Recombinant Human HDAC4 Protein

Name: Recombinant Human HDAC4 Protein
Brand: Beta LifeScience
SKU: BL-0249SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_006037
Synonym	HA6116; HD4; HDAC-A; HDACA; KIAA0288
Background	HDAC4 or Histone deacetylase 4 belongs to class II of the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex that represses transcription when tethered to a promoter. HDAC4 does not bind DNA directly, but through transcription factors MEF2C and MEF2D. Binding of the N terminus of HDAC4 to MEF2C represses MEF2C transcription activity. The catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor NCOR2. Suppression of HDAC4 binding to NCOR2 and to HDAC3 results in loss of enzymatic activity associated with HDAC4.
Description	Recombinant human HDAC4 (101-end) was produced by baculovirus in Sf9 insect cells using an C-terminal GST tag. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	101a.a.-end
Molecular Weight	155 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human HDAC4 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	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. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.
Subcellular Location	Nucleus. Cytoplasm.
Protein Families	Histone deacetylase family, HD type 2 subfamily
Database References	HGNC: 14063 OMIM: 600430 KEGG: hsa:9759 STRING: 9606.ENSP00000264606 UniGene: PMID: 30226605 MiR-22 was up-regulated in CD4+ T cells in peripheral blood and intestinal mucosa tissues of inflammatory intestinal disease patients, which could promote Th17 cell differentiation via targeting HDAC4 to be involved in inflammatory intestinal disease progression PMID: 29880327 HO-1 plays a key role in protecting tumor cells from apoptosis, in a process that involves Smad7 and HDAC4/5 in apoptosis of B-ALL cells PMID: 29886060 Auithors found no significant association between the previously implicated CpG in HDAC4 and either AN or BN. We found that three CpGs were nominally associated with AN (P=0.02-0.03); the largest difference was a 9% hypermethylation in AN. PMID: 29256967 our results demonstrated that MIAT competitively binds to miR-29a-3p and consequently upregulates the expression of HDAC4, which is a downstream target of miR-29a-3p. In conclusion, the present study highlighted the involvement of the MIAT/miR-29a-3p/HDAC4 axis in the development of Gastric cancer (GC), which provided potential diagnostic and therapeutic targets for GC. PMID: 29039602 miR-29a regulated osteogenesis of the subchondral mesenchymal stem cells through modulation of HDAC4 and Wnt3a. PMID: 28884332 Results show that HDAC4 promoter methylation is inversely associated with arachidonic acid post-prandially in adult males. PMID: 27181711 The cytoplasmic location and function of HDAC4 is controlled by the activity of salt-inducible kinase (SIK). These results establish a cytoplasmic role for HDAC4 and identify HDAC4, SIK, and ENIGMA as mediators of vascular calcification. PMID: 28588072 Strong correlation has been proved between the expression levels of HDAC4 and SIRT6. PMID: 27766571 HDAC4 regulates thimerosal-induced cell death in neurons and that treatment with MC1568 prevents thimerosal-induced activation of caspase-3 in the rat prefrontal cortex. PMID: 27660204 HDAC4 promotes proliferation and G1/S cell cycle progression in esophageal carcinoma cells by inhibiting CDK inhibitors p21 and p27 and up-regulating CDK2/4 and CDK-dependent Rb phosphorylation. HDAC4 also enhances ESCC cell migration. Furthermore, HDAC4 positively regulates epithelial-mesenchymal transition (EMT) by increasing the expression of Vimentin and decreasing the expression of E-Cadherin/alpha-Catenin. PMID: 27295551 level of myotubes MTM1 mutations do not dramatically affect calcium homeostasis and calcium release mediated through the ryanodine receptor 1, though they do affect myotube size and nuclear content..mature muscles such as those obtained from patient muscle biopsies exhibit a significant decrease in expression of the ryanodine receptor 1, a decrease in muscle-specific microRNAs and a considerable up-regulation of HDAC4. PMID: 28007904 7-amino-4-methylcoumarin did not affect acetyllysine preference in a multiply acetylated substrate. In contrast, AMC significantly enhanced KDAC6 substrate affinity, greatly reduced Sirt1 activity, eliminated the substrate sequence specificity of KDAC4, and had no consistent effect with KDAC8 substrates. PMID: 28749131 Suggest that HDAC4 and HDAC6 are guardians of irradiation-induced DNA damage and stemness, thus promoting radioresistance in glioblastoma cells. PMID: 28342984 TGF-beta1 increases NADPH oxidase 4 (NOX4) mRNA and protein expression in normal human lung fibroblasts (NHLFs) and causes nuclear export of HDAC4. PMID: 28336812 elevated HO-1 produced less reactive oxygen species, resulting in nuclear localization of HDAC4 and miR-206 repression. PMID: 27488535 Results show that HDAC4 is a direct target of miR-29b in multiple myeloma cells and its high mRNA expression inversely correlates with miR-29b levels in multiple myeloma samples. PMID: 27196750 Collectively, we suggest that VSV treatment will be a useful therapeutic strategy for HCV-infected hepatocellular carcinoma cells because HCV core protein suppresses the anti-viral threshold by down-regulation of the