NARF
(Nuclear Prelamin A Recognition Factor (NARF))
蛋白结构域
Middle Region
宿主
人
资源
合成
应用范围
Blocking Peptide (BP), Western Blotting (WB)
产品特性
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.
Each Investigator should determine their own optimal working dilution for specific applications.
限制
仅限研究用
状态
Lyophilized
溶解方式
Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
浓度
1 mg/mL
缓冲液
Final peptide concentration is 1 mg/mL in PBS.
注意事项
Avoid repeated freeze-thaw cycles.
储存条件
-20 °C
储存方法
For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
抗原
NARF
(Nuclear Prelamin A Recognition Factor (NARF))
背景
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.