Product Overview
Blocking/Immunizing peptide for anti-Karyopherin (importin) beta 1 antibody
Target
Karyopherin (importin) beta 1
Tag/Conjugate
Unconjugated
Application Notes
For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.
Format
Lyophilized powder
Storage
Shipped at ambient temperature, store at -20°C.
Antigen Description
Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. The protein encoded by this gene is a member of the importin beta family. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2013]
Function
Ran GTPase binding; enzyme binding; nuclear localization sequence binding; poly(A) RNA binding; protein binding; protein domain specific binding; protein transporter activity; zinc ion binding;
Synonyms
KPNB1; karyopherin (importin) beta 1; IMB1; IPO1; IPOB; Impnb; NTF97; importin subunit beta-1; PTAC97; importin 1; importin 90; importin-90; nuclear factor p97; importin beta-1 subunit; karyopherin subunit beta-1; pore targeting complex 97 kDa subunit;
Citations
Publication ()
Have you cited CDBP1664 in a publication?
Let us know and earn a reward for your research.