Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: >= 95% SDS-PAGE
- Active: Yes
- Tags: DDDDK tag N-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Product nameRecombinant human PHF8 protein (Active)
See all PHF8 proteins and peptides
Specific Activity: 0.064 pmol/min/μg
Assay conditions: PHF8 enzyme is incubated with biotinylated histone H3 peptide substrate in HEPES-based buffer in a 10 µg reaction for 1 hr. at RT. Add 5 µg of AlphaLISA™ anti-Rabbit Acceptor beads (20 µg/ml), followed by addition of 5 µl of antibody and 30 min. incubation at RT. Add 10 µg of AlphaScreen™ Streptavidin-conjugated donor beads (40 µg/ml). Alpha counts are measured after 10 min. RT incubation.
Purity>= 95 % SDS-PAGE.
Expression systemBaculovirus infected Sf9 cells
Protein lengthProtein fragment
SequenceNRSRAIVQR GRVLPPPAPL DTTNLAGRRT LQGRAKMASV PVYCLCRLPY DVTRFMIECD MCQDWFHGSC VGVEEEKAAD IDLYHCPNCE VLHGPSIMKK RRGSSKGHDT HKGKPVKTGS PTFVRELRSR TFDSSDEVIL KPTGNQLTVE FLEENSFSVP ILVLKKDGLG MTLPSPSFTV RDVEHYVGSD KEIDVIDVTR QADCKMKLGD FVKYYYSGKR EKVLNVISLE FSDTRLSNLV ETPKIVRKLS WVENLWPEEC VFERPNVQKY CLMSVRDSYT DFHIDFGGTS VWYHVLKGEK IFYLIRPTNA NLTLFECWSS SSNQNEMFFG DQVDKCYKCS VKQGQTLFIP TGWIHAVLTP VDCLAFGGNF LHSLNIEMQL KAYEIEKRLS TADLFRFPNF ETICWYVGKH ILDIFRGLRE NRRHPASYLV HGGKALNLAF RAWTRKEALP DHEDEIPETV RTVQLIKDLA REIRLVEDIF QQNVGKTSNI FGLQRIFPAG SIPLTRPAHS TSVSMSRLSL PSKNG
Predicted molecular weight62 kDa including tags
Amino acids2 to 525
TagsDDDDK tag N-Terminus
Our Abpromise guarantee covers the use of ab271712 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.63% Tris HCl, 0.64% Sodium chloride, 0.02% Potassium chloride, 0.04% Tween, 20% Glycerol (glycerin, glycerine), 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
80 µg/ml FLAG peptide
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Histone lysine demethylase PHF8
- Jumonji C domain containing histone demethylase 1F
FunctionHistone 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.
Involvement in diseaseDefects in PHF8 are the cause of mental retardation syndromic X-linked Siderius type (MRXSSD) [MIM:300263]. A disorder characterized by mild to borderline mental retardation with or without cleft lip/cleft palate.
Sequence similaritiesBelongs to the JHDM1 histone demethylase family. JHDM1D subfamily.
Contains 1 JmjC domain.
Contains 1 PHD-type zinc finger.
DomainThe PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2.
The linker region is a critical determinant of demethylase specificity. It enables the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3.
modificationsPhosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.
Cellular localizationNucleus. Nucleus > nucleolus. Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab271712 has not yet been referenced specifically in any publications.