This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This NARF antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 134-160 amino acids from the Central region of human NARF.
NARF
Reaktivität: Human
ELISA
Wirt: Kaninchen
Polyclonal
HRP
Applikationshinweise
For WB starting dilution is: 1:1000
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
0.5 mg/mL
Buffer
Supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Informationen zur Lagerung
Store at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Target
NARF
(Nuclear Prelamin A Recognition Factor (NARF))
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.