Nuclear Prelamin A Recognition Factor (NARF) (Middle Region) Peptide
NARF
Reactivity: Human
Host: Synthetic
BP, WB
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- Target See all NARF products
- NARF (Nuclear Prelamin A Recognition Factor (NARF))
- Protein Region
- Middle Region
- Origin
- Human
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Source
- Synthetic
- Application
- Blocking Peptide (BP), Western Blotting (WB)
- Characteristics
- This is a synthetic peptide designed for use in combination with anti-NARF antibody (Catalog #: ARP54490_P050). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
- Purification
- Purified
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- Application Notes
- Each Investigator should determine their own optimal working dilution for specific applications.
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
- Concentration
- 1 mg/mL
- Buffer
- Final peptide concentration is 1 mg/mL in PBS.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -20 °C
- Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- Target
- NARF (Nuclear Prelamin A Recognition Factor (NARF))
- Background
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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. NARF binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. NARF is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases.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.
Alias Symbols: DKFZp434G0420, FLJ10067, IOP2
Protein Interaction Partner: LMNA,LMNA
Protein Size: 502 - Molecular Weight
- 55 kDa
- Gene ID
- 26502
- NCBI Accession
- NM_031968, NP_114174
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