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Mouse Anti-HDAC2 (AA 415-488) Recombinant Antibody (CBFYH-0832) (CBMAB-H1748-FY)

This product is mouse antibody that recognizes HDAC2. The antibody CBFYH-0832 can be used for immunoassay techniques such as: WB, IHC.
See all HDAC2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-0832
Antibody Isotype
IgG1
Application
WB, IHC

Basic Information

Immunogen
Human recombinant protein fragment corresponding to amino acids 415-488 of human HDAC2 produced in E.coli
Specificity
Human
Antibody Isotype
IgG1
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 freeze/thaw cycles.
Epitope
AA 415-488

Target

Full Name
Histone Deacetylase 2
Introduction
This gene product belongs to the histone deacetylase family. Histone deacetylases act via the formation of large multiprotein complexes, and are responsible for the deacetylation of lysine residues at the N-terminal regions of core histones (H2A, H2B, H3 and H4). This protein forms transcriptional repressor complexes by associating with many different proteins, including YY1, a mammalian zinc-finger transcription factor. Thus, it plays an important role in transcriptional regulation, cell cycle progression and developmental events. Alternative splicing results in multiple transcript variants.
Entrez Gene ID
UniProt ID
Alternative Names
Histone Deacetylase 2; EC 3.5.1.98; HD2; Transcriptional Regulator Homolog RPD3; YY1-Associated Factor 1; RPD3; YAF1
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:28497810).

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

Histone deacetylases act via the formation of large multiprotein complexes (By similarity).

Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404).

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).

Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (PubMed:19343227).

May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity).

Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678).

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).
Biological Process
Behavioral response to ethanol Source: Ensembl
Cardiac muscle hypertrophy Source: Ensembl
Cellular response to dopamine Source: Ensembl
Cellular response to heat Source: Ensembl
Cellular response to hydrogen peroxide Source: Ensembl
Cellular response to retinoic acid Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Chromatin remodeling Source: ComplexPortal
Circadian regulation of gene expression Source: UniProtKB
Dendrite development Source: UniProtKB
Embryonic digit morphogenesis Source: BHF-UCL
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
Heterochromatin organization Source: BHF-UCL
Histone deacetylation Source: ComplexPortal
Histone H3 deacetylation Source: UniProtKB
Histone H4 deacetylation Source: UniProtKB
Negative regulation of apoptotic process Source: BHF-UCL
Negative regulation of dendritic spine development Source: Ensembl
Negative regulation of DNA binding Source: Ensembl
Negative regulation of DNA-binding transcription factor activity Source: BHF-UCL
Negative regulation of MHC class II biosynthetic process Source: BHF-UCL
Negative regulation of neuron projection development Source: BHF-UCL
Negative regulation of peptidyl-lysine acetylation Source: Ensembl
Negative regulation of transcription, DNA-templated Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: BHF-UCL
Odontogenesis of dentin-containing tooth Source: BHF-UCL
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of collagen biosynthetic process Source: BHF-UCL
Positive regulation of epithelial to mesenchymal transition Source: Ensembl
Positive regulation of interleukin-1 production Source: Ensembl
Positive regulation of male mating behavior Source: Ensembl
Positive regulation of oligodendrocyte differentiation Source: Ensembl
Positive regulation of proteolysis Source: BHF-UCL
Positive regulation of signaling receptor activity Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of tumor necrosis factor production Source: Ensembl
Positive regulation of tyrosine phosphorylation of STAT protein Source: Ensembl
Response to amphetamine Source: Ensembl
Response to caffeine Source: Ensembl
Response to cocaine Source: Ensembl
Response to hyperoxia Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to nicotine Source: Ensembl
Response to xenobiotic stimulus Source: Ensembl
Cellular Location
Cytoplasm; Nucleus
PTM
S-nitrosylated by GAPDH. In neurons, S-nitrosylation at Cys-262 and Cys-274 does not affect enzyme activity, but induces HDAC2 release from chromatin. This in turn increases acetylation of histones surrounding neurotrophin-dependent gene promoters and promotes their transcription. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching.

