Histone deacetylase 6 Antibodies

Histone deacetylase 6 (HDAC6)

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 (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.

Gene Information

Human
Gene Name:	HDAC6
Uniprot:	Q9UBN7
Entrez:	10013

Family

Belongs to:
histone deacetylase family

Alternative Names

EC 3.5.1.98; HD6FLJ16239; histone deacetylase 6; JM21; KIAA0901

Molecular Weight

Mass (kDA):
131.419 kDA

Genomic Context

Human
Location:	Xp11.23
Sequence:	X; NC_000023.11 (48801398..48824982)

Subcellular Localizations

Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Perikaryon. Cell projection, dendrite. Cell projection, axon. It is mainly cytoplasmic, where it is associated with microtubules.

Diseases

• Malignant Neoplasms
• Neoplasms
• Malignant Neoplasm Of Breast
• Neurodegenerative Disorders
• Mammary Neoplasms
• Traditional Serrated Adenoma
• Neoplasm Metastasis
• Carcinoma
• Leukemia
• Cell Invasion
• Nerve Degeneration
• Cell Transformation, Neoplastic

• Tumor Angiogenesis
• Malignant Neoplasm Of Prostate
• Tissue Adhesions
• Myeloid Leukemia
• Parkinson Disease
• Multiple Myeloma
• Leukemia, Myelocytic, Acute

Interacting Proteins

• ATP13A2
• BRMS1
• Cdc20
• CTNNB1
• CTTN

• Cttn
• CYLD
• EGFR
• MYD88
• PRKCA

• PRKN
• PROM1

Pathways

• Cell Migration
• Autophagy
• Transport
• Localization
• Cell Motility
• Cell Death
• Cell Cycle
• Cell Growth
• Histone Acetylation
• Cell Proliferation
• Tubulin Deacetylation
• Angiogenesis
• Pathogenesis

• Protein Acetylation
• Cell Cycle Arrest
• Translation
• Rna Interference
• Alpha-tubulin Acetylation
• Mitosis
• Nuclear Export

PTMs

• Acetylation
• Deacetylation
• Phosphorylation
• Ubiquitination
• Cleavage
• Dephosphorylation

• Reduction
• Farnesylation
• Methylation
• Carboxylation
• Ribosylation
• Biotinylation

• Glycosylation

Research Areas

• Breast Cancer
• Cancer
• Cell Cycle and Replication
• Chromatin Research

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HDAC6

Best Uses Of The HDAC6 Marker

If you're in the market for high-quality, highly-specific HDAC6 antibody You've probably heard about Boster Bio. Boster Bio's antibodies have been validated across a variety of platforms, with both positive and negative samples. In addition Boster's antibodies are extremely specific and can bind to a specific target with high affinity. Boster's products come with product credits for first-time reviews. They'll even give you a reward for writing the first review of their products! Boster's products are accessible to all scientists around the globe!

HDAC6 is a standard HDAC

There are many functions of HDAC6 in the cell which includes its regulation of transcription and translation. It regulates the activity heat-shock proteins, as well as stress granules. This review focuses on the significance of HDAC6 for cancer. It also examines the biological process through which HDAC6 interacts with other proteins. This review will also examine the role of HDAC6 in various neurodegenerative diseases.

HDAC6 is a requirement for survival in cancer cells. Knockdown of HDAC6 inhibits anchorage-independent proliferation, which is a hallmark of malignant transformation. HDAC6 knockdown in cancer cells can prevent tumor growth. Cancer cells that lack HDAC6 are unlikely to undergo anchorage-independent growth. In the mouse model, knockdown of HDAC6 inhibited anchorage-independent growth.

In vitro studies have revealed the Tyr 1156 and Arg 1155 residues act as gatekeepers. They alter the conformation of the ubiquitin binding sites. HDAC6 recruits ubiquitin to cells however no crystallographic information are available. The mechanism through which HDAC6 recruits aggregates has been discovered through computational interactions and molecular dynamics simulations.

