I9781
Importin β1 human
≥80% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal histidine tagged), buffered aqueous glycerol solution
Synonym(s):
Importin β, Karyopherin β1, p97
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About This Item
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recombinant
expressed in E. coli (N-terminal histidine tagged)
Assay
≥80% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~97 kDa by SDS-PAGE
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... KPNB1(3837)
General description
Importin β1 has 19 tandemly repeated HEAT (huntingtin, elongation factor 3 (EF3), protein phosphatase 2A (PP2A) and the yeast kinase TOR1) motifs.[1] The gene is mapped to human chromosome 17q21.[2] The protein shuttles between the cytoplasm and nucleus. It belongs to the importin β family of proteins.[3]
Biochem/physiol Actions
Import receptor, prototype of the nuclear transport receptor family, which interact directly with nuclear pore complex (NPC) and mediate nucleocytoplasmic transport.
Importin β, an import receptor, is a prototype of the nuclear transport receptor family, which comprises in human more than 20 proteins (90-180 kDa). These proteins interact directly with nuclear pore complex (NPC) and mediate nucleocytoplasmic transport. Importin β imports into the nucleus proteins carrying canonical nuclear localization signals (NLS) as well as UsnRNAs, which it binds via adaptor proteins, importin α and snurpotin-1 respectively. Importin β also binds directly, without adaptors, ribosomal proteins, Smad proteins, and virus derived proteins such as HIV Rev and Tat, that contain non classical NLS. In addition, Improtin b has been shown to be involved in the nuclear envelope assembly process.
The mechanism of importin β action in nuclear import can be demonstrated by the well-studied import of proteins containing classical NLS. Importin β forms a complex with Importin α, which, in turn, binds the cargo protein via its NLS. The Impβ/Impα/cargo complex translocates into the nucleus. When the complex reaches the nuclear site of the NPC, Ran-GTP binds the Impβ to form Impβ/Ran-GTP complex and released the Impα and the cargo protein. The Impβ/Ran-GTP complex is then exported to the cytoplasm where the complex dissociates upon hydrolysis of GTP to GDP, making Impβ ready for a new import cycle.
The mechanism of importin β action in nuclear import can be demonstrated by the well-studied import of proteins containing classical NLS. Importin β forms a complex with Importin α, which, in turn, binds the cargo protein via its NLS. The Impβ/Impα/cargo complex translocates into the nucleus. When the complex reaches the nuclear site of the NPC, Ran-GTP binds the Impβ to form Impβ/Ran-GTP complex and released the Impα and the cargo protein. The Impβ/Ran-GTP complex is then exported to the cytoplasm where the complex dissociates upon hydrolysis of GTP to GDP, making Impβ ready for a new import cycle.
Physical form
Solution in 5% glycerol containing 20 mM Hepes, pH 7.5, 110 mM potassium-acetate, 2 mM magnesium-acetate, 0.5 mM EGTA, 0.1 mM ATP, 2 mM DTT, and protease inhibitors.
Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Qian An et al.
International journal of cancer, 103(2), 194-204 (2002-11-28)
Suppression subtractive hybridization (SSH) was applied to identify differentially expressed genes in the SV40LT immortalized human bronchial epithelial cell line Y-BE, with normal human bronchial epithelial cells (HBEC) as a control. Two cDNA libraries of up- and downregulated genes were
Amnon Harel et al.
Molecular cell, 16(3), 319-330 (2004-11-05)
Importin beta, once thought to be exclusively a nuclear transport receptor, is emerging as a global regulator of diverse cellular functions. Importin beta acts positively in multiple interphase roles: in nuclear import, as a chaperone for highly charged nuclear proteins
G Cingolani et al.
Nature, 399(6733), 221-229 (1999-06-03)
Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal
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