H2AFZ Antibody

Code CSB-PA010100GA01HU
Size $600
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Product Details

Uniprot No.
Target Names
Alternative Names
H2A histone family member Z antibody; H2A.z antibody; H2A/z antibody; H2afz antibody; H2AZ antibody; H2AZ_HUMAN antibody; Histone H2A.Z antibody; MGC117173 antibody
Raised in
Species Reactivity
Human H2AFZ
Immunogen Species
Homo sapiens (Human)
Purification Method
Antigen Affinity purified
It differs from different batches. Please contact us to confirm it.
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
Tested Applications
Troubleshooting and FAQs
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

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.
Gene References into Functions
  1. H2A.Z associates with epigenetic gene activation in prostate cancer.Acetylated H2A.Z role in activation of newly formed enhancers in prostate cancer. PMID: 29116202
  2. The present study demonstrated that H2A.Z is overexpressed in ICC and expression of H2A.Z correlated with poor prognosis in patients with ICC. H2A.Z regulated cell proliferation in vitro and in vivo via H2A.Z/S-phase kinase-associated protein 2/p27/p21 signaling. PMID: 29532867
  3. study identifies GAS41 as a histone acetylation reader that promotes histone H2A.Z deposition in non-small cell lung cancer. PMID: 29437725
  4. Two possible modes of pioneering associated with combinations of H2A.Z and p300/CBP at nucleosome-occupied enhancers. PMID: 28301306
  5. Results indicate that accumulation of H2A.Z within repressed genes can also be a consequence of the repression of gene transcription rather than an active mechanism required to establish the repression. PMID: 29036442
  6. Findings suggest the oncogenic potential of H2A.Z.1 in liver tumorigenesis and that it plays established role in accelerating cell cycle transition and EMT during hepatocarcinogenesis. PMID: 26863632
  7. Crystal structure results show that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome. PMID: 27358293
  8. Monoubiquitination of histone H2B blocks eviction of histone variant H2A.Z from inducible enhancers. PMID: 27692985
  9. Thus, PWWP2A is a novel H2A.Z-specific multivalent chromatin binder providing a surprising link between H2A.Z, chromosome segregation, and organ development. PMID: 28645917
  10. SMYD3-mediated H2A.Z.1K101 dimethylation activates cyclin A1 expression and contributes to driving the proliferation of breast cancer cells. PMID: 27569210
  11. Results suggest that the N-terminal tail of H2A.Z makes distinctively different contributions to epigenetic events. PMID: 26833946
  12. the H2AFZ gene may confer a risk for schizophrenia and contribute to the impairment of executive function in Han Chinese patients with schizophrenia. PMID: 26246156
  13. The 2.7-A-resolution crystal structure of the human YL1-H2A.Z-H2B complex shows that YL1 binding, similarly to ANP32E binding, triggers an extension of the H2A.Z alphaC helix. PMID: 26974126
  14. H2A.Z removal from chromatin is the primary function of INO80 and ANP32E in promoting homologous recombination. PMID: 26142279
  15. Results demonstrated male-selective association of the H2AFZ gene with schizophrenia, and that modification of the H2AFZ signaling pathway warrants further study in terms of the pathophysiology of schizophrenia PMID: 25392085
  16. Dynamic modulation of H2A.Z exchange and removal by Anp32e reveals the importance of the nucleosome surface and nucleosome dynamics in processing the damaged chromatin template during DSB repair. PMID: 26034280
  17. The findings implicate H2A.Z.2 as a mediator of cell proliferation and drug sensitivity in malignant melanoma. PMID: 26051178
  18. the predictive values regarding low expressions of H2AFZ and CASP8AP2 and high white blood cell count suggest that these features could help to identify more accurately patients at greater risk of relapse. PMID: 24397596
  19. Anp32e may help to resolve the non-nucleosomal H2A.Z aggregates and also facilitate the removal of H2A.Z at the +1 nucleosomes, and the latter may help RNA polymerase II to pass the first nucleosomal barrier. PMID: 24613878
  20. Study mapped H2A.Z genome-wide in embryonic stem cells and neural progenitors; H2A.Z is deposited at promoters and enhancers, and correlates strongly with H3K4 methylation. H2A.Z is present at poised promoters with bivalent chromatin and at active promoters with H3K4 methylation, but is absent from stably repressed promoters that are enriched for H3K27 trimethylation. PMID: 23034477
  21. Depletion of H2A.Z in the osteosarcoma U2OS cell line and in immortalized human fibroblasts does not change parameters of DNA double-strand breaks repair while affecting clonogenic ability and cell cycle distribution. PMID: 24240188
  22. A mutational analysis revealed that the amino-acid difference at position 38 is at least partially responsible for the structural polymorphism in the L1 loop region of H2A.Z.1 and H2A.Z.2. PMID: 24311584
