Recombinant rabbit polyclonal antibodies consist of a mixture of recombinant antibodies co-expressed from a library of heavy and light chains. These antibodies offer a unique advantage by combining the sensitivity of polyclonal antibodies with the specificity of monoclonal antibodies. Additionally, they help provide the consistency that can only be achieved through recombinant antibody production. Similar to traditional polyclonal antibodies, recombinant polyclonal antibodies have the ability to recognize multiple epitope sites on the target molecule. This unique characteristic enables enhanced detection sensitivity, especially for targets with low abundance. However, what sets recombinant polyclonal antibodies apart is their known composition of heavy and light chains, which can be replicated consistently in every production lot. This eliminates the inherent biological variability that is typically associated with subsequent polyclonal lot reproductions. With recombinant polyclonal antibodies, researchers can enjoy the benefits of high sensitivity and reproducibility, helping provide a reliable and consistent tool for their experiments and assays.

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Why choose Invitrogen recombinant rabbit polyclonal antibodies?

With a wide range of antibodies available, we offer solutions for various applications, including western blotting, immunocytochemistry, flow cytometry, and more. Our antibodies undergo rigorous advanced verification processes to ensure optimal performance, specificity, and sensitivity. This comprehensive validation helps provide researchers with confidence in the reliability and accuracy of our antibodies. By choosing Invitrogen Recombinant antibodies, customers can access a diverse portfolio and trust in the quality and performance of our extensively verified products.


Recombinant rabbit polyclonal antibody production

Recombinant rabbit polyclonal antibody production relies on molecular cloning of heavy and light chain encoding genes. The process starts with immunization of rabbits with the desired antigen, followed by isolation and propagation of peripheral blood mononuclear cells (PBMCs). The DNA from these cells is then cloned as a library and further screened using desired end-application to select an exceptional candidate for antibody production. The shortlisted DNA libraries are then scaled-up in vitro using mammalian cell culture followed by large-scale antibody production.

Figure 1. Recombinant rabbit polyclonal antibody production.


Advantages of recombinant rabbit polyclonal antibodies

Recombinant rabbit polyclonal antibodies, generated using recombinant DNA technology, offer distinct advantages over conventional rabbit polyclonal antibodies. They provide precise control and modification of the antibody sequence, helping ensure accurate targeting. Moreover, recombinant antibodies exhibit excellent lot-to-lot reproducibility as they are derived from banked DNA, avoiding cell drift and maintaining consistent expression patterns. These antibodies also demonstrate enhanced specificity and sensitivity due to advanced screening processes, resulting in optimal binding capabilities. In contrast, conventional rabbit polyclonal antibodies may exhibit variability between production lots and have limited customization options. The unique features of recombinant rabbit polyclonal antibodies make them a valuable choice for researchers seeking reliable, consistent, and customizable antibody solutions.

Improved specificity and sensitivity

Recombinant rabbit polyclonal antibodies provide exceptional specificity and sensitivity. These antibodies undergo a comprehensive screening process to evaluate their binding capabilities and those clones with the highest affinity for the target molecule are selected. This stringent selection process helps ensure that the recombinant rabbit polyclonal antibodies specifically recognize and bind to the intended target with precision.

For instance, let's consider the example of the SOD1 Recombinant Polyclonal Antibody (Figure 1). This antibody has been successfully employed to detect SOD1 protein across various cell lines, demonstrating its versatility and reliability in different experimental settings. Additionally, the antibody exhibits remarkable specificity, as evidenced by the results obtained from siRNA mediated knockdown analysis. Even under conditions where the expression of the target protein is reduced, this recombinant rabbit monoclonal antibody maintains high specificity, helping to ensure accurate and reliable detection.

Improved antibody performance in multiple applications

Most recombinant rabbit polyclonal antibodies undergo an extensive functional validation process to ensure optimal performance across various applications, such as western blot, immunocytochemistry, flow cytometry, and immunohistochemistry. This thorough validation helps ensure that our antibodies consistently deliver reliable and accurate results.

For example, in Figure 2, the c-Jun Recombinant Polyclonal Antibody (2HCLC) has undergone comprehensive validation in multiple applications. It has been extensively tested using western blot, immunocytochemistry, and chromatin immunoprecipitation to assess its functionality and specificity. Additionally, this antibody has been further evaluated for specificity through CRISPR-Cas9 knockout experiments. Through our rigorous validation procedures, we help ensure that antibodies meet the highest standards of quality and performance, helping provide researchers with reliable tools for their experiments.

Figure 2. Validation of c-Jun recombinant polyclonal antibody in different applications. A) Western blot analysis was performed on whole cell extracts of COLO 205 (Lane 1), U-937 (Lane 2), NIH/3T3 (Lane 3), HEK-293 (Lane 4) and PC-3 (Lane 5). The blots were probed with c-jun Recombinant Polyclonal Antibody (Cat. No. 711202) and detected by chemiluminescence using Goat anti-Rabbit IgG (Heavy Chain), Superclonal Recombinant Secondary Antibody, HRP (Cat. No. A27036). A 43 kDa band corresponding to c-jun was observed across cell lines tested. B) Immunofluorescence analysis was performed on PC-3 cells for detection of endogenous c-jun using the same primary antibody. Panel a) shows representative cells that were stained for detection and localization of c-jun protein (green), Panel b) is stained for nuclei (blue) using DAPI. Panel c) represents cytoskeletal F-actin staining. Panel d) is a composite image of Panels a, b, and c clearly demonstrating nuclear localization of c-jun. Panel e) represents control cells with no primary antibody. C) Chromatin immunoprecipitation (ChIP) was performed using the same primary antibody on sheared chromatin from U-937 cells and U-937 cells treated with anisomycin. Normal Rabbit IgG (1 µg) was used as a negative IP control. Data is compared between untreated vs treated samples and is presented as fold enrichment of the antibody signal versus the negative control IgG using the comparative CT method. D) Knockout of c-Jun was achieved by CRISPR-Cas9 genome editing. Western blot analysis of c-Jun was performed by loading HEK-293 wild type (Lane-1), HEK-293 Cas9 (Lane-2) and HEK-293 c-Jun KO (Lane-3) modified whole cell extracts. The blot was probed with the same c-Jun Recombinant Polyclonal Antibody and Goat anti-Rabbit IgG Superclonal Recombinant Secondary Antibody, HRP as above. Loss of signal upon CRISPR mediated knockout (KO) using the LentiArray CRISPR product line confirms that the antibody is specific to c-Jun.


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* The use or any variation of the word “validation” refers only to research use antibodies that were subject to functional testing to confirm that the antibody can be used with the research techniques indicated. It does not ensure that the product(s) was validated for clinical or diagnostic use.

For Research Use Only. Not for use in diagnostic procedures.

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