NARF polyclonal antibody, anti-human

Background:
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 nuclear prelamin A recognition factor encoded by NARF 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.

Research Area: Others

Synonyms: NARF, Nuclear prelamin A recognition factor, Iron-only hydrogenase-like protein 2, IOP2

Immunogen: The antiserum was produced against synthesized peptide derived from human AMPK alpha around the phosphorylation site of Thr172. AA range:140-189

Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Formulation: Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Concentration: 1 mg/ml

Storage:
-20°C for 1 year