The NARF Polyclonal Antibody (PACO51738) is a valuable tool for researchers studying the NARF protein, which is involved in various cellular processes, including mitochondrial function and metabolism. This antibody, produced in rabbits, is highly specific to human samples and has been validated for use in Western blot applications.NARF, also known as Nucleolar and coiled-body phosphoprotein, plays a crucial role in maintaining mitochondrial homeostasis and has been implicated in diseases such as cancer and neurodegenerative disorders.
By targeting the NARF protein, researchers can gain insights into the molecular mechanisms underlying these conditions and develop potential therapeutic interventions.With its high reactivity and specificity, the NARF Polyclonal Antibody is an essential tool for researchers in the fields of cell biology, biochemistry, and cancer research. Its ability to detect and analyze NARF in various cell types makes it a valuable asset for studying the role of this protein in health and disease.
Nuclear prelamin A recognition factor (Iron-only hydrogenase-like protein 2) (IOP2), NARF
UniProt Protein Function:
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. [provided by RefSeq, Jul 2008]Chromosomal Location of Human Ortholog: 17q25.3Cellular Component: lamin filament; nuclear lamina; nuclear lumenMolecular Function: lamin binding
UniProt Protein Details:
NCBI Summary:
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]