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Cross reactivity antibody1/8/2024 ![]() ![]() Moreover, our α-TOR antibody is useful for coimmunoprecipitation assays. Antiserum was purified by an antigen-specific purification method, and the purified polyclonal α-TOR antibody successfully detected endogenous TOR proteins in wild-type Arabidopsis and TOR orthologous in major crop plants, including tomato, maize, and alfalfa. coli, and a mixture of proteins (at a 1:1 ratio) was used for immunizing rabbits. ![]() Recombinant His-TOR 1−200 and His-TOR 1113−1304 proteins were individually expressed in E. Here, we produced a polyclonal α-TOR antibody using two truncated variants of TOR (1–2–1304 amino acids) as antigens because recombinant full-length TOR is challenging to express in Escherichia coli. Moreover, a lack of reliable molecular and biochemical assay tools limits our ability to explore TOR functions in plants. In Arabidopsis thaliana, the loss-of-function tor mutant displays embryo lethality, but the precise mechanisms of TOR function are still unknown. TOR was first identified in yeast mutant screens, as its mutants conferred resistance to rapamycin, an antibiotic with immunosuppressive and anticancer activities. ![]() TOR plays a role as a master regulator that integrates nutrient, energy, and stress signaling to orchestrate development. TARGET OF RAPAMYCIN (TOR), a member of the phosphatidylinositol 3-kinase-related family of protein kinases, is encoded by a single, large gene and is evolutionarily conserved in all eukaryotes. ![]()
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