The NARF Antibody (PACO03845) is a high-quality polyclonal antibody designed for research involving NARF, a critical protein involved in regulating mitochondrial function. This antibody is raised in rabbits and is highly specific for detecting NARF in human samples, making it ideal for Western blot applications.NARF is a key player in maintaining mitochondrial integrity and function, making it essential for cellular energy production and overall cell health. Dysregulation of NARF has been linked to various diseases, including neurodegenerative disorders and metabolic diseases.
By using the NARF Antibody, researchers can gain valuable insights into the role of NARF in these disease processes and potentially identify new therapeutic targets.With its high reactivity and specificity, the NARF Antibody is a valuable tool for studies in cell biology, metabolism, and disease pathology. By enabling precise detection and analysis of NARF in different cell types and experimental conditions, this antibody opens up new possibilities for understanding the complex interplay between mitochondrial function and disease development.
Antibody Name:
NARF Antibody
Antibody SKU:
PACO03845
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
WB:1:500-1:2000
Species Reactivity:
Human
Immunogen:
synthesized peptide derived from the Internal region of human NARF.
Form:
Liquid
Storage Buffer:
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Synonyms:
NARF; Nuclear prelamin A recognition factor; Iron-only hydrogenase-like protein 2; 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]