Nuclear Prelamin A Recognition Factor (NARF) (Middle Region) Peptide
NARF
Reactivity: Human
Host: Synthetic
BP, WB
Catalog No. ABIN980494
Quick Overview for Nuclear Prelamin A Recognition Factor (NARF) (Middle Region) Peptide (ABIN980494)
Target
NARF
(Nuclear Prelamin A Recognition Factor (NARF))
Origin
Human
Source
Synthetic
Application
Blocking Peptide (BP), Western Blotting (WB)
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Protein Region
- Middle Region
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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.
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Purification
- Purified
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Application Notes
- Each Investigator should determine their own optimal working dilution for specific applications.
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
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Concentration
- 1 mg/mL
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Buffer
- Final peptide concentration is 1 mg/mL in PBS.
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Handling Advice
- Avoid repeated freeze-thaw cycles.
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Storage
- -20 °C
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Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- NARF (Nuclear Prelamin A Recognition Factor (NARF))
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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
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Gene ID
- 26502
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NCBI Accession
- NM_031968, NP_114174
Target
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