP4, RBBP7, SIN3, SAP18, SAP30

Q13547
O09106

1 https://www.uniprot.org/uniprotkb/Q13547/entry
2 Dunaway LS, Pollock JS. Cardiovasc Res. 118(8):1885-1903. 2022.
3 Segré CV, Senese S, Loponte S, et al. MAbs. 8(1):37-42. 2016.
4 Hagelkruys A, Lagger S, Krahmer J, et al. Development. 141(3):604-616. 2014.
5 Vcelkova T, Reiter W, Zylka M, et al. Nucleic Acids Res. 51(21):11748-11769. 2023.
6 Torres HM, Fang F, May DG, et al. J Biol Chem. 300(1):105522. 2024.
7 Simões M, Rino J, Pinheiro I, et al. Viruses. 7(9):4978-4996. 2015.
8. Guantes R, Rastrojo A, Neves R, et al. Genome Res. 25(5):633-644. 2015.