Recombinant Human Histone Deacetylase 3 (HDAC3) Protein (His-SUMO)

Name: Recombinant Human Histone Deacetylase 3 (HDAC3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04293P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Histone Deacetylase 3 (HDAC3) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15379
Target Symbol	HDAC3
Synonyms	HD3; HDAC 3; HDAC3; HDAC3_HUMAN; Histone deacetylase 3; RPD3 2; RPD3; RPD3-2; SMAP45
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI
Expression Range	1-428aa
Protein Length	Full Length
Mol. Weight	64.8kDa
Research Area	Transcription
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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), and some other non-histone substrates. 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. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation. Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress. Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner. During the activation phase, promotes the accumulation of ubiquitinated ARNTL/BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and ARNTL/BMAL1. The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver. 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. Interacts with SETD5.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasm, cytosol.
Protein Families	Histone deacetylase family, HD type 1 subfamily
Database References	HGNC: 4854 OMIM: 605166 KEGG: hsa:8841 STRING: 9606.ENSP00000302967 UniGene: PMID: 30053564 in rheumatoid arthritis peripheral blood mononuclear cells, the activity and expression of HDAC3 is decreased, which is accompanied with enhanced histone acetyltransferase activity PMID: 30402512 High HDAC3 expression is closely correlated with ER-negative expression, PR-negative expression, HER2 overexpression, PT stage, and clinical stage of breast tumors. PMID: 29680858 these findings indicate that AKAP12 may be a potential prognostic predictor and therapeutic target for the treatment of colorectal cancer in combination with HDAC3 PMID: 29484387 CHD5 was identified as a direct target of miR-454. CHD5 was downregulated in GC tissues/cell lines and the expresssion of CHD5 inversely correlated with the level of miR-454 in GC tissues. Taken together, these observations indicate that HDAC3 is associated with GC cell growth via the miR-454-mediated targeting of CHD5. PMID: 29115379 DANCR associated with EZH2 and HDAC3 to epigenetically silence lncRNA-LET and then regulated gastric cancer cells migration and invasion. PMID: 28951520 Data show there is allosteric communication between the inositol-binding site and the active sites in histone deacetylases HDAC1 and HDAC3. PMID: 27109927 Results show that proteasomal degradation of HDAC1 and HDAC3 by Vpr counteracts HIV-1 latency to reactivate the viral promoter. PMID: 27550312 the NCOR/HDAC3 complex is a major suppressor of differentiation in rhabdomyosarcoma PMID: 27956629 These findings indicate the importance of developing HDAC3-selective inhibitors, and their combined use with osimertinib, for treating EGFR-mutated lung cancers carrying the BIM deletion polymorphism PMID: 27986747 HDAC3-mediated p53 acetylation and oligomerization is induced by apoptosis caused by delphinidin in prostate cancer cells PMID: 27462923 Knockdown of either Xist or SPEN expression in breast cancer cells suppressed the expression of PHLPP1, a phosphatase in AKT dephosphorylation, and was correlated with increased HDAC3 recruitment to the PHLPP1 promoter. PMID: 27248326 Data show that BRCA2 was required for HDAC2/3 association with acetylated BubR1 in nocodazole (Noc)-arrested cells. PMID: 28985013 Data show that the nuclear HDAC3 and cytoplasmic CDH1 have independent prognostic value in pancreatic cancer and provide targets for prognostic therapeutics. PMID: 26918727 HDAC3 uniquely primes Ucp1 and the thermogenic transcriptional program to maintain a critical capacity for thermogenesis in brown adipose tissue that can be rapidly engaged upon exposure to dangerously cold temperature PMID: 28614293 The low expression of HDAC3 and overexpession of inflammatory cytokines (IL-18, IL-12 and TNF-alpha) in intrahepatic cholestasis of pregnancy may be involved in liver cell apoptosis and in the pathophysiology of the disease. PMID: 28697498 SNP rs14251 was found to be significant (and rs2530223 to be nominally significantly associated with the increasing risk of SCZ susceptibility in Han Chinese individuals, suggesting this gene as a potential genetic modifier for SCZ development. PMID: 27573569 Inhibition of HDAC3 with targeted therapy could benefit treatment of the diseases associated with sGCbeta1 down-regulation and/or deficiency such as cancer and several vascular-related diseases. PMID: 27279362 that histone deacetylase 3 interaction with MeCP2 positively regulates a subset of neuronal genes through FOXO deacetylation, and disruption of HDAC3 contributes to cognitive and social impairment PMID: 27428650 miRNA1236 regulates hypoxia-induced epithelial-mesenchymal transformation and metastasis by repressing HDAC3 and SENP1 expression. PMID: 27177472 class I HDACs (HDAC1, 2, 3 and 8) play a major role in regulating extracellular matrix and Epithelial-mesenchymal