Nuclear Prelamin A Recognition Factor (NARF) (Middle Region) Peptid
Kurzübersicht für Nuclear Prelamin A Recognition Factor (NARF) (Middle Region) Peptid (ABIN980494)
Target
Spezies
Quelle
Applikation
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Protein Region
- Middle Region
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Produktmerkmale
- 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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Aufreinigung
- Purified
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Applikationshinweise
- Each Investigator should determine their own optimal working dilution for specific applications.
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Beschränkungen
- Nur für Forschungszwecke einsetzbar
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Format
- Lyophilized
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Rekonstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
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Konzentration
- 1 mg/mL
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Buffer
- Final peptide concentration is 1 mg/mL in PBS.
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Handhabung
- Avoid repeated freeze-thaw cycles.
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Lagerung
- -20 °C
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Informationen zur Lagerung
- 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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Hintergrund
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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 -
Molekulargewicht
- 55 kDa
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Gen-ID
- 26502
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NCBI Accession
- NM_031968, NP_114174
Target
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