JMJD7 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P0C870 |
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Clone Names | 90826187 |
Gene ID | 100137047 |
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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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | JMJD7 {ECO:0000303|PubMed:28847961, ECO:0000312|HGNC:HGNC:34397} |
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Function | Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase (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 a Fe(2+) and 2- oxoglutarate-dependent monooxygenase, 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 |
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Provided below are standard protocols that you may find useful for product applications.
Background
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
References
Song,C., et.al., J. Biol. Chem. 274 (24), 17063-17067 (1999)
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