R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Exportin-1/CRM1 (D6V7N) Rabbit mAb #46249
Filter:
- WB
- IP
- IHC
- IF
Supporting Data
REACTIVITY | H M Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 123 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:50 |
Immunohistochemistry (Paraffin) | 1:300 - 1:1200 |
Immunofluorescence (Immunocytochemistry) | 1:400 - 1:1600 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier free (BSA and azide free) version of this product see product #49000.
For a carrier free (BSA and azide free) version of this product see product #49000.
Protocol
Specificity / Sensitivity
Exportin-1/CRM1 (D6V7N) Rabbit mAb recognizes endogenous levels of total exportin-1/CRM1 protein.
Species Reactivity:
Human, Mouse, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human exportin-1/CRM1 protein.
Background
Exportins are a family of seven proteins that are responsible for intracellular transport. Exportin-1, also known as chromosome region maintenance 1 (CRM1), is a protein essential for nuclear export of hundreds of proteins, mRNAs, and rRNAs (1-3). Exportin-1 binds to substrates with nuclear export signals (NESs) rich in leucine and other hydrophobic amino acids (4). These hydrophobic sequences form an alpha-helix-loop that can bind to the exportin-1 hydrophobic groove (5). Studies have shown that these NESs can be modified either by protein modifications or by mutation to regulate exportin-1 binding (6-7). Targets of exportin-1 include many tumor suppressors, such as Rb, p53, FoxO1, BAF47, as well as oncoproteins, such as p21 and p27 (1). In addition, Myc can upregulate exportin-1 during biogenesis, where it can export newly formed 40S and 60S subunits from the nucleoli (8-9).
Inhibition of nuclear export has been pursued for therapeutic application since the finding that leptomycin B could suppress HIV replication by suppressing the ability of exportin-1 to export the HIV-1 protein Rev (2, 10). Overexpression of exportin-1 has been associated with poor prognosis in various cancer types (11-13). Genomic approaches and development of inhibitors have identified exportin-1 as a druggable target (14-16). The use of various inhibitors of exportin-1 is also being explored in various antiviral therapies (17-18).
Inhibition of nuclear export has been pursued for therapeutic application since the finding that leptomycin B could suppress HIV replication by suppressing the ability of exportin-1 to export the HIV-1 protein Rev (2, 10). Overexpression of exportin-1 has been associated with poor prognosis in various cancer types (11-13). Genomic approaches and development of inhibitors have identified exportin-1 as a druggable target (14-16). The use of various inhibitors of exportin-1 is also being explored in various antiviral therapies (17-18).
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- Dong, X. et al. (2009) Nat Struct Mol Biol 16, 558-60.
- Vogt, P.K. et al. (2005) Cell Cycle 4, 908-13.
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- Golomb, L. et al. (2012) Mol Cell 45, 222-32.
- Wolff, B. et al. (1997) Chem Biol 4, 139-47.
- Noske, A. et al. (2008) Cancer 112, 1733-43.
- Shen, A. et al. (2009) Neurosurgery 65, 153-9; discussion 159-60.
- Yao, Y. et al. (2009) Oncol Rep 21, 229-35.
- Schmidt, J. et al. (2013) Leukemia 27, 2357-65.
- Boyle, S.M. et al. (1999) J Virol 73, 6872-81.
- Walker, C.J. et al. (2013) Blood 122, 3034-44.
- Yadav, V. et al. (2016) Virusdisease 27, 357-368.
- Chutiwitoonchai, N. et al. (2017) Virology 507, 32-39.
限制使用
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