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Mouse Anti-HDAC5 Recombinant Antibody (CBFYH-0877) (CBMAB-H0665-FY)

This product is mouse antibody that recognizes HDAC5. The antibody CBFYH-0877 can be used for immunoassay techniques such as: ELISA, WB.
See all HDAC5 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-0877
Antibody Isotype
IgG1, κ
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1, κ
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
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Histone Deacetylase 5
Introduction
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
10014
UniProt ID
Q9UQL6
Alternative Names
Histone Deacetylase 5; Antigen NY-CO-9; EC 3.5.1.98; HD5; KIAA0600; NY-CO-9
Function
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Serves as a corepressor of RARA and causes its deacetylation (PubMed:28167758).

In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758).
Biological Process
B cell activation Source: UniProtKB
B cell differentiation Source: UniProtKB
Cellular response to insulin stimulus Source: BHF-UCL
Chromatin organization Source: UniProtKB
Chromatin remodeling Source: ProtInc
Heterochromatin assembly Source: ProtInc
Histone deacetylation Source: BHF-UCL
Inflammatory response Source: UniProtKB
Negative regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
Negative regulation of myotube differentiation Source: BHF-UCL
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: MGI
Positive regulation of DNA-binding transcription factor activity Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Protein deacetylation Source: UniProtKB
Regulation of gene expression, epigenetic Source: UniProtKB
Regulation of myotube differentiation Source: UniProtKB
Regulation of protein binding Source: BHF-UCL
Cellular Location
Nucleus; Cytoplasm. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1.
PTM
Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription (By similarity).
Ubiquitinated. Polyubiquitination however does not lead to its degradation.

He, X., Zhang, J., Guo, Y., Yang, X., Huang, Y., & Hao, D. (2022). Exosomal miR-9-5p derived from BMSCs alleviates apoptosis, inflammation and endoplasmic reticulum stress in spinal cord injury by regulating the HDAC5/FGF2 axis. Molecular Immunology, 145, 97-108.

Zhou, Y., Jin, X., Yu, H., Qin, G., Pan, P., Zhao, J., ... & Wu, H. (2022). HDAC5 modulates PD-L1 expression and cancer immunity via p65 deacetylation in pancreatic cancer. Theranostics, 12(5), 2080.

Yang, J., Gong, C., Ke, Q., Fang, Z., Chen, X., Ye, M., & Xu, X. (2021). Insights into the function and clinical application of HDAC5 in cancer management. Frontiers in Oncology, 11, 661620.

Xu, Z., Jia, K., Wang, H., Gao, F., Zhao, S., Li, F., & Hao, J. (2021). METTL14-regulated PI3K/Akt signaling pathway via PTEN affects HDAC5-mediated epithelial–mesenchymal transition of renal tubular cells in diabetic kidney disease. Cell death & disease, 12(1), 32.

Hu, B., Xu, Y., Li, Y. C., Huang, J. F., Cheng, J. W., Guo, W., ... & Yang, X. R. (2020). CD13 promotes hepatocellular carcinogenesis and sorafenib resistance by activating HDAC5‐LSD1‐NF‐κB oncogenic signaling. Clinical and translational medicine, 10(8), e233.

Sato, T., Verma, S., Andrade, C. D. C., Omeara, M., Campbell, N., Wang, J. S., ... & Wein, M. N. (2020). A FAK/HDAC5 signaling axis controls osteocyte mechanotransduction. Nature communications, 11(1), 3282.

Gu, P., Pan, Z., Wang, X. M., Sun, L., Tai, L. W., & Cheung, C. W. (2018). Histone deacetylase 5 (HDAC5) regulates neuropathic pain through SRY-related HMG-box 10 (SOX10)-dependent mechanism in mice. Pain, 159(3), 526-539.

Zhao, M., Li, L., Zhou, J., Cui, X., Tian, Q., Jin, Y., & Zhu, Y. (2018). MiR-2861 behaves as a biomarker of lung cancer stem cells and regulates the HDAC5-ERK system genes. Cellular reprogramming, 20(2), 99-106.

Cao, C., Wu, H., Vasilatos, S. N., Chandran, U., Qin, Y., Wan, Y., ... & Huang, Y. (2018). HDAC5–LSD1 axis regulates antineoplastic effect of natural HDAC inhibitor sulforaphane in human breast cancer cells. International journal of cancer, 143(6), 1388-1401.

Gu, X., Fu, C., Lin, L., Liu, S., Su, X., Li, A., ... & Wang, X. (2018). miR‐124 and miR‐9 mediated downregulation of HDAC5 promotes neurite development through activating MEF2C‐GPM6A pathway. Journal of Cellular Physiology, 233(1), 673-687.

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

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