Reactive species
Human;Mouse;Rat
Applications
WB;IHC;IF;ELISA
Antibody type
Polyclonal Antibody
Protein name
Importin subunit alpha-2
Immunogen
Synthesized peptide derived from the N-terminal region of human Karyopherin α2.
Specificity
Karyopherin α2 Polyclonal Antibody detects endogenous levels of Karyopherin α2 protein.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
IHC-p: 100-300.WB: 1/500 - 1/2000. ELISA: 1/10000.. IF 1:50-200
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
KPNA2; RCH1; SRP1; Importin subunit alpha-2; Karyopherin subunit alpha-2; RAG cohort protein 1; SRP1-alpha
Background
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J re
Function
domain:Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.,domain:The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins.,domain:The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within i
