| Description : |
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. |
| Conjugation : |
HIS |
| Source : |
E. coli |
| Form : |
Lyophilised:Reconstitute with 125 μl aqua dest. |
| Storage buffer : |
Preservative: NoneConstituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5 |
| Storage : |
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 |
