Recombinant antibodies offer several key advantages compared to traditional antibodies. These include superior lot-to-lot consistency, continuous supply, and animal-free manufacturing. As such, recombinant antibodies are seeing increased use for scientific research, especially as a means of addressing the ongoing reproducibility crisis.
Traditional polyclonal and monoclonal antibodies are the product of normal B cell development and genetic recombination. They are generated by immunizing an animal with an antigen to elicit an immune response. While polyclonal antibodies are secreted by many different B cell clones and recognize multiple antigenic epitopes, monoclonals originate from a single B cell clone and are specific for just one epitope.
Recombinant antibodies are monoclonal, but their production involves in vitro genetic manipulation. After cloning the antibody genes into an expression vector, this is then transfected into an appropriate host cell line for antibody expression. Mammalian cell lines are most commonly used for recombinant antibody production, although cell lines of bacterial, yeast, or insect origin are also suitable.
Because recombinant antibody production involves sequencing the antibody light and heavy chains, it is a highly controlled and reliable process. In contrast, hybridoma-based systems for producing monoclonal antibodies are subject to genetic drift and instability, increasing the potential for lot-to-lot variability or loss of antibody expression. Recombinant antibodies are highly consistent from lot to lot, thereby ensuring reproducible experimental results.
In vitro methods for producing antibodies are amenable to large-scale production, meaning antibody availability is unlikely to become a limiting factor. Moreover, since the recombinant antibody sequence is known, continuity of supply is assured; in situations where an antibody will be used to support large, long-term studies, this can be an especially critical factor.
Unlike traditional methods for antibody production, recombinant approaches avoid the need to use animals. Where polyclonal antibodies are purified directly from the serum of the immunized host, and monoclonals are purified from either hybridoma-derived tissue culture supernatant or ascites, recombinant antibodies are instead purified from the tissue culture supernatants of transfected host cell lines. Regardless of whether an antibody is polyclonal, monoclonal or recombinant, it must always be properly validated in the intended application prior to experimental use. At CST, we adhere to the Hallmarks of Antibody Validation™, six complementary strategies for determining the specificity, sensitivity, and functionality of an antibody in any given assay. By carefully tailoring these strategies to each antibody product, we guarantee that CST antibodies will work as expected, to help you achieve results you can trust.
| Cat. # | Size | Qty. | Price |
|---|---|---|---|
| 49000SF | 100 µg |
|
| REACTIVITY | H M Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 123 |
| Source/Isotype | Rabbit IgG |
Product Information
Human, Mouse, Monkey
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human exportin-1/CRM1 protein.
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).
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