Specificity
Brain-specific.
Tag/Conjugate
Unconjugated
SequenceSimilarities
Belongs to the protein arginine N-methyltransferase family. PRMT8 subfamily.
Alternative Names
The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein.The N-terminal region (1-60) inhibits the enzymatic activity.
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.
Antigen Description
Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Arginine methylation is involved in a number of cellular processes, including DNA repair, RNA transcription, signal transduction, protein compartmentalization, and possibly protein translation (Lee et al., 2005 [PubMed 16051612]).[supplied by OMIM, Mar 2008]
Function
S-adenosylmethionine-dependent methyltransferase activity; histone methyltransferase activity (H4-R3 specific); histone-arginine N-methyltransferase activity; identical protein binding; protein binding; protein heterodimerization activity; protein homodim
Synonyms
PRMT8; protein arginine methyltransferase 8; HRMT1L3; HRMT1L4; protein arginine N-methyltransferase 8; HMT1 hnRNP methyltransferase-like 3; protein arginine N-methyltransferase 4; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
Citations
Publication ()
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COA
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