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Mouse Anti-HDAC8 Antibody (2C8) (CBMAB-0447-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
2C8
Antibody Isotype
IgG2b
Application
IP, MA

Basic Information

Immunogen
Recombinant protein
Specificity
Human
Antibody Isotype
IgG2b
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
Supernatant
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
HDAC8
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. HDAC8 (histone deacetylase 8) belongs to class I of the histone deacetylase family. HDAC8 catalyzes the deacetylation of lysine residues in the histone N-terminal tails and represses transcription in large multiprotein complexes with transcriptional co-repressors.
Entrez Gene ID
55869
UniProt ID
Q9BY41
Alternative Names
HD8; WTS; RPD3; CDA07; CDLS5; MRXS6; HDACL1
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:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, 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:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748).

Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748).

Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700).

May play a role in smooth muscle cell contractility (PubMed:15772115).

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
Chromatin assembly or disassembly Source: ProtInc
Chromatin organization Source: UniProtKB
Histone H3 deacetylation Source: GO_Central
Histone H4 deacetylation Source: GO_Central
Negative regulation of protein ubiquitination Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: ProtInc
Positive regulation of transcription by RNA polymerase II Source: GO_Central
Regulation of cohesin loading Source: UniProtKB
Regulation of protein stability Source: BHF-UCL
Regulation of telomere maintenance Source: BHF-UCL
Sister chromatid cohesion Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm; Chromosome. Excluded from the nucleoli (PubMed:10748112). Found in the cytoplasm of cells showing smooth muscle differentiation (PubMed:15772115, PubMed:16538051).
Involvement in disease
Cornelia de Lange syndrome 5 (CDLS5):
A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.
PTM
Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4.
More Infomation

Kim, J. Y., Cho, H., Yoo, J., Kim, G. W., Jeon, Y. H., Lee, S. W., & Kwon, S. H. (2022). Pathological role of HDAC8: Cancer and beyond. Cells, 11(19), 3161.

Fontana, A., Cursaro, I., Carullo, G., Gemma, S., Butini, S., & Campiani, G. (2022). A therapeutic perspective of HDAC8 in different diseases: an overview of selective inhibitors. International Journal of Molecular Sciences, 23(17), 10014.

Yang, W., Feng, Y., Zhou, J., Cheung, O. K. W., Cao, J., Wang, J., ... & Cheng, A. S. L. (2021). A selective HDAC8 inhibitor potentiates antitumor immunity and efficacy of immune checkpoint blockade in hepatocellular carcinoma. Science translational medicine, 13(588), eaaz6804.

Sawada, Y., Nakatsuji, T., Dokoshi, T., Kulkarni, N. N., Liggins, M. C., Sen, G., & Gallo, R. L. (2021). Cutaneous innate immune tolerance is mediated by epigenetic control of MAP2K3 by HDAC8/9. Science immunology, 6(59), eabe1935.

Spreafico, M., Gruszka, A. M., Valli, D., Mazzola, M., Deflorian, G., Quintè, A., ... & Pistocchi, A. (2020). HDAC8: a promising therapeutic target for acute myeloid leukemia. Frontiers in Cell and Developmental Biology, 8, 844.

Hassan, M. M., Israelian, J., Nawar, N., Ganda, G., Manaswiyoungkul, P., Raouf, Y. S., ... & Gunning, P. T. (2020). Characterization of conformationally constrained benzanilide scaffolds for potent and selective HDAC8 targeting. Journal of Medicinal Chemistry, 63(15), 8634-8648.

An, P., Chen, F., Li, Z., Ling, Y., Peng, Y., Zhang, H., ... & Wang, H. (2020). HDAC8 promotes the dissemination of breast cancer cells via AKT/GSK-3β/Snail signals. Oncogene, 39(26), 4956-4969.

Saito, S., Zhuang, Y., Suzuki, T., Ota, Y., Bateman, M. E., Alkhatib, A. L., ... & Lasky, J. A. (2019). HDAC8 inhibition ameliorates pulmonary fibrosis. American Journal of Physiology-Lung Cellular and Molecular Physiology, 316(1), L175-L186.

Zhao, C., Zang, J., Inks, E. S., Xu, W., Chou, C. J., & Zhang, Y. (2018). Discovery of meta-sulfamoyl N-hydroxybenzamides as HDAC8 selective inhibitors. European Journal of Medicinal Chemistry, 150, 282-291.

Amin, S. A., Adhikari, N., & Jha, T. (2018). Structure-activity relationships of HDAC8 inhibitors: non-hydroxamates as anticancer agents. Pharmacological Research, 131, 128-142.

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

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