
-
Your selected country is
Middle East / Africa
- Change country/language
Old Browser
This page has been recently translated and is available in French now.
Looks like you're visiting us from {{countryName}}.
Would you like to stay on the current country site or be switched to your country?





Western blot analysis of Karyopherin β on a Jurkat cell lysate (Human T-cell leukemia; ATCC TIB-152). Lane 1: 1:1000, lane 2: 1: 2000, lane 3: 1:4000 dilution of the mouse anti-karyopherin β antibody.

Immunofluorescence staining of rat pituitary cells.


BD Transduction Laboratories™ Purified Mouse Anti-Karyopherin β

BD Transduction Laboratories™ Purified Mouse Anti-Karyopherin β

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Companion Products


.png?imwidth=320)
Using nuclear import assays, several cytosolic proteins that form a multi-protein complex have been identified. These proteins of 54 kDa, 56 kDa, and 97 kDa stimulate the nuclear transport of proteins containing a nuclear localization signal (NLS). The 97 kDa protein has been named karyopherin β. The NLS binds to karyopherin α. Binding is enhanced by karyopherin β. The NLS substrate also binds to the N-terminal region of karyopherin β. Both karyopherins bind to repeat sequences of nucleoporins at the nuclear envelope. Once the substrate is docked to the nuclear envelope, Ran hydrolyzes GTP and translocation occurs. Karyopherin β also binds to and inhibits the Ran GTPase protein, thus providing a mechanism of nuclear transport termination.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
-
Iborra FJ, Jackson DA, Cook PR. The path of RNA through nuclear pores: apparent entry from the sides into specialized pores. J Cell Sci. 2000; 113(2):291-302. (Biology: Electron microscopy). View Reference
-
Radu A, Blobel G, Moore MS. Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc Natl Acad Sci U S A. 1995; 92(5):1769-1773. (Biology). View Reference
-
Rexach M, Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 1995; 83(5):683-692. (Biology). View Reference
-
Saitoh H, Pizzi MD, Wang J. Perturbation of SUMOlation enzyme Ubc9 by distinct domain within nucleoporin RanBP2/Nup358. J Biol Chem. 2002; 277(7):4755-4763. (Biology: Immunofluorescence). View Reference
-
Wiese C, Wilde A, Moore MS, Adam SA, Merdes A, Zheng Y. Role of importin-beta in coupling Ran to downstream targets in microtubule assembly. Science. 2001; 291(5504):653. (Biology: Western blot). View Reference
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Report a Site Issue
This form is intended to help us improve our website experience. For other support, please visit our Contact Us page.