| 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. [provided by RefSeq, Jul 2008]. |
| Source : |
HEK293 |
| Species : |
Human |
| Tag : |
MYC/DDK |
| Form : |
25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol. |
| Molecular Mass : |
51 kDa |
| Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining |
| Concentration : |
>50 ug/mL as determined by microplate BCA method |
