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Mouse Anti-HDAC1 Recombinant Antibody (CAP882) (CBMAB-AP2683LY)


See all HDAC1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CAP882
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
A synthetic peptide of human HDAC1
Specificity
Human
Antibody Isotype
IgG
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
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 1
Introduction
Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis. [provided by RefSeq, Jul 2008]
Entrez Gene ID
3065
UniProt ID
Q13547
Alternative Names
Histone Deacetylase 1; EC 3.5.1.98; RPD3L1; HD1; Reduced Potassium Dependency, Yeast Homolog-Like 1; GON-10; 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) (PubMed:16762839, PubMed:17704056, PubMed:28497810).

Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:16762839, PubMed:17704056).

Histone deacetylases act via the formation of large multiprotein complexes (PubMed:16762839, PubMed:17704056).

Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3 (PubMed:12837748, PubMed:16478997, PubMed:17996965, PubMed:19343227).

Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed:12837748, PubMed:16478997).

Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed:19081374).

Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed:19081374).

Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed:19343227).

Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed:17000776).

Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed:17996965).

Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity).

Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer (By similarity).

Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity).

In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810).
Biological Process
Cellular response to platelet-derived growth factor stimulus Source: BHF-UCL
Chromatin organization Source: UniProtKB
Chromatin remodeling Source: ComplexPortal
Circadian regulation of gene expression Source: UniProtKB
DNA methylation-dependent heterochromatin assembly Source: BHF-UCL
Embryonic digit morphogenesis Source: BHF-UCL
Endoderm development Source: Ensembl
Epidermal cell differentiation Source: BHF-UCL
Eyelid development in camera-type eye Source: BHF-UCL
Fungiform papilla formation Source: BHF-UCL
Hair follicle placode formation Source: BHF-UCL
Hippocampus development Source: Ensembl
Histone deacetylation Source: ComplexPortal
Histone H3 deacetylation Source: BHF-UCL
Histone H4 deacetylation Source: BHF-UCL
Negative regulation by host of viral transcription Source: UniProtKB
Negative regulation of androgen receptor signaling pathway Source: BHF-UCL
Negative regulation of apoptotic process Source: BHF-UCL
Negative regulation of canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
Negative regulation of gene expression Source: CACAO
Negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
Negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Neuron differentiation Source: Ensembl
Odontogenesis of dentin-containing tooth Source: BHF-UCL
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of gene expression Source: BHF-UCL
Positive regulation of oligodendrocyte differentiation Source: Ensembl
Positive regulation of signaling receptor activity Source: BHF-UCL
Positive regulation of smooth muscle cell proliferation Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Protein deacetylation Source: UniProtKB
Regulation of amyloid-beta clearance Source: ARUK-UCL
Regulation of endopeptidase activity Source: ARUK-UCL
Regulation of transcription by RNA polymerase II Source: ARUK-UCL
Cellular Location
Nucleus
PTM
Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1.
Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.
Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by KCTD11, leading to proteasomal degradation.

Dunaway, L. S., & Pollock, J. S. (2022). HDAC1: an environmental sensor regulating endothelial function. Cardiovascular Research, 118(8), 1885-1903.

Bontempi, G., Terri, M., Garbo, S., Montaldo, C., Mariotti, D., Bordoni, V., ... & Strippoli, R. (2022). Restoration of WT1/miR-769-5p axis by HDAC1 inhibition promotes MMT reversal in mesenchymal-like mesothelial cells. Cell Death & Disease, 13(11), 965.

Zhang, L., Yu, Z., Qu, Q., Li, X., Lu, X., & Zhang, H. (2022). Exosomal lncRNA HOTAIR promotes the progression and angiogenesis of endometriosis via the miR-761/HDAC1 Axis and activation of STAT3-mediated inflammation. International journal of nanomedicine, 1155-1170.

Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., ... & Zhao, Y. (2022). Class I histone deacetylases (HDAC1–3) are histone lysine delactylases. Science advances, 8(3), eabi6696.

Nan, S., Wang, Y., Xu, C., & Wang, H. (2021). Interfering microRNA-410 attenuates atherosclerosis via the HDAC1/KLF5/IKBα/NF-κB axis. Molecular Therapy-Nucleic Acids, 24, 646-657.

Sun, J., Piao, J., Li, N., Yang, Y., Kim, K. Y., & Lin, Z. (2020). Valproic acid targets HDAC1/2 and HDAC1/PTEN/Akt signalling to inhibit cell proliferation via the induction of autophagy in gastric cancer. The FEBS Journal, 287(10), 2118-2133.

Kim, M. Y., Yan, B., Huang, S., & Qiu, Y. (2020). Regulating the regulators: the role of histone deacetylase 1 (HDAC1) in erythropoiesis. International journal of molecular sciences, 21(22), 8460.

Pao, P. C., Patnaik, D., Watson, L. A., Gao, F., Pan, L., Wang, J., ... & Tsai, L. H. (2020). HDAC1 modulates OGG1-initiated oxidative DNA damage repair in the aging brain and Alzheimer’s disease. Nature communications, 11(1), 2484.

Ohta, S., Morine, Y., Imura, S., Ikemoto, T., Arakawa, Y., Iwahashi, S., ... & Shimada, M. (2019). Carbohydrate antigen 19-9 is a prognostic factor which correlates with HDAC1 and HIF-1α for intrahepatic cholangiocarcinoma. Anticancer Research, 39(11), 6025-6033.

Wang, S., Ge, W., Harns, C., Meng, X., Zhang, Y., & Ren, J. (2018). Ablation of toll-like receptor 4 attenuates aging-induced myocardial remodeling and contractile dysfunction through NCoRI-HDAC1-mediated regulation of autophagy. Journal of molecular and cellular cardiology, 119, 40-50.

Kundu, R., Banerjee, S., Baidya, S. K., Adhikari, N., & Jha, T. (2022). A quantitative structural analysis of AR-42 derivatives as HDAC1 inhibitors for the identification of promising structural contributors. SAR and QSAR in Environmental Research, 33(11), 861-883.

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

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