In the mouse model, the deletion of HDAC6 reduced growth of tumors. The HDAC6 inhibitor, emt-TCL1HDAC6KO, blocked the progression of tumors. HDAC6 silencing in humans prevented cancer progression and immune surveillance. This study highlights the importance of HDAC6 in the T-cell immune system. While HDAC6 is not yet fully understood yet, its function is intriguing.

HDAC6 is crucial for the cell's response to stress. It regulates the process of translation. Its ubiquitin-binding and deacetylase activities allow it to recruit SGs to a motor protein through the binding of a Ras-GTPase-activated protein (Ras-GTPase-activated-protein), also known as G3BP1. The receptor-binding HDAC6 blockades NFKb p50/p52.

It blocks proteasome activity.

The HDAC6 protein is a proteasome marker. activity. This protein is ubiquitinated . It forms an aggresome-like organelle. HDAC6 interacts with ubiquitinated proteins, and joins them to form an encapsulated complex of proteins. HDAC6-protein complexes can be dissociated by AAATPase/VCP. They are eliminated through autophagy. This protein is also involved in transcription activation of genes.

HDAC6 is an important factor in tumorigenesis. There have been numerous research on the role of this protein in the process of tumor formation. Its ability to block proteasome activity and stabilize MTs makes it a prime target for oncologists and researchers trying to treat cancer. It also plays vital roles in the cell biology, including the regulation of stress granules and heat-shock protein.

This protein is responsible for HDAC6 inhibition as well as de-acetylation survivin. HDAC6 plays a role in de-acetylation the survivin protein which aids in nuclear translocation. This de-acetylation of survivin results in decreased protein stability and lowers its ability to protect cells from the proteasome.

A new drug targeting the HDAC6 protein has been discovered which can block the activity of the proteasome. The Boster Bio HDAC6 marker blocks the function of the proteasome in the lab. The drug is a small thiazole Ring inhibitor, binds the HDAC6 protein in a way similar to the natural HDAC6 inhibitors.

Many biological assays employ antibodies to detect HDAC6. Monoclonal and polyclonal antibody react with HDAC6 in numerous samples. Boster Bio develops antibodies that target HDAC6 within mouse and rabbit samples. The HDAC6 protein is a key player in cell motility and the degradation of protein aggregates. The HDAC6 protein is an essential component of a variety of NDs.

It interacts with tau.

HDAC6 is involved in signaling pathways and is associated with neurodegenerative disorders. It also regulates cytoskeletal remodelling and neuronal cell dynamics. HDAC6 interacts with tau in many ways. Continue reading to find out more about this vital protein. Below are a few examples of the roles that HDAC6 plays in neurodegenerative disorders. Here are the primary roles of HDAC6.

The cellular environment of neurons is modified by the accumulation of Amyloid-B and Tau aggregates. This neurotoxicity causes an increase in oxidative stress and the creation of reactive oxygen and nitrogen species (ROS and RNS). This causes damage to the cell membrane, mitochondrial dysfunctions and demyelination, among other effects. To prevent this damage, the aggregates build up are directed toward the proteasome system ubiquitin and cleared via the HDAC6-mediated aggresome pathway.

Researchers discovered that the HD phenotype is reduced when chaperones of humans are co-expressed within Drosophila models. However, the human chaperones are embedded in huntingtin aggregates decreasing their intracellular accessibility and causing abnormal protein folding. It is possible that HDAC6 plays an important protective function in HD. The expression of HDAC6 is seen in the striatum and caudate nucleus. This indicates a protective role.

HDAC6 has been shown to be able to bind to Tau in molecular studies. This association can alter the function of Tau. It reduces the activity of the deacetylase a-tubulin and alters Tau's propensity to aggregate. The molecular basis of this interaction is not clarified. It is well-known that HDAC6 hinders tau by alteration of its a-tubulin and Ubiquitin Ligases.

