Rabbit Anti-c-Myc (9E10)

This product is a plant-made, recombinant monoclonal antibody which offers several benefits including the following:

• Capable of detecting c-Myc and recombinant proteins fused to c-Myc tags, upwards of 2.5ng.
• No animals or animal products are used in the development of this protein.
• BSA and Azide free.

For more information on plant-made, recombinant monoclonal antibodies click here.

Figure 1. ELISA Dose Response curve showing increasing absorbance at 370 nm with increasing amounts of PtX™ Rabbit Anti-c-Myc (9E10) antibody added to a 96 well plate coated with 0.1 ng/ µl c-Myc tagged Antigen.

Figure 2. Western blot analysis of PtX™ Rabbit Anti-c-Myc (9E10). Lanes 2 – 6: Varying amounts of c-Myc tagged Serglycin protein were run on the SDS-PAGE. Separated bands were transferred to the membrane and PtX™ Rabbit Anti-c-Myc (9E10) (1: 2 000) was used to detect the antigen. The single bands of c-Myc tagged protein were visualized in each lane following the addition of anti-rabbit secondary antibody with HRP and substrate. Our antibody was able to detect antigen amounts upwards of 2.5 ng (Lane 5).

Figure 3. Immunocytochemistry: HeLa cells were plated at 200 000 cells/ well in 6-well plates on coverslips and allowed to adhere. Following fixing and blocking, cells were incubated with 1:200 dilution of Cape Biologix PtX™ Rabbit Anti-c-Myc primary antibody (Cat# CBT_A0007), and 1:300 dilution of a commercial Anti-Rabbit Alexa Fluor® 488 conjugated commercial secondary antibody. Cells were then stained with Hoechst 33342. Images were taken on a Zeiss LSM780 with ELYRA PS1 platform confocal microscope (60X) at the Stellenbosch University CAF unit. Thank you to Prof Georgia Schafer (ICGEB) for kindly donating the HeLa cells and Mrs Lize Engelbrecht for her outstanding assistance.

The biotechnology behind the development and manufacture of this product, transient plant-based expression, effectively turns Nicotiana benthamiana plants into single-use, biodegradable bioreactors. Infiltrating this plant species with Agrobacterium tumefaciens cells, transformed with our proprietary plant expression vectors, allows rapid production of a wide variety of recombinant proteins. Plants are harvested and proteins extracted by various stages of filtration, clarification, purification, and polishing – resulting in a highly functional final

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