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JMJD7 Antibody (C-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession P0C870
Clone Names 90826187
Peptide ID 90826187
Additional Information
Gene ID 100137047
Other Names JmjC domain-containing protein 7, Jumonji domain-containing protein 7, JMJD7
Target/Specificity The synthetic peptide sequence used to generate the antibody AP9020b was selected from the C-term region of human JMJD7. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name JMJD7 {ECO:0000303|PubMed:28847961, ECO:0000312|HGNC:HGNC:34397}
Function Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase (PubMed:28847961, PubMed:29915238). 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 (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 (PubMed:28847961). After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery (PubMed:29915238). Acts as Fe(2+) and 2-oxoglutarate- dependent monoxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (PubMed:29915238).
Cellular Location Nucleus. Cytoplasm
Research Areas
Citations (0)

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JMJD7 is a highly conserved protein with a JmjC domain, which are part of the cupin metalloenzyme superfamily. JmjC proteins may function as 2-oxoglutarate-Fe(II)-dependent dioxygenases. Most tissues also express read-through


Song,C.,, J. Biol. Chem. 274 (24), 17063-17067 (1999)

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$ 99.00
Cat# BP9020b
Availability: In Stock
Bulk Size
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