Hua, H. S., Wen, H. C., Lee, H. S., Weng, C. M., Yuliani, F. S., Kuo, H. P., ... & Lin, C. H. (2023). Endothelin-1 induces connective tissue growth factor expression in human lung fibroblasts by disrupting HDAC2/Sin3A/MeCP2 corepressor complex. Journal of Biomedical Science, 30(1), 1-16.

Kwak, S., Park, S. H., Kim, S. H., Sung, G. J., Song, J. H., Jeong, J. H., ... & Choi, K. C. (2022). miR-3189-targeted GLUT3 repression by HDAC2 knockdown inhibits glioblastoma tumorigenesis through regulating glucose metabolism and proliferation. Journal of Experimental & Clinical Cancer Research, 41(1), 87.

Li, W., Ye, K., Li, X., Liu, X., Peng, M., Chen, F., ... & Zhu, L. (2022). YTHDC1 is downregulated by the YY1/HDAC2 complex and controls the sensitivity of ccRCC to sunitinib by targeting the ANXA1-MAPK pathway. Journal of Experimental & Clinical Cancer Research, 41(1), 1-18.

Zhao, H., Li, G., Wang, R., Tao, Z., Ma, Q., Zhang, S., ... & Luo, Y. (2020). Silencing of microRNA‐494 inhibits the neurotoxic Th1 shift via regulating HDAC2‐STAT4 cascade in ischaemic stroke. British Journal of Pharmacology, 177(1), 128-144.

Darvishi, N., Rahimi, K., Mansouri, K., Fathi, F., Menbari, M. N., Mohammadi, G., & Abdi, M. (2020). MiR-646 prevents proliferation and progression of human breast cancer cell lines by suppressing HDAC2 expression. Molecular and cellular probes, 53, 101649.

Liu, B., Chen, S., Rose, A. L., Chen, D., Cao, F., Zwinderman, M., ... & Haisma, H. J. (2020). Inhibition of histone deacetylase 1 (HDAC1) and HDAC2 enhances CRISPR/Cas9 genome editing. Nucleic acids research, 48(2), 517-532.

Hu, X. T., Xing, W., Zhao, R. S., Tan, Y., Wu, X. F., Ao, L. Q., ... & Xu, X. (2020). HDAC2 inhibits EMT-mediated cancer metastasis by downregulating the long noncoding RNA H19 in colorectal cancer. Journal of Experimental & Clinical Cancer Research, 39(1), 1-14.

Tang, W., Zhou, W., Xiang, L., Wu, X., Zhang, P., Wang, J., ... & Wang, J. (2019). The p300/YY1/miR-500a-5p/HDAC2 signalling axis regulates cell proliferation in human colorectal cancer. Nature communications, 10(1), 663.

Fang, W. F., Chen, Y. M., Lin, C. Y., Huang, H. L., Yeh, H., Chang, Y. T., ... & Lin, M. C. (2018). Histone deacetylase 2 (HDAC2) attenuates lipopolysaccharide (LPS)-induced inflammation by regulating PAI-1 expression. Journal of inflammation, 15, 1-11.

Gao, Y., She, R., Wang, Q., Li, Y., & Zhang, H. (2018). Up-regulation of miR-299 suppressed the invasion and migration of HTR-8/SVneo trophoblast cells partly via targeting HDAC2 in pre-eclampsia. Biomedicine & Pharmacotherapy, 97, 1222-1228.

Liao, M., Liao, W., Xu, N., Li, B., Liu, F., Zhang, S., ... & Zhang, Y. (2019). LncRNA EPB41L4A-AS1 regulates glycolysis and glutaminolysis by mediating nucleolar translocation of HDAC2. EBioMedicine, 41, 200-213.

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

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