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Protein expression services for Kdm8 | Bifunctional peptidase and arginyl-hydroxylase JMJD5

Description
Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionnally, acts as Fe(2+) and 2-oxoglutarate-dependent monoxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (By similarity). Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a catalytically-independent manner (By similarity). Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation (By similarity).
Species
Rattus norvegicus
Length
414 amino acids
Sequence
MSEDTTEPLVGPSTLWKDLRALLPDTEEELKLDLSEKVDRSMATLLRQALGLFYEGRWQKCLQASEAVLDYSWEKLNTGPWRDVDKEWRRVYSFGCLLKTLCLCQAPQKATAVAEALRVCDMGLLMGAAILGDILLKVATVLQTHLLPRKQPACGPHQDQPATKKAKHDASSTPDVVLDREVPRLRCPPLQHFKKHFLVPGRPVILEGVADHWPCMKKWSLQYIQEIAGCRTVPVEVGSRYTDEDWSQTLMTVNEFIHKYILSEAKDVGYLAQHQLFDQIPELKQDISIPDYCCLGNGEEEEITINAWFGPQGTISPLHQDPQQNFLVQVLGRKYIRLYSPQESEAVYPHETHILHNTSQVDVENPDLEKFPKFTEAPFLSCILSPGDTLFIPAKYWHYVRSLDLSFSVSFWWS
Mass
47.2 kDa
Simulated SDS-PAGE
Western blot of Kdm8 recombinant protein(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)
Safety
Upon ordering, we will perform rigorous biosecurity and export control screening to ensure that order fulfillment is consistent with all legal and regulatory guidance.
Protein synthesis service
Make Kdm8 using our protein expression services starting at $99 + $.30/amino acid in as fast as two weeks (includes the cost of DNA synthesis)

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