NARF Antibody / Nuclear prelamin A recognition factor

Western blot: 0.5-1ug/ml,Flow cytometry: 1-3ug/million cells,Direct ELISA: 0.1-0.5ug/ml

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.

Antigen affinity purified

0.5mg/ml if reconstituted with 0.2ml sterile DI water

E. coli-derived recombinant human protein (amino acids H41-Q353) was used as the immunogen for the NARF antibody.

Antigen affinity purified

Q9UHQ1