epitope corresponding to amino acids 42-110 mapping near the N-terminus of Ral GDS of human origin
Modification Notes
Ral A and Ral B constitute a distinct subfamily of Ras-related GTPases (i.e., GDP/GTP binding proteins) (1-3). Ral proteins are activated by a unique nucleotide exchange factor, Ral GDS, and deactivated by a distinct GTPase-activating protein (4,5). Unlike Ras proteins, Ral A and Ral B fail to induce transformed foci when activated variants are expressed in various recipient cells (1). A potential downstream target of Ral, designated Ral BP-1, has been shown to contain a Rho-GTPase-activating domain (1). This Rho-GTPase-activating domain interacts preferentially with the Rho family member Cdc42 (1). A Ras/Ral signaling pathway has been reported to mediate phospholipase D (PLD) activation by v-Src, thus indicating PLD as another downstream target of Ral A (6).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Ral GDS of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 42-110 mapping near the N-terminus of Ral GDS of human origin
Tissue Specificity
epitope corresponding to amino acids 42-110 mapping near the N-terminus of Ral GDS of human origin
Western blot analysis of Ral GDS expression in MIA PaCa-2 whole cell lysate.
Application
Western blot analysis of Ral GDS expression in non-transfected 293T: (A), mouse Ral GDS transfected 293T: (B) and HeLa (C) whole cell lysates.
Application Notes
recommended for detection of Ral GDS of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.