| KCNA2 antibodies | |
| This is a review about KCNA2 antibodies, based on 3 published articles using KCNA2 antibodies in western blot, immunohistochemistry, immunoprecipitation, immunocytochemistry, and other immunological technologies. It is aimed to help ExactAntigen visitors find the most suited KCNA2 antibody. Information in this review (with links to publications) can be searched freely. |
MILLIPORE search Millipore KCNA2 products includes other brands or spellings
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| ic, ip, wb | | Upstate Biotechnology mouse monoclonal antibody (aKv-i) raised against the nearly complete C terminus (aa 428-499) of Kv1.2 is used in western blot, immunoprecipitation and immunocytochemistry to demonstrate a dynamic, phosphorylation-dependent interaction between Kv1.2 and the actin cytoskeleton-binding protein cortactin. |
| ih | | Upstate KCNA2 antibody was tested in immunohistochemistry by HPA (CAB001976) . |
| wb | | Upstate Biotechnology mouse anti-Kv1.2 monoclonal antibody was used in western blot to study the allowed N-glycosylation sites on the Kv1.2 potassium channel S1–S2 linker. |
INVITROGEN search Invitrogen KCNA2 products includes other brands or spellings
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| ic, ip | | BIOSOURCE International rabbit polyclonal antibody (aKv-e) directed against a peptide encoding a portion of the first extracellular loop (aa 192-208) of Kv1.2 is used in immunoprecipitation and immunocytochemistry to demonstrate a dynamic, phosphorylation-dependent interaction between Kv1.2 and the actin cytoskeleton-binding protein cortactin. |
Articles Reviewed |
| 1. David Hattan et al. Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin. 2002 |
| 2. Jing Zhu et al. Allowed N-glycosylation sites on the Kv1.2 potassium channel S1-S2 linker: implications for linker secondary structure and the glycosylation effect on channel function. 2003 |
| 3. Anja Persson et al. A human protein atlas based on antibody proteomics. 2006 |
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