PHF8 Antibody

Code CSB-PA892365XA01HU
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) PHF8 Polyclonal antibody
Uniprot No.
Target Names
PHF8
Alternative Names
Histone lysine demethylase PHF8 antibody; JHDM1F antibody; Jumonji C domain containing histone demethylase 1F antibody; MRXSSD antibody; PHD finger protein 8 antibody; PHF8 antibody; PHF8_HUMAN antibody; ZNF422 antibody
Raised in
Rabbit
Species Reactivity
Homo sapiens (Human)
Immunogen
Recombinant Homo sapiens (Human) PHF8 protein
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
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

Function
Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3.
Gene References into Functions
  1. These findings suggested that PHF8 played an oncogenic role in facilitating FIP200-dependent autophagic degradation of E-cadherin, EMT and metastasis in hepatocellular carcinoma (HCC). PHF8 might be a promising target for prevention, treatment and prognostic prediction of HCC. PMID: 30180906
  2. the PHF8 oncogene is involved in the progression of CRC. The preliminary findings indicated that PHF8, as a potential target of miR-488, can be suppressed by the overexpression of miR-488. Low levels of miR-488 and high levels of PHF8 were correlated with poor overall survival rates in patients with CRC. PMID: 28765946
  3. PIP2-binding mutant of PHF8 has increased the activity of rDNA promoter (20%) and expression of pre-rRNA genes (47S-100%; 45S-66%). PMID: 29246768
  4. Our data reveal novel mechanisms that underlie the regulation of PHF8 and KDM3A during NED and in CRPC, and support the candidacy of PHF8 as a therapeutic target in CRPC. PMID: 27689328
  5. Thus, PHF8 forms a positive feedback loop with the MEK/ERK pathway, and PHF8 knockdown enhances the lethality of PD184352 in ALL cells. In conclusion, this study identifies oncogenic functions of PHF8 in adult ALL and suggests a novel epigenetic strategy for disease intervention. PMID: 29330049
  6. Knockdown or knockout of PHF8 by RNAi or CRISPR-Cas9 system reduced the activation of HIF1alpha. PMID: 28734980
  7. USP7 promotes breast carcinogenesis by stabilizing PHF8 and upregulating cyclin A2. and the interaction between USP7 and PHF8 is augmented during DNA damage. PMID: 27183383
  8. PHF8 reduces the H3K9me2 level at the E2F4 transcriptional start site, demonstrating a direct function of PHF8 in endothelial E2F4 gene regulation PMID: 26751588
  9. PHF2 is likely to repress rDNA transcription by competing with PHF8 for binding of ribosomal DNA promoter and by recruiting H3K9me2/3 methyltransferase SUV39H1. PMID: 25204660
  10. PHF8 promotes lung cancer cell growth and survival by regulating miR-21. PMID: 25065740
  11. knockdown of PHF8 led to a reduction in the number of migratory and invasive cells. Furthermore, downregulation of PHF8 attenuated the tumorigenicity of ESCC cells in vivo. PMID: 24146981
  12. PHF8 is regulated by APC(cdc20) and plays an important role in the G2/M transition. PMID: 23979597
  13. study identified the histone demethylase PHF8 as a coactivator that is specifically recruited by RAR-alpha fusions to activate expression of their downstream targets upon all-trans retinoic acid treatment in acute promyelocytic leukemia PMID: 23518351
  14. Results show that PHF8 controls the expression of genes involved in cell adhesion and cytoskeleton organization such as RhoA, Rac1 and GSK3beta. PMID: 22850744
  15. a role of PHF8 in cell migration and invasion PMID: 22120715
  16. PHF8 is a histone demethylase and coactivator for RARalpha and that the F279S mutation identified in an XLMR patient results in loss of its demethylase activity. PMID: 20548336
  17. H3K9me2 level was elevated in the promoter region of the rDNA gene in PHF8 knockdown cells and reduced significantly when the wild type but not the catalytically inactive H247A mutant PHF8 was overexpressed. PMID: 20531378
  18. PHF8 demethylates H4K20me1 and H3K9me1 both in vitro and in vivo, and both H3K4me3-binding and catalytic functions of PHF8 are important for its ability to positively regulate gene expression PMID: 20622853
  19. identification and characterization of an H4K20me1 demethylase, PHF8, has revealed an intimate link between this enzyme and two distinct events in cell cycle progression PMID: 20622854
  20. Results show that PHF8 can act as a transcriptional coactivator and that its activation function largely depends on binding of the PHD to H3K4me3. PMID: 20421419
  21. A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation is reported. PMID: 20346720
  22. Results rationalize the lack of activity for the clinically observed F279S PHF8 variant and they will help to identify inhibitors selective for specific N(epsilon)-methyl lysine demethylase subfamilies. PMID: 20067792
  23. PHF8 exerts a positive effect on rDNA transcription, with transcriptional activation requiring both the JmjC domain and the PHD finger. PHF8 demethylates H3K9me1/2, and its catalytic activity is stimulated by adjacent H3K4me3 PMID: 20208542
  24. Molecular mechanism underlying PHF8-associated developmental and neurological diseases. PMID: 20101266
  25. PHF8 is an Fe(II) and 2-oxoglutarate-dependent N(epsilon)-methyl lysine demethylase. PMID: 19843542
  26. an important function of PHF8 is in midline formation and in the development of cognitive abilities, and may have a role in X linked mental retardation associated with cleft lip/palate PMID: 16199551
  27. A novel missense mutation c.836C>T of the PHF8 gene was identified in a Finnish family with multiple-affected male patients with X-linked mental retardation PMID: 17661819
  28. deletion of the PHF8 gene is associated with the X-linked mental retardation Siderius-Hamel syndrome and the larger size of the Xp11.22 deletion including genes FAM120C and WNK3 may be involved in the pathogenesis of autism. PMID: 18498374
  29. PHF8 is a histone lysine demethylase with di-/monomethyl state selectivity. Clinical PHF8 mutants disrupt PHF8 activity. Oxygen-dependence of PHF8 activity suggests link with increased incidence of cleft lip/palate from maternal hypoxia during gestation. PMID: 19843542

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Involvement in disease
Mental retardation, X-linked, syndromic, Siderius type (MRXSSD)
Subcellular Location
Nucleus. Nucleus, nucleolus.
Protein Families
JHDM1 histone demethylase family, JHDM1D subfamily
Database Links

HGNC: 20672

OMIM: 300263

KEGG: hsa:23133

STRING: 9606.ENSP00000350676

UniGene: Hs.133352

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