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Mouse Anti-HDAC10 Recombinant Antibody (CBFYH-0818) (CBMAB-H1730-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-0818
Antibody Isotype
IgG1
Application
IF, IHC-P, WB

Basic Information

Immunogen
Full length human recombinant protein of human HDAC10 produced in HEK293T cell
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.

Target

Full Name
HDAC10
Introduction
The protein encoded by this gene belongs to the histone deacetylase family, members of which deacetylate lysine residues on the N-terminal part of the core histones. Histone deacetylation modulates chromatin structure, and plays an important role in transcriptional regulation, cell cycle progression, and developmental events. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
83933
UniProt ID
Q969S8
Alternative Names
Histone Deacetylase 10; HD10; EC 3.5.1.98
Function
Polyamine deacetylase (PDAC), which acts preferentially on N8-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954).

Exhibits attenuated catalytic activity toward N1,N8-diacetylspermidine and very low activity, if any, toward N1-acetylspermidine (PubMed:28516954).

Histone deacetylase activity has been observed in vitro (PubMed:11861901, PubMed:11726666, PubMed:11677242, PubMed:11739383).

Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039).

The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:28516954).

May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:23801752, PubMed:29968769).

May play a role in homologous recombination (PubMed:21247901).

May promote DNA mismatch repair (PubMed:26221039).
Biological Process
Chromatin organization Source: UniProtKB
DNA repair Source: UniProtKB-KW
Histone deacetylation Source: UniProtKB
Homologous recombination Source: UniProtKB
Macroautophagy Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Peptidyl-lysine deacetylation Source: UniProtKB
Polyamine deacetylation Source: UniProtKB
Positive regulation of mismatch repair Source: UniProtKB
Protein deacetylation Source: UniProtKB
Regulation of transcription, DNA-templated Source: UniProtKB
Spermidine deacetylation Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus. Excluded from nucleoli.
Involvement in disease
In neuroblastoma cells, may promote autophagy in response to chemotherapy-induced DNA damage and efflux of chemotherapeutics via lysosomal exocytosis, hence protecting cells from cytotoxic agents (PubMed:23801752, PubMed:29968769). Expression levels may correlate with survival in neuroblastoma patients, with low levels in the tumor correlating with long-term patient survival and high expression with poor prognosis (PubMed:23801752). Therefore has been proposed as a biomarker to predict neuroblastoma chemoresistance and treatment outcome (PubMed:23801752).
More Infomation

Zeyen, P., Zeyn, Y., Herp, D., Mahmoudi, F., Yesiloglu, T. Z., Erdmann, F., ... & Sippl, W. (2022). Identification of histone deacetylase 10 (HDAC10) inhibitors that modulate autophagy in transformed cells. European Journal of Medicinal Chemistry, 234, 114272.

Steimbach, R. R., Herbst-Gervasoni, C. J., Lechner, S., Stewart, T. M., Klinke, G., Ridinger, J., ... & Miller, A. K. (2022). Aza-SAHA derivatives are selective histone deacetylase 10 chemical probes that inhibit polyamine deacetylation and phenocopy HDAC10 knockout. Journal of the American Chemical Society, 144(41), 18861-18875.

Xi, J., Xu, Y., Guo, Z., Li, J., Wu, Y., Sun, Q., ... & Kang, J. (2022). LncRNA SOX1‐OT V1 acts as a decoy of HDAC10 to promote SOX1‐dependent hESC neuronal differentiation. EMBO reports, 23(2), e53015.

Yu, D. S., Song, X. L., & Yan, C. (2021). Oncogenic miRNA‐1908 targets HDAC10 and promotes the aggressive phenotype of cervical cancer cell. The Kaohsiung Journal of Medical Sciences, 37(5), 402-410.

Herbst-Gervasoni, C. J., Steimbach, R. R., Morgen, M., Miller, A. K., & Christianson, D. W. (2020). Structural basis for the selective inhibition of HDAC10, the cytosolic polyamine deacetylase. ACS chemical biology, 15(8), 2154-2163.

Dahiya, S., Beier, U. H., Wang, L., Han, R., Jiao, J., Akimova, T., ... & Hancock, W. W. (2020). HDAC10 deletion promotes Foxp3+ T-regulatory cell function. Scientific reports, 10(1), 424.

Li, Y., Zhang, X., Zhu, S., Dejene, E. A., Peng, W., Sepulveda, A., & Seto, E. (2020). HDAC10 regulates cancer stem-like cell properties in KRAS-driven lung adenocarcinoma. Cancer research, 80(16), 3265-3278.

Shan, C., Lu, Z., Li, Z., Sheng, H., Fan, J., Qi, Q., ... & Zhang, S. (2019). 4-hydroxyphenylpyruvate dioxygenase promotes lung cancer growth via pentose phosphate pathway (PPP) flux mediated by LKB1-AMPK/HDAC10/G6PD axis. Cell death & disease, 10(7), 525.

Ridinger, J., Koeneke, E., Kolbinger, F. R., Koerholz, K., Mahboobi, S., Hellweg, L., ... & Oehme, I. (2018). Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes neuroblastoma chemoresistance. Scientific reports, 8(1), 10039.

Shinsky, S. A., & Christianson, D. W. (2018). Polyamine deacetylase structure and catalysis: prokaryotic acetylpolyamine amidohydrolase and eukaryotic HDAC10. Biochemistry, 57(22), 3105-3114.

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

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