HDAC8 Antibody

Code CSB-PA010244ESR1HU
Size US$166
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  • Immunohistochemistry of paraffin-embedded human pancreatic tissue using CSB-PA010244ESR1HU at dilution of 1:100

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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) HDAC8 Polyclonal antibody
Uniprot No.
Target Names
Alternative Names
CDA07 antibody; CDLS5 antibody; HD 8 antibody; HD8 antibody; HDAC 8 antibody; Hdac8 antibody; HDAC8_HUMAN antibody; HDACL 1 antibody; HDACL1 antibody; Histone deacetylase 8 antibody; Histone deacetylase like 1 antibody; MRXS6 antibody; RPD 3 antibody; RPD3 antibody; WTS antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Histone deacetylase 8 protein (1-377AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Form
Liquid
Tested Applications
ELISA, IHC
Recommended Dilution
Application Recommended Dilution
IHC 1:20-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility.
Gene References into Functions
  1. we report a de novo missense HDAC8 mutation that causes overlapping features of Rett-related disorder and Cornelia de Lange syndrome. It is possible that this HDAC8 mutation may be harmful via MECP recruitment, and may consequently cause Rett-related disorder PMID: 29519750
  2. this study identifies additional underlying causes of CdLS, describes the first instance of a somatic HDAC8 mutation in an individual with CdLS features and provides insight into the molecular bases of HDAC8 deletions. PMID: 29279609
  3. The present study identified a novel missense mutation (c.806T>G, p.I269R) in the HDAC8 gene leading to Cornelia de Lange Syndrome (CdLS), which not only provided strong evidence for diagnosis in this present patient, but also expanded the spectrum of pathogenic mutations for CdLS. PMID: 29991052
  4. chemical crosslinking approach identified novel HDAC8-specific substrates with high catalytic efficiency, thus presenting a general strategy for unbiased deacetylase substrate discovery PMID: 29035536
  5. Co2+ and Zn2+ are the most active metals in HDAC8 biocatalysis, followed by Fe2+, and Mn2+ and Mg2+ to be the least active. PMID: 26996235
  6. MSC from MPN have higher expression of HDAC8 than normal ones, and the inhibition of HDAC8 expression by its specific inhibitor decreases the capacity of the stroma to support hematopoietic cells from MPN patients, suggesting that HDAC8 may be a potential therapeutic target in this setting. PMID: 28390197
  7. This study for the first time demonstrated that HDAC8 activity determines susceptibility to cell cycle arrest induced by Anthrax Lethal Toxin, through regulating the PI3K-PTEN-AKT signaling axis. PMID: 28509866
  8. AHR regulated cell proliferation and tumorigenesis by directly targeting and activating HDAC8 expression in hepatocellular carcinoma cells. PMID: 27283490
  9. The Epac-Rap1-Akt pathway mediates cAMP signaling-induced inhibition of JNK-dependent HDAC8 degradation, and the resulting HDAC8 increase augments cisplatin-induced apoptosis by repressing TIPRL expression in H1299 lung cancer cells. PMID: 28232663
  10. The X-ray crystal structure of HDAC8 complexed with inhibitor confirms the formation of a unique subpocket in HDAC8. PMID: 27374062
  11. These data provide support for the hypothesis that HDAC8 may undergo metal switching in vivo that, in turn, may regulate its activity. However, future studies are needed to explore the identity of the metal ion bound to HDAC8 in cells under varied conditions PMID: 28937750
  12. The study reports the crystal structure of the HDAC8-trapoxin A complex at 1.24 A resolution, revealing that the ketone moiety of l-Aoe undergoes nucleophilic attack to form a zinc-bound tetrahedral gem-diolate that mimics the tetrahedral intermediate and its flanking transition states in catalysis. PMID: 28846375
  13. The findings suggest that miR-455-3p plays a critical role during chondrogenesis by directly targeting HDAC2/8 and promoting histone H3 acetylation. PMID: 27638301
  14. 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
  15. Enzymological, biophysical, and structural studies of Cornelia de Lange Syndrome HDAC8 protein mutants have yielded critical insight on compromised catalysis in vitro. Most CdLS HDAC8 mutations trigger structural changes that directly or indirectly impact substrate binding and catalysis. PMID: 27576763
  16. 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
  17. Losses of catalytic efficiency in histone deacetylase 8 (HDAC8) are observed for G304A and G305A mutations. PMID: 27933794
  18. Data suggest sequencing of histone deacetylase 8 protein (HDAC8) as an indispensable part of the routine molecular diagnostic for patients with Cornelia de Lange syndrome (CdLS) or CdLS-overlapping features. PMID: 26671848
  19. HDAC8 were overexpressed in oral squamous cell carcinoma tissues, mainly localized in the cytoplasm. PMID: 28004115
  20. Study reveals that HDAC8 can bind and catalyze deacetylation of many acetylated peptides with sequences corresponding to cellular, non-histone proteins, thereby opening a new window to the functional role of HDAC8 in cells. PMID: 26933971
  21. Findings suggest the therapeutic potential of histone deacetylase 8 histone (HDAC8)inhibition to suppress Notch1 signaling in breast cancer. PMID: 26625202
  22. Data show that histone deacetylase 8 (HDAC8) inhibition led to accumulation of acetylated-SMC3 protein but had no influence on the transcription of estrogen-responsive genes. PMID: 27072133
