Recombinant Human HDAC7 Protein

Name: Recombinant Human HDAC7 Protein
Brand: Beta LifeScience
SKU: BL-0233SG
Availability: InStock

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_015401
Synonym	HD7A; HDAC7A; DKFZp586J0917; FLJ99588
Background	HDAC7 or Histone deacetylase 7 belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. The protein encoded by HDAC7 gene has sequence homology to members of the histone deacetylase family whose protein promotes repression mediated via the transcriptional co-repressor SMRT (1). HDAC7 interacts with beta-catenin keeping endothelial cells in a low proliferation stage. HDAC7 regulates NUR77 and apoptosis in developing thymocytes (2). HDAC7 is expressed in human osteoarthritis that contributes to cartilage degradation via promoting MMP-13 gene expression.
Description	Recombinant human HDAC7 (501-end) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	501a.a.-end
Molecular Weight	~80 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 HDAC7 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 by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3. Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding. In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response.
Subcellular Location	Nucleus. Cytoplasm. Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation.
Protein Families	Histone deacetylase family, HD type 2 subfamily
Database References	HGNC: 14067 OMIM: 606542 KEGG: hsa:51564 STRING: 9606.ENSP00000080059 UniGene: PMID: 29071516 Study suggests that Hdac7 promotes lung tumorigenesis by inhibiting Stat3 activation via deacetylating Stat3. Also, high HDAC7 mRNA level was found to be correlated with poor prognosis of human lung cancer patients. PMID: 29126425 High HDAC7 expression is associated with distant metastasis in gastric cancer. PMID: 28299580 silencing induces apoptosis and autophagy in salivary mucoepidermoid carcinoma cells PMID: 28178760 Study found increased HDAC7 expression in human pancreatic islets from type 2 diabetic compared with non-diabetic donors. HDAC7 expression correlated negatively with insulin secretion in human islets. PMID: 27796421 silencing HDAC7 can reset the tumor suppressor activity of STAT3, independently of the EGFR/PTEN/TP53 background of the glioblastoma. PMID: 26853466 This study demonstrated a simple and straightforward method of quantifying proneural/mesenchymal markers in glioblastoma. Of note, HDAC7 expression might be a novel therapeutic target in glioblastoma treatment. PMID: 26272600 identify a new target of ROCK signaling via myosin phosphatase subunit (MYPT1) and histone deacetylase (HDAC7) at the nuclear level PMID: 25511694 Study identifies the miR-34a-HDAC1/HDAC7-HSP70 K246 axis as a novel molecular signature predictive of therapy resistance. PMID: 25173798 The transcriptional function of HCS was shown by in vitro pull down and in vivo co-immunoprecipitation assays to depend on its interaction with the histone deacetylases HDAC1, HDAC2 and HDAC7 PMID: 24239178 endothelial progenitor cells involved in the angiogenesis might be controlled by VEGF-PKD1-HDAC7 axis, which regulates the EPCs angiogenesis by PKD1, but not the ERK and PI3K pathway PMID: 24189120 Histone deacetylase 7 promotes Toll-like receptor 4-dependent proinflammatory gene expression in macrophages. PMID: 23853092 Expression of JHDM2A was significantly increased but HDAC2, HDAC7, and SUV39H2 were significantly down-regulated in Systemic Sclerosis B cells relative to controls PMID: 23891737 Authors identified acetyltransferase p300 and deacetylase HDAC7 as enzymes modulating human T cell leukemia virus type 1 Tax protein acetylation. PMID: 23880157 Our findings uncover a novel role for HDAC7 in maintaining the identity of a particular cell type by silencing lineage-inappropriate genes. PMID: 23696748 VEGF and PKC promote degradation-independent protein ubiquitination of FLNB to control intracellular trafficking of HDAC7. PMID: 23401860 demonstrated for the first time that AKAP12 tumor/angiogenesis suppressor gene is an epigenetic target of HDAC7 PMID: 22584896 HDAC7 reduction