NARF
Reactivity: Human
ELISA
Host: Rabbit
Polyclonal
HRP
Application Notes
NARF antibody can be used for detection of NARF by ELISA at 1:312500. NARF antibody can be used for detection of NARF by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Add 50 ?L of distilled water. Final antibody concentration is 1 mg/mL.
Concentration
1 mg/mL
Buffer
Antibody is lyophilized in PBS buffer with 2 % sucrose.
Handling Advice
As with any antibody avoid repeat freeze-thaw cycles.
Storage
4 °C/-20 °C
Storage Comment
For short periods of storage (days) store at 4 °C. For longer periods of storage, store NARF antibody at -20 °C.
Target
NARF
(Nuclear Prelamin A Recognition Factor (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. NARF binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. NARF is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases.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.