|Application ||WB, E|
|Other Accession||NP_001033707.1, NP_001077077.1|
|Calculated MW||51156 Da|
|Antigen Region||134-160 aa|
|Other Names||Nuclear prelamin A recognition factor, Iron-only hydrogenase-like protein 2, IOP2, NARF|
|Target/Specificity||This NARF antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 134-160 amino acids from the Central region of human NARF.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NARF Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Tissue Location||Ubiquitous. Predominantly expressed in skeletal muscle, heart and brain.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Moller-Krull, M., et al. J. Mol. Biol. 382(3):601-609(2008)
Melzer, D., et al. PLoS Genet. 4 (5), E1000072 (2008) :
Lattanzi, G., et al. J. Cell. Biochem. 102(5):1149-1159(2007)
Matsuoka, S., et al. Science 316(5828):1160-1166(2007)
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