in COPD causes a defect of HIF-1alpha induction response to hypoxia with impaired VEGF gene expression. This poor cellular adaptation might play a role in the pathogenesis of COPD. PMID: 22172637 The expression of HDAC7 protein plays an important role in the apoptosis and vascular tubulogenesis of hepatocellular carcinoma by the upregulation of p21 and HIF-1alpha and the downregulation of cyclin E and MMP10. PMID: 20693714 Data demonstrate that Mitf and HDAC7 interact in RAW 264 cells and osteoclasts. The transcriptional activity of Mitf is repressed by HDAC7. PMID: 21324898 Findings highlight for the first time an unrecognized link between HDAC7 and c-Myc and offer a novel mechanistic insight into the contribution of HDAC7 to tumor progression. PMID: 21120446 Elevated HDAC7 expression in human osteoarthritis may contribute to cartilage degradation via promoting MMP-13 gene expression. PMID: 19784544 HDAC7 interacts with beta-catenin keeping endothelial cells in a low proliferation stage. PMID: 20224040 these data implicate a novel role for HDAC7 and FoxA1 in estrogen repression of RPRM. PMID: 19917725 histone deacetylase 7 has a role in function of misfolded CFTR in cystic fibrosis PMID: 19966789 HDAC7 phosphorylation is mediated by calcium/calmodulin-dependent kinase I, which also promotes the association of HDAC7 with 14-3-3 and stabilizes HDAC7 PMID: 15166223 HDAC7 increased transcriptional activity of HIF-1alpha through the formation of a complex with HIF-1alpha, HDAC7, and p300 PMID: 15280364 HDAC7 is sequestered to the cytoplasm from mitochondrial and nuclear compartments upon initiation of apoptosis PMID: 15364908 Data indicate that protein kinase D1 regulates the expression of Nur77 during thymocyte activation at least in part by phosphorylating HDAC7. PMID: 15623513 a mutant of HDAC7 specifically deficient in phosphorylation by protein kinase D, inhibits T cell receptor-mediated apoptosis of T cell hybridomas PMID: 15738054 These results identify HDAC7 as a novel Androgen receptor corepressor whose subcellular and subnuclear compartmentalization can be regulated in an androgen-selective manner. PMID: 16860317 Class IIa histone deacetylases (HDACs) are subjected to signal-independent nuclear export that relies on their constitutive phosphorylation. EMK and C-TAK1, are identified as regulators of this process. PMID: 16980613 HDAC7 is a key modulator of endothelial cell migration and angiogenesis, at least in part, by regulating platelet-derived growth factor-B (PDGF-B) and its receptor PDGFR-beta gene expression. PMID: 17947801 Histone deacetylase 7 associates with Runx2 and represses its activity during osteoblast maturation in a deacetylation-independent manner PMID: 17997710 HDAC7 has a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity PMID: 18285338 PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. PMID: 18339811 Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function. PMID: 18458084 PML sequesters HDAC7 to relieve repression and up-regulate gene expression PMID: 18463162 The data showed alteration of HDACs gene expression in pancreatic cancer. Increased expression of HDAC7 discriminates PA from other pancreatic tumors. PMID: 18506539 These results demonstrate that phosphorylation of HDAC7 serves as a molecular switch to mediate VEGF signaling and endothelial function. PMID: 18509061 VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating MT-MMP1/MMP10 expression and angiogenesis. PMID: 18617643 These results demonstrate a novel function of HDAC7 and provide a regulatory mechanism of PML sumoylation. PMID: 18625722 recent developments in the crystal structure analysis of human HDAC4, HDAC7, and HDAC8 recent developments in the crystal structure analysis of human HDAC4, HDAC7, and HDAC8 [REVIEW] PMID: 19355988 Characterization of the mouse HDAC7 ortholog. PMID: 10640276 Interaction of HDAC7 with MEF2D is essential for repression of Nur77. PMID: 12753745

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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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