HDAC10 Antibodies

Polyamine deacetylase HDAC10 (HDAC10)

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. .

Gene Information

Human
Gene Name:	HDAC10
Uniprot:	Q969S8
Entrez:	83933

Family

Belongs to:
histone deacetylase family

Alternative Names

DKFZP761B039; EC 3.5.1.98; HD10; histone deacetylase 10; MGC149722

Molecular Weight

Mass (kDA):
71.445 kDA

Genomic Context

Human
Location:	22q13.33
Sequence:	22; NC_000022.11 (50245183..50251265, complement)

Tissue Specificity

Ubiquitous. High expression in liver, spleen, pancreas and kidney.

Subcellular Localizations

Cytoplasm. Nucleus. Excluded from nucleoli.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Lung Neoplasms
• Traditional Serrated Adenoma
• Stomach Neoplasms
• Tumor Angiogenesis
• Malignant Neoplasm Of Lung
• Cell Transformation, Neoplastic
• Adenoma
• Neoplasm Metastasis
• Malignant Neoplasm Of Breast

• Hepatitis B
• Lung Diseases
• Neoplasm Invasiveness
• Lung Diseases, Obstructive
• Malignant Neoplasm Of Adrenal Cortex
• Adrenal Cortical Adenoma

Interacting Proteins

• TRIM54

Pathways

• Localization
• Cell Growth
• Pathogenesis
• Cell Proliferation
• Induction Of Apoptosis
• Cell Cycle
• Histone Acetylation
• Angiogenesis
• Protein Phosphorylation
• Gene Silencing
• Osteoblast Differentiation
• Dna Methylation
• Dna Repair

• Alpha-tubulin Acetylation
• Nuclear Export
• Cell Cycle Arrest
• Methylation
• Gene Conversion
• Feeding Behavior
• Rna Processing

PTMs

• Acetylation
• Deacetylation

• Phosphorylation
• Cleavage

• Methylation

Research Areas

• Breast Cancer
• Cancer
• Checkpoint signaling
• Chromatin Research
• Epigenetics

• Transcription Factors and Regulators

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HDAC10

Best Uses of the HDAC10 Marker

The HDAC10 Marker can be used in many areas of biology. The protein is detected by antibodies, monoclonal and polyclonal, which react with HDAC10 in many animal samples. Boster Bio has been developing antibodies against HDAC10 using HDAC10 enzyme models in rabbit and mouse. Histone acetylation is an important step in transcriptional regulation. It also acts as a marker for epigenetic repression. HDACs, multiprotein complex enzymes, act on histones through large complexes. Tong and his colleagues isolated HDAC10 in 2004, a new human class II histone deacetylase.

HDAC10 Marker

Biological assays use antibodies for HDAC10. These antibodies can either be monoclonal/polyclonal and are compatible for use with many samples, including those from mice, rabbit, or humans. HDAC10 deacetylases regulate transcription via modification of histones. They act via large multiprotein complicatedes. Tong J.J. and colleagues identified HDAC10 as a novel class II human histone deacetylase.

Applications

The HDAC10 genome encodes a protein that has regulatory effects on AKT levels. Its phosphorylation influences many pathways including the cell cycle and gene transcription as well as tumor growth. Analyzing the expression of HDAC10 in lung cancer tissues can help you identify it. This gene is highly expressed in lung cancer cells, but it is also found in adjacent normal cells. The HDAC10 gene is used in cancer research for the study of tumors, drug discovery and structural biology.

HDAC10 is expressed in high levels in lung cancer cells. This is because it is vital for tumour growth. It also promotes apoptosis, homologous replication and homologous gene expression. Although there are no approved therapies for this stage of the disease, combination therapy is emerging as a promising treatment that can increase the effectiveness and survival rates. There is not consensus about the role of HDAC10 for lung cancer.

HDAC10 protein is composed two polypeptide domains which interact with a substrate. The HDAC10 peptide is very similar in structure to the PDACHDAC6 heterodomain assembly found in Schizosaccharomyces. Its E274 mutation provides many benefits. It increases the active sites and eliminates steric clashes from the acetyllysine rearbone. HDAC activity is also introduced.

HDAC10 also has many other uses. It has been used for the treatment of lung carcinoma. It has been shown to increase tumour growth when it is overexpressed in lung cancer cells. HDAC10 also promotes the growth in vivo of tumour cells. These findings support previous observations on lung cancer cell line lines. These findings may not be conclusive but are indicative of its potential use in a variety healthcare settings.

Researchers were also capable of detecting the HDAC10 genes expression in several lung tumor cell lines. The HDAC10 protein resides in both the nucleus and the cytoplasm of these lung cancer cells. HDAC10 can be used to differentiate cancer tumors from surrounding normal tissue by detecting HDAC10. The HDAC10 score must be the same as that of normal cells when evaluating cancer cell lines.

Primers

Tong J.J., along with colleagues, identified the HDAC10 mark. It is a novel human class II histone deacetylase. It plays an important role in the regulation of transcription, and provides a tag for epigenetic repression. It is the result of large multiprotein combinations. HDACs are found in many bacteria species. Boster Bio has developed monoclonal as well as polyclonal antibody to detect HDAC10.

Molecular cloning and characterization of a novel histone deacetylase

This article describes the Molecular cloning of and characterization of a novel histone-deacetylase marker, HDAC10. This enzyme is a repressor of transcription, tethered to the promoter of a gene. Its structure, pharmacology, and localization expand the complexity of the HDAC family.

The HDAC3 enzyme controls the methylation of H3K9 during DNA damage response and regulates the activity of a protein called SUV39h2. It also negatively regulates the NF-kappa B pathway. The SIRT1 gene regulates the H3K9 methylation process by deacetylating K266 in the SUV39h2 protein. The SIRT6 Gene induces monoubiquitination cysteines within SUV39h2.

HDACs can be multifaceted enzymes, with many different catalytic activities. Figure 1 shows HDAC's domain structure. On the right of each protein, you can see the total number of amino acid residues and molecular weight. The domain structure is crucial for regulation of polyubiquitin-chain turnover. The HDACs have zinc-finger domains that ubiquitinbind to polyubiquitin, which can negatively regulate turnover. The authors of the paper identified two distinct deacetylase domains, reclassified as the catalytic domain 1 (CD1) and the catalytic domain 2 (CD2). These domains are capable of recognizing different substrates.

HDAC6 is a microtubule-associated deacetylase that primarily localizes in the cytoplasm. It also has a microtubule binding domain and is involved with chemotactic cell movement. Both HDACs contain NLS motifs at adjacent Kac sites, and are recruited to the nucleus via the exportin receptor CRM1/exportin.

Targeted therapeutic strategies for specific cancers could be made possible by the discovery and targeting of a novel HDAC8 substrate. Targeting the genes responsible in HDAC8 dysregulation can help us identify tumor suppressor ARID1A. This gene is important for mitosis. These new substrates can be used to guide future therapeutic strategies against HDAC8. This study adds to our understanding about HDAC8's function.

HDACs play a variety of roles in cancer biology. They can affect the metabolism of a variety of cytoplasmic proteins such as RNA binding proteins. HDACs in class IIa are involved the trans-repressions gluconeogenic enzymes. They also mediate FoxO activation. SIRT2 also deacetylates isocitrate deshydrogenase 1, an enzyme involved the TCA cycle. It has been shown, that sirtuins prevent the growth of colorectal tumor liver metastases.