Anti-Human CRM1 DyLight® 488 conjugated XPO1 Antibody (monoclonal, 5G3), Carrier-free

Exportin 1 (XPO1), also known as chromosomal maintenance 1 (CRM1), is an eukaryotic protein that mapped to human chromosome 2p16 by fluorescence in situ hybridization. This protein mediates leucine-rich nuclear export signal (NES)-dependent protein transport. It specifically inhibits the nuclear export of Rev and U snRNAs. Additionally, this protein is involved in the control of several cellular processes by controlling the localization of cyclin B, MPAK, and MAPKAP kinase 2. It also regulates NFAT and AP-1.

E.coli-derived human CRM1 recombinant protein (Position: N966-D1071). Human CRM1 shares 93.4% and 91.5% amino acid (aa) sequence identity with mouse and rat CRM1, respectively.

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Not expressed in the kidney.

Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). 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, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The ionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.

1. Dong, X., Biswas, A., Suel, K. E., Jackson, L. K., Martinez, R., Gu, H., Chook, Y. M. Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature 458: 1136-1141, 2009. Note: Erratum: Nature 461: 550 only, 2009. 2. Fornerod, M., van Baal, S., Valentine, V., Shapiro, D. N., Grosveld, G. Chromosomal localization of genes encoding CAN/Nup214-interacting proteins--human CRM1 localizes to 2p16, whereas Nup88 localizes to 17p13 and is physically linked to SF2p32. Genomics 42: 538-540, 1997. 3. Kudo, N., Khochbin, S., Nishi, K., Kitano, K., Yanagida, M., Yoshida, M., Horinouchi, S. Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J. Biol. Chem. 272: 29742-29751, 1997.

Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.