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Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. Additionally we are shipping Ras-Related GTP Binding B Proteins (4) and many more products for this protein.
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Inhibition of glutaminolysis prevents GTP (show AK3 Antibodies) loading of RagB and lysosomal translocation and subsequent activation of mTORC1.
RagA (show RRAGA Antibodies) and RagB are key regulators of lysosomal function and cardiac protection.
Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified.
Ras-related GTP binding B
, ras-related GTP-binding protein A
, Ras-related GTP binding A
, ras-related GTP-binding protein B
, GTP-binding protein ragB
, rag B