The Ras-encoded family of proteins bind GDP and GTP with high affinity. They possess a low level of intrinsic GTPase activity that increases more than 100-fold when interacting with cytosolic GTPase activating protein (GAP). Ras family members include H-Ras, K-Ras, N-Ras, M-Ras, R-Ras, E-Ras, Rheb, TC 21, RASL11B, and Rad (Ras associated with diabetes) GTPase. Rad GTPase is a GTP-binding protein that is similar to Ras but has unique features. Unlike other small GTPases, Rad GTPase lacks typical prenylation motifs at its C terminus. The Rad GTPase enzyme binds calmodulin, inhibits vascular lesion formation, has low intrinsic GTPase activity and cannot be stimulated by any known GAP molecules. Rad GTPase is expressed in skeletal muscle, cardiac muscle and lung tissues and is overexpressed in the skeletal muscle tissue of individuals with type II diabetes. It is also expressed to a lesser extent in the placenta, adipose tissue and kidney.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Rad GTPase of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-143 mapping at the N-terminus of Rad GTPase of human origin
Tissue Specificity
epitope corresponding to amino acids 1-143 mapping at the N-terminus of Rad GTPase of human origin