|Application ||WB, E|
|Other Accession||EAW83708, 119604114|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||Predicted: 105 kDa |
Observed: 99 kDa
|Application Notes||TNPO3 antibody can be used for detection of TNPO3 by Western blot at 1 - 2 µg/mL.|
|Reconstitution & Storage||TNPO3 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||TNPO3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains.|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Expressed in skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
TNPO3 Antibody: TNPO3 is a member of the importin beta/transportin family of nuclear import receptors and is specific for the essential splicing factors termed SR proteins, binding specifically and directly to the arginine/serine (RS)-rich domains of these proteins. Further experiments demonstrated that this interaction occurs only when these RS domains are phosphorylated. More recently, TNPO3 was identified as an HIV dependency factor (HDF) and that depletion of TNPO3 resulted in HIV inhibition after reverse transcription but before integration, suggesting that TNPO3 may be an important drug target in HIV treatment. At least three isoforms of TNPO3 are known to exist.
Kataoka N, Bachorik JL and Dreyfuss G. Transportin-SR, a nuclear import receptor for SR proteins. J. Cell Biol.1999; 145:1145-52.
Lai M-C, Lin R-I, Huang S-Y, et al. A human importin-b family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J. Biol. Chem.2000; 275:7950-7.
Brass AL, Dykxhoorn DM, Benita Y, et al. Identification of host proteins required for HIV infection through a functional genomic screen. Science2008; 319:921-6.
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