STAT1-HDAC4 signaling axis. PMID: 27150631 In osteoarthritis (OA) chondrocytes, hydrostatic pressure (HP) restores the expression levels of some miRNAs, downregulates MMP-13, ADAMTS-5, and HDAC-4, and modulates the Wnt/beta-catenin pathway activation. PMID: 28085114 HDAC4 is a target gene of miR-140 and is involved in miR-140-mediated suppression of osteosarcoma cells. PMID: 27624383 HDAC4 increases endogenous SIRT1 expression by enhancing its sumoylation modification levels PMID: 26414199 downregulated in sustained virologic responders compared to the spontaneous clearers of Hepatitis C PMID: 26568966 we demonstrate that nuclear HDAC4 is a key regulator promoting the progressive epithelial ovarian cancer on fibrillar collagen matrices PMID: 26572940 HDAC4 destabilizes MAP1S, suppresses autophagy flux and promotes the accumulation of mHTT aggregates. PMID: 26540094 Mechanical compression regulates chondrocyte gene expression through HDAC4 relocation from the cell's cytoplasm to the nucleus via PP2A-dependent HDAC4 dephosphorylation. PMID: 27106144 Elevated HDAC-4 expression in Pancreatic Adenocarcinoma was significantly associated with the absence of organ metastases and borderline with the absence of lymph node metastases and tumor proliferative capacity. PMID: 26502922 Over-expression of HDAC4 suppressed the transcription of genes involved in energy expenditure in a SIRT1-dependent manner. In contrast, HDAC4 knockdown/inhibition neutralized the effect of IFN-gamma on cellular metabolism by normalizing SIRT1 expression PMID: 26619800 HDAC4-RelB-p52 complex maintains repressive chromatin around proapoptotic genes Bim and BMF and regulates multiple myeloma survival and growth PMID: 26455434 Results show that overexpression of miR10b in ER-positive breast cancer cell lines led to increased resistance to tamoxifen and HDAC4 was identified as its direct target. MiR10b-HDAC4 nexus may be one of the molecular mechanism of tamoxifen resistance. PMID: 26206152 the pro-inflammatory role of miR-22 in emphysema has revealed that HDAC4 specifically regulated smoking-related lung inflammation and TH17 responses PMID: 26437241 This study leads to the discovery of a novel molecular mechanism in which the miRNA miR-125a-5p suppresses HDAC4 expression PMID: 25504437 Dysregulation of HDAC4 and/or HDAC6 could play a role in the pathogenesis of Frontotemporal lobar degeneration-tau associated with Pick bodies PMID: 24861260 Idiopathic pulmonary fibrosis fibroblast interaction with polymerized type I collagen results in an aberrant PP2A/HDAC4 axis, which suppresses miR-29, causing a pathologic increase in type I collagen expression. PMID: 25612003 Decreased HDAC4 partially contributes to the pathogenesis of osteoarthritis cartilage degeneration. PMID: 25424126 Data suggeet the potential clinical use of histone deacetylase 4 (HDAC4) inhibitors in combination with docetaxel for the treatment of gastric cancer. PMID: 25091122 observations suggested that some other candidate genes for neuronal development exist in the telomeric region of HDAC4 PMID: 25329715 Increased expression of HDAC4 was found in cartilage from knee osteoarthritis patients. PMID: 25515592 Haploinsufficiency of HDAC4 does not cause intellectual disability in all affected individuals. PMID: 24715439 We demonstrated that HDAC4 promotes gastric cancer cell progression mediated through the repression of p21. PMID: 24896240 expression of the proliferation marker Ki-67 exhibited a similar tendency with that of HDAC4 PMID: 25103231 Thus, HDAC4 contributes to podocyte injury and is one of critical components of a signal transduction pathway that links renal injury to autophagy in diabetic nephropathy. PMID: 24717296 novel HDAC1/4/miR-200b/E2F3 signaling contributes to chemoresistance of human lung adenocarcinoma cells PMID: 24830600 Data show that HDAC4 plays global roles in the regulation of gene transcription, cell growth, survival and proliferation, and their aberrant expression or activity leads to cancer development. PMID: 24579951 Results show that HDAC4 is the Upstream 6PGD Deacetylase that removes acetylation from both K76 and K294 sites. PMID: 25042803 HDAC4 played an important role in the regulation of Endoplasmic reticulum stress-induced apoptosis through interacting with ATF4 and inhibiting its transcriptional activity. PMID: 24308964 The expression pattern of HDAC4 in obese subjects before and after physical exercise, its correlation with various physical, clinical and metabolic parameters and its inhibitory effect on NF-kappaB are suggestive of a protective role against obesity. PMID: 24086512 EZH2 and HDAC4 represent mutually exclusive epigenetic pathways across human cancers PMID: 24079712 Increased HDAC4 expression is associated with chemoresistance in breast cancer. PMID: 23817620 analysis of eight members across four generations identified a missense mutation in the histone deacetylase 4 (HDAC4) gene that segregated with eating disorders PMID: 24216484 Correlation studies depicted two distinct groups of soft tissue sarcomas: one in which MEF2 repression correlates with PTEN downregulation and a second group in which MEF2 repression correlates with HDAC4 levels. PMID: 24043307

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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