  23. Sirt1 and H2A.Z deregulation in prostate cancer are related. Epigenetic mechanisms, mostly histone post-translational modifications, are likely involved and impair sirt1-mediated downregulation of H2A.Z via proteasome-mediated degradation. PMID: 24127549
  24. H2A.Z-dependent crosstalk between enhancer and promoter regulates cyclin D1 expression. PMID: 23108396
  25. SETD6 monomethylates H2AZ on lysine 7. PMID: 23324626
  26. Data show that histone deacetylase inhibitors (HDACi) induce p21 transcription and reduce cell proliferation of MDA-MB231, an ERalpha-negative mammary tumor cell line, in a H2A.Z dependent manner. PMID: 23349794
  27. Data indicate that histone H2A.Z as a protein capable of binding ST1926 specifically. PMID: 23245330
  28. age-dependent p400 downregulation and loss of H2A.Z localisation may contribute to the onset of replicative senescence through a sustained high rate of p21 transcription PMID: 23146670
  29. H2A.Z exchange promotes specific patterns of histone modification and reorganization of the chromatin architecture, leading to the assembly of a chromatin template that is an efficient substrate for the DNA double-strand break repair machinery. PMID: 23122415
  30. ZNF24 may be implicated in transcriptional regulation of genes associated with oncogenesis via interaction with H2A.Z. PMID: 22678762
  31. incorporation of the histone variant H2A.Z at the promoter regions of PPARgamma target genes by p400/Brd8 is essential to allow fat cell differentiation PMID: 23064015
  32. nucleosomes containing H2AZ are primarily composed of H4 K12ac and H3 K4me3 but not H3 K36me3 PMID: 22393239
  33. The short forms of H2A.Z in both yeast and human cells are more loosely associated with chromatin than the full-length proteins, indicating a conserved function for the H2A.Z C-terminal tail in regulating the association of H2A.Z with nucleosomes. PMID: 22493515
  34. acetylation of H2A.Z is a key modification associated with gene activity in normal cells and epigenetic gene deregulation in tumorigenesis. PMID: 21788347
  35. H2A.Z is maintained during mitosis and marks the +1 nucleosome of active genes, which shifts during mitosis, resulting in occupancy at the transcriptional start site and a reduced nucleosome-depleted region. PMID: 20864037
  36. This review provides a brief overview of H2A.Z biology and presents hypotheses that could reconcile contradictory reports that are found in the literature regarding the influence of H2A.Z on nucleosome stability. PMID: 20364108
  37. Eesterogen Receptor alpha directly associates to the H2A.Z promoter, and consequently modulates its expression. PMID: 20023423
  38. chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z PMID: 15878876
  39. neither H2AZ itself nor other features of the H2AZ-containing nucleosome spread to the neighboring nucleosomes in vivo, arguing against a role for H2AZ as a self-perpetuating epigenetic mark PMID: 16809769
  40. identify the essential histone variant H2A.Z as a new structural component of the centromere PMID: 17194760
  41. Monoubiquitylation of H2A.z distinguishes its association with euchromatin or facultative heterochromatin. PMID: 17636032
  42. Upon DNA damage, histone H2A.Z is first evicted from the p21 promoter, followed by the recruitment of the Tip60 histone acetyltransferase to activate p21 transcription. PMID: 17671089
  43. histone variant H2A.Z is associated with breast cancer progression PMID: 18414489
  44. Results show that H2A.Z nucleosomes protect only approximately 120 bp of DNA from MNase digestion and exhibit specific sequence preferences, suggesting a novel mechanism of nucleosome organization for the H2A.Z variant. PMID: 19246569
  45. Both genetic and epigenetic features are likely to participate in targeting H2A.Z to distinct chromatin loci. PMID: 19261190
  46. The nucleosome destabilizing effect of H2A.Z acetylation takes place synergistically with the acetylation of the rest of the core histones. PMID: 19385636
  47. H2A.Z is incorporated into the promoter regions of estrogen receptor (ERalpha) target genes only upon gene induction, and that, in a cyclic pattern PMID: 19515975
  48. show that upon gene induction, human H2A.Z associates with gene promoters and helps in recruiting the transcriptional machinery. PMID: 19834540
  49. Both H2A.Z and H3.3 affect nucleosome positioning, either creating new positions or altering the relative occupancy of the existing nucleosome position space. Only H2A.Z-containing nucleosomes exhibit altered linker histone binding. PMID: 19856965

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Subcellular Location
Nucleus. Chromosome.
Protein Families
Histone H2A family
Database Links

HGNC: 4741

OMIM: 142763

KEGG: hsa:3015

STRING: 9606.ENSP00000296417

UniGene: Hs.119192

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