The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF138 (ring finger protein 138), also known as HSD4 or NARF, is a 245 amino acid protein that contains one RING-type zinc finger and functions as an E3 ubiquitin-protein ligase, playing an important role in protein ubiquitination. Expressed as multiple alternatively spliced isoforms, RNF138 interacts with Nlk and is thought to act as a negative regulator of the Wnt/∫-catenin-mediated signaling pathway. RNF138 may be auto-ubiquitinated and is subject to post-translational phosphorylation, probably by ATM or ATR.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of RNF138 of mouse and human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of RNF138 of mouse and human origin by WB, IP and ELISA