The NARF Polyclonal Antibody (PACO10732) is a valuable tool for researchers studying the NARF protein, an essential component of mitochondrial function and energy metabolism. This antibody, produced in rabbits, exhibits high specificity for human samples and has been validated for use in Western blot applications. By binding to the NARF protein, this antibody allows for the detection and analysis of NARF in a variety of cell types, making it an ideal choice for studies in mitochondrial biology and metabolic disorders.NARF, also known as the NADH-quinone oxidoreductase chaperone, plays a crucial role in the assembly and function of complex I in the mitochondrial electron transport chain.
Dysregulation of NARF has been linked to various mitochondrial disorders and metabolic diseases, making it a promising target for research in areas such as neurodegenerative diseases, metabolic syndromes, and aging. By understanding the function and regulation of NARF, researchers can gain insights into the mechanisms underlying these conditions and develop potential therapeutic interventions.
nuclear prelamin A recognition factor;NARF;DKFZp434G0420;FLJ10067;IOP2 ;
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]
