Anti-NARF Antibody Picoband® fluoro488 Vervoeging

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.

E3 ubiquitin-protein ligase RNF169; RING finger protein 169; RING-type E3 ubiquitin transferase RNF169; RNF169; KIAA1991

NARF

26502

Q9UHQ1

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human NARF recombinant protein (Position: H41-Q353) .

Expressed in immature but not mature T-cells. Also found in CD34+ cells from peripheral blood, CD34+ precursors from umbilical cord blood and adult bone marrow.

Flow Cytometry

Hematopoietic Progenitors, Lymphoid, Stem Cells, T Lymphocytic Lineage

Immunogen affinity purified.

Liquid

Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair.

1. Barton, R. M., Worman, H. J. Prenylated prelamin A interacts with Narf, a novel nuclear protein. J. Biol. Chem. 274: 30008-30018, 1999.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

41409 MW

6

Ring finger protein 169

Nucleoplasm.

Protein NDRG3

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.