epitope corresponding to amino acids 119-194 mapping near the N-terminus of rhophilin isoform 3 of human origin
Modification Notes
Rho, the Ras-related small GTPase, is responsible for the regulation of Actin-based cytoskeletal structures, including stress fibers, focal adhesions and the contractile ring apparatus. Rho proteins act as molecular switches which are able to turn cytokinesis on and off. Although little is known about signaling downstream of Rho, several proteins have been implicated as Rho effectors. Protein kinase N (PKN) is a fatty acid-activated serine/threonine kinase whose catalytic domain exhibits homology with that of the PKC family. PKN associates with Rho via its amino-terminus, is activated in a GTP-dependent manner and phosphorylates the head-rod domain of neurofilament proteins. A second protein, rhophilin, exhibits 40% sequence identity with the amino-terminal Rho binding domain. The enzymatic activity of rhophilin has not been demonstrated and it is possible that it acts through the recruitment of cytoskeletal components that initiate a kinase signaling cascade. Citron interacts specifically with active Rho and Rac 1 but not Cdc42. Citron exhibits a distinctive protein organization and little homology with the Rho binding domains of PKN and rhophilin.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of all rhophilin isoforms of 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 119-194 mapping near the N-terminus of rhophilin isoform 3 of human origin
Tissue Specificity
epitope corresponding to amino acids 119-194 mapping near the N-terminus of rhophilin isoform 3 of human origin