  23. Results provide direct evidence that potential KDAC8 substrates can be directly deacetylated by KDAC8. PMID: 26402585
  24. study elucidates an HDAC8-mediated p53-inactivating mechanism promoting leukemia stem cells activity PMID: 26387755
  25. Studies indicate that histone deacetylase 8 protein (HDAC8) aberrantly deacetylates p53 protein and promotes leukemia stem cells (LSCs) transformation and maintenance. PMID: 26923266
  26. Our data exhibited an important role of HDAC8 in promoting gastric cancer tumorigenesis and identify this HDAC8 as a potential therapeutic target for the treatment of gastric cancer. PMID: 26412386
  27. The H143A and H142A/H143A mutants exhibit activity that is >80000-fold lower than that of wild-type HDAC8; the buried D176N and D176A mutants have significant catalytic effects, with more subtle effects caused by D183N and D183A PMID: 26806311
  28. cAMP signaling increases HDAC8 protein levels by reducing JNK-mediated autophagy and ubiquitin-proteasome-dependent degradation of the HDAC8 protein in H1299 lung cancer cells. PMID: 26792731
  29. HDAC8i induced cell growth inhibition and marked S-phase cell cycle arrest in human and murine-derived MPNST cells PMID: 26200462
  30. Report the preparation and biophysical evaluation of five HDAC8 mutants: P91L, G117E, H180R, D233G, and G304R. Additionally, the double mutants D233G-Y306F and P91L-Y306F were prepared to enable cocrystallization of intact enzyme-substrate complexes. PMID: 26463496
  31. HDAC8 was increased in BRAF-mutated melanoma. Increased cytoplasmic HDAC8 immunoreactivity was independently associated with an improved survival from both diagnosis of primary melanoma and from first detection of stage IV disease to melanoma death PMID: 25836739
  32. findings show how HDAC8 drives nonalcoholic fatty liver disease-associated hepatocarcinogenesis PMID: 26383163
  33. Data reveal a role for miR-21-3p in regulating HDAC8 expression and Akt/Gsk3beta pathway in cardiac hypertrophy. PMID: 25504627
  34. Studied the kinetics, thermodynamics, and selectivity of Zn(II) and Fe(II) binding to HDAC8. PMID: 25516458
  35. HDAC8 X-ray crystal structures reveal that each Cornelia de Lange syndrome mutation causes local structural changes that compromise catalysis and/or thermostability. PMID: 25075551
  36. report the X-ray crystal structures of HDAC8 complexed with three synthetic analogues of Largazole in which the depsipeptide ester is replaced with a rigid amide linkage PMID: 25793284
  37. On the corresponding BMF gene promoter, loss of HDAC8 was associated with signal transducer and activator of transcription 3 (STAT3)/specificity protein 3 (Sp3) transcription factor exchange and recruitment of p300. PMID: 25321483
  38. Our mechanistic and cellular studies on HDAC8 activation have the potential to provide insight into the development of novel anticancer drugs. PMID: 25605725
  39. Deregulation of HDAC8 is frequent in urothelial cancer, but neither specific pharmacological inhibition nor siRNA-mediated knockdown of HDAC8 impaired viability of urothelial cancer cell lines in a therapeutic useful manner. PMID: 25011684
  40. histone deacetylase 8 inhibition reduces gene expression and production of proinflammatory cytokines in vitro and in vivo PMID: 25451941
  41. detailed thermodynamic studies of the binding of structurally similar ligands, which differed with respect to the "cap", "linker", and "metal-binding" regions of the suberoylanilide hydroxamic acid pharmacophore, to HDAC8 PMID: 25407689
  42. Loss-of-function mutations in HDAC8 cause a range of overlapping phenotypic spectrum of Cornelia de Lange syndrome-like feature. PMID: 24403048
  43. In response to contractile stimulation, HDAC8 may mediate cortactin deacetylation, which subsequently promotes actin filament polymerization and smooth muscle contraction. PMID: 24920679
  44. DEC1 coordinates with HDAC8 to differentially regulate TAp73 and DeltaNp73 expression. PMID: 24404147
  45. Data indicate prominent changes in urothelial cancer cell lines (UCC) were HDAC2 and/or HDAC8 up-regulation. PMID: 22944197
  46. Using molecular dynamics simulations the study found a mechanism whereby the interactions and dynamics of two loops tune the configuration of functionally important residues of HDAC8 and could therefore influence the activity of the enzyme. PMID: 24171457
  47. HDAC8 isoverexpressed in hepatocellular carcinoma; knockdown suppresses tumor growth and enhances apoptosis PMID: 24077923
  48. HDAC8 plays an important role in the modulation of SOCS1 and SOCS3 by curcumin. PMID: 23430957
  49. SOX4 is a direct target gene of FRA-2 and induces expression of HDAC8 in adult T-cell leukemia/lymphoma. PMID: 23482931
  50. Data indicate that knockdown of HDAC8 resulted in the increased expression of SOCS1 and SOCS3, and overexpression of SOCS1 and SOCS3 significantly inhibited cell growth and suppressed JAK2/STAT signaling. PMID: 23111066

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Involvement in disease
Cornelia de Lange syndrome 5 (CDLS5); Wilson-Turner X-linked mental retardation syndrome (WTS)
Subcellular Location
Nucleus. Cytoplasm. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation.
Protein Families
Histone deacetylase family, HD type 1 subfamily
Tissue Specificity
Weakly expressed in most tissues. Expressed at higher level in heart, brain, kidney and pancreas and also in liver, lung, placenta, prostate and kidney.
Database Links

HGNC: 13315

OMIM: 300269

KEGG: hsa:55869

STRING: 9606.ENSP00000362674

UniGene: Hs.310536

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