||Recombinant fragment, corresponding to amino acids 1-322 of Human NARF Isoform 2 with an N terminal His tag; Predicted MWt 37 kDa.
||Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.
||Lyophilised:Reconstitute with 125 μl aqua dest.
||Preservative: NoneConstituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5
||Shipped at 4°C. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles.
|Sequences of amino acids:
||MKCEHCTRKECSKKTKTDDQENVSADAPSPAQENGEKGEF HKLADAKIFLSDCLACDSCMTAEEGVQLSQQNAKDFFR VLNLNKKCDTSKHKVLVVSVCPQSLPYFAAKFNLSVTD ASRRLCGFLKSLGVHYVFDTTIAADFSILESQKEFVRR YRQHSEEERTLPMLTSACPGWVRYAERVLGRPITAHLCTA KSPQQVMGSLVKDYFARQQNLSPEKIFHVIVAPCYDKK LEALQESLPPALHGSRGADCVLTSEISQAWWCTPVITA TREAAARESLEPGRQRLQRDKIAPLDSSLGGGGEIAQI MEQGDLSVRDAAVD