Mouse Anti-HDAC10 Recombinant Antibody (CBFYH-0819) (CBMAB-H1731-FY)

Name: Mouse Anti-HDAC10 Recombinant Antibody (CBFYH-0819)
SKU: CBMAB-H1731-FY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYH-0819

Application

WB, IF, FC

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

Buffer

PBS, PH 7.3, 1% BSA, 50% glycerol

Preservative

0.02% Sodium azide

Concentration

0.34 mg/mL

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

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).

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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

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