karyopherin β3 Antibody (H-4): sc-17802
- karyopherin β3 Antibody (H-4) is a mouse monoclonal IgG1 κ, cited in 6 publications, provided at 200 µg/ml
- raised against amino acids 1-300 mapping at the N-terminus of karyopherin β3 of human origin
- recommended for detection of karyopherin β3 of mouse, rat and human origin by WB, IP, IF and ELISA
- m-IgG Fc BP-HRP, m-IgG1 BP-HRP and m-IgGκ BP-HRP are the preferred secondary detection reagents for karyopherin β3 Antibody (H-4) for WB applications. These reagents are now offered in bundles with karyopherin β3 Antibody (H-4) (see ordering information below).
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karyopherin β3 Antibody (H-4) is a mouse monoclonal IgG1 antibody that detects karyopherin β3 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Karyopherin β3 plays a crucial role in the nuclear import of proteins, particularly those essential for ribosome biogenesis and cellular function. By facilitating the transport of ribosomal proteins into the nucleus, karyopherin β3 ensures proper assembly of ribosomes, which are vital for protein synthesis in all living cells. Efficient functioning of karyopherin β3 is particularly important in rapidly dividing cells, where protein synthesis demand is high. Additionally, karyopherin β3 interacts with various nucleoporins, which are integral components of the nuclear pore complex, further underscoring significance in selective transport of proteins across the nuclear envelope. Anti-karyopherin β3 antibody (H-4) is an invaluable tool for researchers studying nuclear transport mechanisms and their implications in cellular processes and diseases.
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karyopherin β3 Antibody (H-4) References:
- Structural basis for substrate recognition and dissociation by human transportin 1. | Imasaki, T., et al. 2007. Mol Cell. 28: 57-67. PMID: 17936704
- A novel function of karyopherin beta3 associated with apolipoprotein A-I secretion. | Chung, KM., et al. 2008. Mol Cells. 26: 291-8. PMID: 18562802
- RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1. | Fritz, J., et al. 2009. Mol Cell Biol. 29: 1487-97. PMID: 19124606
- A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1. | Van Dusen, CM., et al. 2010. Mol Cell Biol. 30: 2552-62. PMID: 20308327
- Transportin 1 in the mouse brain: appearance in regions of neurogenesis, cerebrospinal fluid production/sensing, and circadian clock. | Sato, M., et al. 2011. J Comp Neurol. 519: 1770-80. PMID: 21452213
- Molecular dynamics simulation of conformational heterogeneity in transportin 1. | Wang, X., et al. 2012. Proteins. 80: 382-97. PMID: 22105828
- A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1. | Barraud, P., et al. 2014. Proc Natl Acad Sci U S A. 111: E1852-61. PMID: 24753571
- The non-classical nuclear import carrier Transportin 1 modulates circadian rhythms through its effect on PER1 nuclear localization. | Korge, S., et al. 2018. PLoS Genet. 14: e1007189. PMID: 29377895
- Inhibition of the acetyltransferase NAT10 normalizes progeric and aging cells by rebalancing the Transportin-1 nuclear import pathway. | Larrieu, D., et al. 2018. Sci Signal. 11: PMID: 29970603
- Cloning and characterization of human karyopherin beta3. | Yaseen, NR. and Blobel, G. 1997. Proc Natl Acad Sci U S A. 94: 4451-6. PMID: 9114010
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
karyopherin β3 Antibody (H-4) | sc-17802 | 200 µg/ml | $316.00 | |||
karyopherin β3 Antibody (H-4): m-IgG Fc BP-HRP Bundle | sc-536589 | 200 µg Ab; 10 µg BP | $354.00 | |||
karyopherin β3 Antibody (H-4): m-IgGκ BP-HRP Bundle | sc-533740 | 200 µg Ab; 40 µg BP | $354.00 | |||
karyopherin β3 Antibody (H-4): m-IgG1 BP-HRP Bundle | sc-544693 | 200 µg Ab; 20 µg BP | $354.00 |