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IPO9 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| FC, IHC-P, WB, E |
|---|---|
| Primary Accession | Q96P70 |
| Other Accession | Q91YE6, NP_060555.2 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 115963 Da |
| Antigen Region | 79-106 aa |
| Gene ID | 55705 |
|---|---|
| Other Names | Importin-9, Imp9, Ran-binding protein 9, RanBP9, IPO9, IMP9, KIAA1192, RANBP9 |
| Target/Specificity | This IPO9 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 79-106 amino acids from the N-terminal region of human IPO9. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | IPO9 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | IPO9 {ECO:0000303|PubMed:30855230, ECO:0000312|HGNC:HGNC:19425} |
|---|---|
| Function | Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin (PubMed:11823430, PubMed:34711951, PubMed:30855230). Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430). Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11823430). At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran (PubMed:11823430). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11823430). Mediates the import of pre-assembled proteasomes into the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome complex (PubMed:11823430, PubMed:34711951). Mediates the nuclear import of histones H2A, H2B, H4 and H4 (PubMed:11823430, PubMed:30855230). In addition to nuclear import, also acts as a chaperone for histones by preventing inappropriate non-nucleosomal interactions (PubMed:30855230). Mediates the nuclear import of actin (By similarity). |
| Cellular Location | Cytoplasm. Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
Background
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP-and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of H2B histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains. May also import H2A, H3, H4 histones (By similarity), RPL4 and RPL6.
References
King, F.W., et al. Mol. Cell. Biol. 24(16):7091-7101(2004)
Lubert, E.J., et al. Biochem. Biophys. Res. Commun. 303(3):908-913(2003)
Jakel, S., et al. EMBO J. 21(3):377-386(2002)
Muhlhausser, P., et al. EMBO Rep. 2(8):690-696(2001)
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