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In the diagnostic field, it is important to know which antibody is against to the carboxyl, the NH2 or the rod domain. However, It is not clear to me and to some customers (because I reviewed the answers posted in the website) the bunch of antibodies you offer are directed to.
It is mentioned they share reactivity to the transmembrane part or are associated or share affinity to the other dystrophin associated proteins, but specifically the question is not answered.
I wonder if you do not mind, to explain me the specific affinity of the antibody (rod, NH2, COOH domains) the antibodies are directed.
Asked on May 11 2017
Thank you for your inquiry.
Based on its primary structure, the dystrophin can be divided into four distinct structural domains: (1) the N-terminal actin-binding domain (aa 14-240), (2) the large triple helical spectrin-like domain (aa 253-3040) composed of 24 repeating units similar to those in β-spectrin, which are predicted to form triple-helical coiled-coils, (3) the cysteine-rich domain (aa 3080- 3360) and the C-terminal domain (aa 3361- 3685). http://www.sciencedirect.com/science/article/pii/0092867488903832
Please find information on the location of the immunogens by antibody below:
ab129996: epitope not mapped to our knowledge
ab14452: epitope not mapped to our knowledge
ab85302: spectrin-like domain/ rod
Please note the above antibodies are tested and guaranteed for different species and applications. Please choose carefully. If you let me know what species your samples are from and what application you are planning I will be happy to help choose the most suitable antibody.
Importantly, I also have to confirm that all our products are for research purposes only and are not intended for diagnostic or therapeutic use.
Answered on May 11 2017