HDAC8 Recombinant Monoclonal Antibody

Code: CSB-RA215311A0HU

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Size:

50μl100μl

US$210

Quantity:

Species Reactivity: Human, Mouse

Application: ELISA, WB, IHC, IF, FC

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Product Details
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Target Background

Product Details

Uniprot NO.

Q9BY41

Target Names

HDAC8

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

Species Reactivity

Human, Mouse

Immunogen

A synthesized peptide derived from human HDAC8

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

19A7

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Western Blotting(WB) Protocol Immunohistochemistry (IHC) Protocol Immunofluorescence (IF) Protocol Flow Cytometry (FC) Protocol

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:2000
IHC	1:50-1:200
IF	1:50-1:200
FC	1:50-1:200

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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

Antibody FAQs

Images

Western Blot
Positive WB detected in: SH-SY5Y whole cell lysate(20µg), Hela whole cell lysate(20µg), U-251MG whole cell lysate(20µg), JURKAT whole cell lysate(20µg), HEK293 whole cell lysate(20µg),A549 whole cell lysate(20µg), Mouse liver tissue lysate(20µg)
All lanes: HDAC8 antibody at 1:1000
Secondary
Goat polyclonal to rabbit IgG at 1/40000 dilution
Predicted band size: 42 kDa
Observed band size: 45 kDa
Exposure time：1min
IHC image of CSB-RA215311A0HU diluted at 1:100 and staining in paraffin-embedded human ovarian cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
IHC image of CSB-RA215311A0HU diluted at 1:100 and staining in paraffin-embedded human tonsil tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
Immunofluorescence staining of Hela cell with CSB-RA215311A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Overlay Peak curve showing HepG2 cells stained with CSB-RA215311A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*10⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/1*10⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.

Description

HDAC8 is a class I histone deacetylase that plays a critical role in chromatin remodeling and transcriptional regulation. Unlike other class I HDACs, HDAC8 exhibits unique substrate specificity and has emerged as a significant target in cancer research, with particular relevance to neuroblastoma, T-cell lymphoma, and other malignancies. Its involvement in cell proliferation and differentiation pathways makes it an important focus for both basic epigenetic studies and therapeutic development.

This recombinant monoclonal antibody, produced using rabbit host cells and the 19A7 clone, offers the consistency and reproducibility that demanding research applications require. Because the antibody sequence is defined and production is cell-based, you can expect reliable lot-to-lot performance across long-term studies and collaborative projects where experimental continuity matters.

Validation data demonstrates robust performance across multiple platforms. Western blot analysis detects HDAC8 in a range of human cell lines including SH-SY5Y, HeLa, U-251MG, Jurkat, HEK293, and A549, as well as mouse liver tissue, confirming cross-species reactivity between human and mouse samples. The observed band at approximately 45 kDa runs slightly higher than the predicted 42 kDa molecular weight, which likely reflects post-translational modifications such as phosphorylation or acetylation known to occur on this protein. Immunohistochemistry staining has been validated in human ovarian cancer and tonsil tissue sections, while immunofluorescence studies in HeLa cells reveal the expected nuclear localization pattern. Flow cytometry analysis in HepG2 cells further demonstrates the antibody's versatility for single-cell applications.

This antibody serves researchers investigating epigenetic mechanisms, cancer biology, and HDAC inhibitor development, providing a dependable tool for characterizing HDAC8 expression and localization across diverse experimental systems.

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Target Background

Function(From Uniprot)

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

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
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
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
chemical crosslinking approach identified novel HDAC8-specific substrates with high catalytic efficiency, thus presenting a general strategy for unbiased deacetylase substrate discovery PMID:29035536
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
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
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
AHR regulated cell proliferation and tumorigenesis by directly targeting and activating HDAC8 expression in hepatocellular carcinoma cells. PMID:27283490
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
The X-ray crystal structure of HDAC8 complexed with inhibitor confirms the formation of a unique subpocket in HDAC8. PMID:27374062
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
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
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
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
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
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
Losses of catalytic efficiency in histone deacetylase 8 (HDAC8) are observed for G304A and G305A mutations. PMID:27933794
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
HDAC8 were overexpressed in oral squamous cell carcinoma tissues, mainly localized in the cytoplasm. PMID:28004115
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
Findings suggest the therapeutic potential of histone deacetylase 8 histone (HDAC8)inhibition to suppress Notch1 signaling in breast cancer. PMID:26625202
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
Results provide direct evidence that potential KDAC8 substrates can be directly deacetylated by KDAC8. PMID:26402585
study elucidates an HDAC8-mediated p53-inactivating mechanism promoting leukemia stem cells activity PMID:26387755
Studies indicate that histone deacetylase 8 protein (HDAC8) aberrantly deacetylates p53 protein and promotes leukemia stem cells (LSCs) transformation and maintenance. PMID:26923266
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
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
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
HDAC8i induced cell growth inhibition and marked S-phase cell cycle arrest in human and murine-derived MPNST cells PMID:26200462
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
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
findings show how HDAC8 drives nonalcoholic fatty liver disease-associated hepatocarcinogenesis PMID:26383163
Data reveal a role for miR-21-3p in regulating HDAC8 expression and Akt/Gsk3beta pathway in cardiac hypertrophy. PMID:25504627
Studied the kinetics, thermodynamics, and selectivity of Zn(II) and Fe(II) binding to HDAC8. PMID:25516458
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
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
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
Our mechanistic and cellular studies on HDAC8 activation have the potential to provide insight into the development of novel anticancer drugs. PMID:25605725
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
histone deacetylase 8 inhibition reduces gene expression and production of proinflammatory cytokines in vitro and in vivo PMID:25451941
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
Loss-of-function mutations in HDAC8 cause a range of overlapping phenotypic spectrum of Cornelia de Lange syndrome-like feature. PMID:24403048
In response to contractile stimulation, HDAC8 may mediate cortactin deacetylation, which subsequently promotes actin filament polymerization and smooth muscle contraction. PMID:24920679
DEC1 coordinates with HDAC8 to differentially regulate TAp73 and DeltaNp73 expression. PMID:24404147
Data indicate prominent changes in urothelial cancer cell lines (UCC) were HDAC2 and/or HDAC8 up-regulation. PMID:22944197
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
HDAC8 isoverexpressed in hepatocellular carcinoma; knockdown suppresses tumor growth and enhances apoptosis PMID:24077923
HDAC8 plays an important role in the modulation of SOCS1 and SOCS3 by curcumin. PMID:23430957
SOX4 is a direct target gene of FRA-2 and induces expression of HDAC8 in adult T-cell leukemia/lymphoma. PMID:23482931
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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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

UNIGENE: Hs.310536

KEGG: hsa:55869

STRING: 9606.ENSP00000362674

OMIM: 300269

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