RRAS2 polyclonal antibody

H-, K- and N-Ras represent the prototype members of a family of small G proteins that are frequently activated to an oncogenic state in a wide variety of human tumors. Activation is due to point mutations at either position 12 or 61 within their coding sequence. Such mutations cause these proteins to be constitutively converted to their active GTP-bound, rather than the inactive GDP-bound, state. The related human R-Ras gene was initially cloned by low stringency hybridization methods. Position 38 and 87 (analogous to position 12 and 61 in H-Ras) mutants of R-Ras have been shown to be capable of activating oncogenic function. An additional member of the Ras oncogene family, designated TC 21 (or R-Ras-2) is most closely related to R-Ras. While wild type TC 21 does not exhibit transforming potential in vitro, mutant forms of TC 21 that possess amino acid substitutions analogous to those that activate Ras oncogenic potential, exhibit potent transforming activities comparable to the activity characteristic of the known oncogenic Ras proteins.