Nuclear Prelamin A Recognition Factor (NARF) Antibody

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Description
Nuclear Prelamin A Recognition Factor Antibody is a Rabbit Polyclonal antibody against Nuclear Prelamin A Recognition Factor.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Nuclear Prelamin A Recognition Factor (NARF) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Antigen Affinity Chromatography. |
Size 1 | 100 µl |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS, pH 7.3, containing 0.1% Sodium Azide and 50% Glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q9UHQ1 |
Gene ID | 26502 |
NCBI Accession | NP_001033707.1, NM_001038618.2, NP_001077077.1, NM_001083608.1, NP_036468.1, NM_012336.3 |
OMIM | 605349 |
Background | Antibody anti-NARF |
Status | RUO |
Descripción
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Nuclear Prelamin A Recognition Factor (NARF) Antibody
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.
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