Rabbit anti-Exportin-5 Antibody Affinity Purified
Product Details
Specifications
The epitope recognized by A303-991A maps to a region between residue 1154 to 1204 of human Exportin 5 using the numbering given in entry NP_065801.1 (GeneID 57510).
Immunoglobulin concentration was determined using Beer’s Law where 1mg/mL IgG has an A280 of 1.4. Antibody was affinity purified using an epitope specific to Exportin-5 immobilized on solid support.
The epitope recognized by A303-991A-T maps to a region between residue 1154 to 1204 of human Exportin 5 using the numbering given in entry NP_065801.1 (GeneID 57510).
Additional Product Information
Exportin-5 mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). Exportin-5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. Exportin-5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport [taken from the Universal Protein Resource (UniProt) www.uniprot.org/uniprot/Q9HAV4].
Alternate Names
exp5; exportin-5; ran-binding protein 21
Applications
All western blot analysis is performed using 5% Milk-TBST for blocking and as antibody diluent. Primary antibody is incubated overnight.
Western blots of cell lysates are performed using Goat anti-Rabbit IgG Heavy and Light Chain Antibody (Cat. No. A120-101P).
Western blots of immunoprecipitates are performed using Goat anti-Rabbit Light Chain HRP Conjugate (Cat. No. A120-113P) with 5% Normal Pig Serum (Cat. No. S100-020) added to the blocking buffer.