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You are here:Home » Antibodies » Abs to Transport Proteins » Anti -Karyopherin beta 3 (KPNB3, DKFZp686O1576, FLJ43041, Importin beta 3 Subunit, IMB3, IPO5, MGC2068, OTTHUMP00000040733, Ran GTP Binding Protein 5, RanBP5)

Anti -Karyopherin beta 3 (KPNB3, DKFZp686O1576, FLJ43041, Importin beta 3 Subunit, IMB3,
IPO5, MGC2068, OTTHUMP00000040733, Ran GTP Binding Protein 5, RanBP5)

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Specifications

Clone Host Grade Applications
Polyclonal Goat Affinity Purified E
Nucleocytoplasmic transport takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Karyopherin (importin) beta 3 (KPNB3) 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.
Catalog #K0102-37B
ApplicationsSuitable for use in ELISA. Other applications not tested.
Recommended DilutionELISA: 1:4000
Optimal dilutions to be determined by the researcher.
Storage and StabilityMay be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Clone TypePolyclonal
IsotypeIgG
HostGoat
SourceHuman
Concentration~0.5mg/ml
FormSupplied as a liquid in Tris saline, 0.02% sodium azide, pH7.3, 0.5% BSA.
PurityPurified by immunoaffinity chromatography.
ImmunogenSynthetic peptide corresponding to PEDQVGKLEATEN, from N-terminus of the protein sequence according to NP_002262.
SpecificityRecognizes human KPNB3.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.


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