|Other Names||Nuclear prelamin A recognition factor, Iron-only hydrogenase-like protein 2, IOP2, NARF|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Tissue Location||Ubiquitous. Predominantly expressed in skeletal muscle, heart and brain.|
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Several proteins have been found to be prenylated andmethylated at their carboxyl-terminal ends. Prenylation wasinitially believed to be important only for membrane attachment.However, another role for prenylation appears to be its importancein protein-protein interactions. The only nuclear proteins known tobe prenylated in mammalian cells are prelamin A- and B-type lamins.Prelamin A is farnesylated and carboxymethylated on the cysteineresidue of a carboxyl-terminal CaaX motif. Thispost-translationally modified cysteine residue is removed fromprelamin A when it is endoproteolytically processed into maturelamin A. The protein encoded by this gene binds to the prenylatedprelamin A carboxyl-terminal tail domain. It may be a component ofa prelamin A endoprotease complex. The encoded protein is locatedin the nucleus, where it partially colocalizes with the nuclearlamina. It shares limited sequence similarity with iron-onlybacterial hydrogenases. Alternatively spliced transcript variantsencoding 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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