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 |
|---|---|---|---|
| 88163SF | 100 µg |
|
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45-65 |
| Source/Isotype | Rabbit IgG |
Product Information
Human
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the extracellular domain of human TACSTD2/TROP2 protein. The antigen has been further characterized as corresponding to residues surrounding Ile219 of human TACSTD2/TROP2 protein.
TROP2 is a transmembrane glycoprotein encoded by gene TACSTD2 (tumor associated calcium signal transducer 2). TROP2 was first discovered as a biomarker of invasive trophoblast cells and later reported in many types of cancer cells as well as in various organs during development, and adult stem cells during homeostasis (1,2). TROP2 has an extracellular domain with EGF thyroglobulin type-1 repeats, a transmembrane domain, and a short cytoplasmic tail with a HIKE domain containing a PIP2 binding site and PKC phosphorylation site (Ser303) (1-4). TROP2 functions by regulating multiple signaling pathways including interaction of extracellular domain with integrin beta1 to regulate FAK signaling, association of its transmembrane domain with Claudin-1 and Claudin-7 for tight junction formation, as well as regulation of intracellular calcium release by its PIP2 binding and activation of the ERK/MAPK pathway (1,2,5-8). All of these functions are important for its role in tumor proliferation, metastasis, and invasion (1,2). PKC can phosphorylate TROP2 at Ser303; the phosphorylation changes the cytoplasmic tail conformation and further promotes its signaling (9). TROP2 can be activated through intramembrane proteolysis first by TACE, followed by further cleavage by Presenilin 1 and Presenilin 2. The proteolysis process is required for its role in tumor cell proliferation (10,11).
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