NARF Polyclonal Antibody

NARF

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.

PBS with 0.05% NaN3 and 40% Glycerol,pH7.4

1.56 mg/mL

Unconjugated

IHC 1:50-1:300, ELISA 1:5000-1:10000

Fusion protein of human NARF

Antigen affinity purification

DKFZp434G0420;FLJ10067;GC17P078009;IOP2;Iron only hydrogenase like protein 2;Nuclear prelamin A recognition factor;Prenyl dependent prelamin A binding protein

Q9UHQ1