transition, whereas class IIa HDACs (HDAC4 and 5) are less effective. PMID: 27420561 Histone deacetylase 3 regulates the inflammatory gene expression programme of rheumatoid arthritis fibroblast-like synoviocytes. PMID: 27457515 Study demonstrated an association of elevated HDAC3 activity and HDAC3 mRNA expression in patients with type 2 diabetes (T2DM) which was positively correlated with proinflammation and insulin resistance. PMID: 27904654 HDAC3 upregulation is associated with hepatocellular carcinoma. PMID: 27342975 High HDAC3 expression is associated with pancreatic cancer. PMID: 26745602 These findings pinpoint that TGF-beta represses miR-30d through a Smad2/3-HDAC3-NCoR repression complex and provide novel insights into a potential target for the treatment of podocyte injury-associated glomerulopathies. PMID: 26432290 Results show the direct regulation of CAGE expression by HDAC3 and that HDAC3-CAGE axis regulates the activation of EGFR. HDAC3 targets CAGE to regulate the tumorigenic potential and angiogenic potential of cancer cells. PMID: 26883907 HDAC3 knockdown or HDAC3 inhibition was associated with simultaneous upregulation of the expression of miR130a and downregulation of the expression of TNF1alpha in peripheral blood mononuclear cells. PMID: 26531724 Data suggest that complexes of HDAC3-H1.3 with NCOR1 and NCOR2/SMRT accumulate on chromatin in synchronized HeLa cells in late G2 phase and mitosis; deacetylation activity of HDAC3 is activated via phosphorylation of Ser-424 by CK2 only in mitosis. PMID: 26663086 this is the first report on the regulation mechanism of SIRT7 gene, in which, HDAC3 collaborated with C/EBPalpha to occupy its responding element in the upstream region of SIRT7 gene and repressed its expression in human cells. PMID: 26704017 Among the class II HDACs, HDAC4 interacted with both MR and HDAC3 after aldosterone stimulation. The nuclear translocation of HDAC4 was mediated by protein kinase A (PKA) and protein phosphatases (PP) PMID: 26305553 miR-335 exerted apoptotic effects and inhibited ubiquitination of HDAC3 in anti-cancer drug-resistant cancer cell lines. miR-335 negatively regulated the invasion, migration, and growth rate of cancer cells. PMID: 25997740 Data suggest, in chronic hepatitis C virus infection, HDAC9 (histone deacetylase 9) induction in liver regulates hepatic gluconeogenesis and systemic insulin resistance via deacetylation of FoxO1 (Forkhead box O 1) and HDAC3 (histone deacetylase 3). PMID: 26420860 These data suggest that HDAC3 indirectly modulates tubulin acetylation PMID: 26450925 The inhibition of the transcriptional activity of BCL9-2 by WWOX and HDAC3 constitutes a new molecular mechanism and provides new insight for a broad range of cancers. PMID: 25678599 These observations suggested that HDAC3 plays an important role in the pathological courses of spinal cord injury by regulating miR-130a expression PMID: 25973054 Time-course analysis revealed that HDAC6, HDAC3, and acetylated histone H3 protein levels are significantly inhibited. PMID: 25307283 Aberrant overexpression of HDACs in basal cells of IPF lungs may contribute to the bronchiolisation process in this disease. Similarly, generation and apoptosis resistance of IPF fibroblasts are mediated by enhanced activity of HDAC enzymes. PMID: 26359372 Sequencing of HDAC3 revealed six single-nucleotide polymorphisms. The G allele of rs2530223 was significantly associated with the number of acute medications/month used and with the number of days/month in which medications were used PMID: 26542778 HDAC3 is an essential target to disrupt HIV-1 latency, and inhibition of HDAC2 may also contribute to the effort to purge and eradicate latent HIV-1 infection. PMID: 25136952 HDAC3 contributes to vasculogenic mimicry in gliomas, possibly through the PI3K/ERK-MMPs-laminin5gamma2 signaling pathway. PMID: 25940092 our results uncovered a mechanism by which PINK1-HDAC3 network mediates p53 inhibitory loop in response to oxidative stress-induced damage. PMID: 25305081 SOX4 interacts with EZH2 and HDAC3 to suppress microRNA-31 in invasive esophageal cancer cells. PMID: 25644061 PML-mediated suppression of IL-6-induced STAT3 activation by disrupting interactions between STAT3 and HDAC3. PMID: 25892518 c-Myc contributes to the epigenetic regulation of HPP1 via the dominant recruitment of HDAC3. PMID: 24919179 Data point to HDAC3 as a potential drug target for preserving beta cells against lipotoxicity in diabetes. PMID: 25610877 Htt aggregates impair nuclear proteasome activity through the inhibition of HDAC3 PMID: 25380050 These results demonstrate that mutant H3K27M can be specifically identified with high specificity and sensitivity using an H3K27M antibody and immunohistochemistry to detect high-grade astrocytomas. PMID: 25200321 Findings reveal strong expression of HDAC3 in patients with pancreatic cancer and suggest that HDAC3 participates in the pathogenesis and progression of pancreatic cancer. PMID: 25070540 dysbindin-1 formed a protein complex with HDAC3 in human neuroblastoma cells PMID: 25196196

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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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