Recombinant Human PHF8, GST-tagged

Cat.No. : PHF8-63H
Product Overview : Recombinant Human PHF8 includes amino acids 80-447 of PHF8 (accession number NP_055922) was generated by expressing a GST fusion protein containing residues 80-447 of PHF8 in E. coli cells, followed by affinity purification and cleavage of the GST tag with thrombin to produce a protein with an observed molecular weight of 42.592 kDa.
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Description : PHF8 (PHD finger protein 8), also known as Lysine (K)-specific demethylase 7B (KDM7B) and JmjC domain-containing histone demethylation protein 1D-B (JHDM1DB), is a member of the JmjC-containing (Jumonji-C) class of histone demethylase proteins that are involved in the regulation of genome function through the removal of methyl groups from histones. PHF8 has two N-terminal domains, a PHD finger that binds trimethylated lysine 4 of histone H3 (H3K4me3) and a Jumonji domain that demethylates monomethylated H3 Lys9 (H3K9me1), Histone H3 dimethyl Lys9 (H3K9me2), Histone H3 dimethyl Lys27 (H3K27me2) (which are all modifications associated with transcriptional repression) and also Histone H3 dimethyl Lys36 (H3K36me2).
Source : E. coli
Species : Human
Form : 50 mM Tris pH 8.0, 400 mM NaCl.
Applications : Enzyme kinetics, inhibitor screening, and selectivity profiling.
Storage : Recombinant proteins in solution are temperature sensitive and must be stored at -80°C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Concentration : 0.3 mg/ml
Tag : Non
Protein length : 80-447 a.a.
Gene Name PHF8 PHD finger protein 8 [ Homo sapiens ]
Official Symbol PHF8
Synonyms PHF8; PHD finger protein 8; histone lysine demethylase PHF8; JHDM1F; jumonji C domain containing histone demethylase 1F; KIAA1111; ZNF422; jumonji C domain-containing histone demethylase 1F; MRXSSD; DKFZp686E0868;
Gene ID 23133
mRNA Refseq NM_001184896
Protein Refseq NP_001171825
MIM 300560
UniProt ID Q9UPP1
Chromosome Location Xp11.22
Function chromatin binding; histone demethylase activity; histone demethylase activity (H3-K27 specific); histone demethylase activity (H3-K36 specific); histone demethylase activity (H3-K9 specific); histone demethylase activity (H4-K20 specific); iron ion binding; metal ion binding; methylated histone residue binding; oxidoreductase activity; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; protein binding; zinc ion binding;

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