It inhibits the Ubiquitin-proteasome

Boster Bio HDAC6 inhibitors target a key protein in the ubiquitin-proteasome. The HDAC6 enzyme connects to polyubiquitinated misfolded protein and then recruits cargo to Dynein motors. This fusion produces aggresomes which are concentrated protein aggregates. Autophagy is an essential function in normal cells, however it plays an an even more critical role in neurodegenerative disorders.

An immunocytochemical analysis was carried out on total cellular proteins to determine the concentration of HDAC6 inhibitors. Cell Signaling, Santa Cruz Biotechnology Sigma and Abcam purchased antibodies. Secondary antibodies were employed to show protein localization. Nuclei were visualized using 4,6-diamidino-2-phenylindole (DAPI) stain. The blots were mounted onto coverslips and the results examined under an Eclipse TE 2000E microscope with BeNeLux technical assistance.

Poly-ubiquitinated protein accumulation is seen in IOSE-29 and ES-2 cell treated with 10mM NK84 and PS-341, respectively. This is due to the simultaneous inhibition of HDAC6 activity as well as proteasome activity. The cell's toxicity results from. In addition, the HDAC6-dependent pathway is a minor degradation pathway under normal conditions but becomes an essential pathway when the stress of UPS is high.

HDAC6 blocks aggresome formation. It also regulates the ubiquitin-proteasome-mediated degradation of alpha-synuclein. It is also associated with neurodegenerative diseases. Zhang and Zhu recently discovered that HDAC6 plays a role in the formation of prion protein. The study suggests that this protein is involved in a process called autophagy.

Although the ubiquitin–proteasome pathway was initially thought to be a distinct process, recent research has proven that they are in fact interdependent. These results suggest that the two pathways could interact and cooperate in the degradation of misfolded proteins. To identify which pathways are the most essential to cellular processes, further research is needed. If the combination of HDAC6 inhibitors and proteasome inhibits autophagy, cells could suffer from a host-sparing effect.

It blocks neurodegenerative processes.

HDAC6 is an important regulator of postmitotic cells which includes neurons. Its roles in neuronal survival and growth are dependent on its role in protein degradation as well as axonal transport. This enzyme has emerged as a therapeutic target for neurodegenerative diseases, such as Alzheimer's and Parkinson's. This review summarizes the knowledge we have about HDAC6's function and the primary arguments for its use as a treatment for neurodegenerative diseases.

The reduction of HDAC6 levels in mice with AD models improved memory and learning. Additionally, the loss of HDAC6 rendered neurons resistant to the amyloid-b-mediated decline of mitochondrial trafficking, a common cause of neurodegeneration. In addition, in AD patients, HDAC2 and HDAC3 were found to be mutated in the Nucleus Basalis of Meynert. In addition, the overexpression of HDAC3 reduced dendritic spine density in mice APPswe/PS1dE9.

Many neurodegenerative diseases cause impaired function of the ubiquitin-proteasome system. Neurotoxicity can be caused by HDAC6-dependent protein deacetylation. However, the deacetylating capacity of HDAC6 could also play a role in neuroprotection. Thus, targeting HDAC6's deacetylating activity may be a viable treatment for neurodegenerative diseases.

HDAC6 is a stutterer of neuronal aggregate formation in the early stages of the disease. It regulates autophagy as well as the PI3K/Akt/mTOR axis, which are crucial elements in neurodegenerative disorders. Furthermore, the study demonstrated that HDAC6 increased the viability of cells in PD and AD mice with high levels of misfolded protein accumulation.

The degeneration of asynuclein could be prevented by preventing HDAC6 neurons in the presence of 1-methyl-4-phenylpyridinium. This process is essential for proper degradation of a-synuclein-associated proteins in the brain. Studies on neurodegeneration mediated through a-synuclein have also demonstrated that HDAC6's overexpression stops neuronal cell death in the spinobulbar muscular atrophy model.