Anti-E3 ubiquitin-protein ligase RNF31

Evaluated by Western Blotting in Jurkat cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected E3 ubiquitin-protein ligase RNF31 in 10 µg of Jurkat cell lysate.

Anti-E3 ubiquitin-protein ligase RNF31, Cat. No. ABS1486, is a rabbit polyclonal antibody that detects E3 ubiquitin-protein ligase RNF31 and has been tested for use in Immunohistochemistry (Paraffin) and Western Blotting.

Immunohistochemistry Analysis: A 1:250 dilution from a representative lot detected E3 ubiquitin-protein ligase RNF31 in human adrenal gland and human uterus tissues.

Research Category
Signaling

This rabbit polyclonal antibody detects E3 ubiquitin-protein ligase RNF31 in human cells. It targets an epitope within 17 amino acids from the C-terminal region. Immunogen sequence is conserved in all 3 isoforms.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

E3 ubiquitin-protein ligase RNF31 (UniProt: Q96EP0; also known as EC: 2.3.2.27, HOIL-1-interacting protein, HOIP, RING finger protein 31, RING-type E3 ubiquitin transferase RNF31, Zinc in-between-RING-finger ubiquitin-associated domain protein) is encoded by the RNF31 (also known as ZIBRA) gene (Gene ID: 55072) in human. E3 ubiquitin-protein ligase RNF31 is a cytoplasmic protein that is a component of the linear ubiquitin chain assembly complex (LUBAC complex), which conjugates linear (′Met-1′-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG (NEMO) and receptor interacting serine/threonine Kinase 1 (RIPK1) and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. LUBAC-mediated polyubiquitination interferes with TNF-induced cell death and thereby prevents inflammation. Together with OUTLIN deubiquitinase, the LUBAC complex is also reported to regulate the canonical Wnt signaling pathway during angiogenesis. E3 ubiquitin-protein ligase RNF31 is expressed in both normal and transformed breast epithelial cell lines. It contains a polyubiquitin-binding (PUB) domain (aa 71-142) that mediates interaction with the PCNA-interacting motifs of C-terminus of the AAA+ ATPase p97 (VCP) and RNF31, with a strong preference for RNF3. It also has a ubiquitin-associated (UBA) domain (aa 564-615) that mediates association with RanBP-type and C3HC4-type zinc finger-containing protein 1 (RBCK1/HOIL1) via interaction with its ubiquitin-like (UBL) domain. (Ref.: Elliot, PR et al (2014). Mol. Cell 54(3); 335-48).

~120 kDa observed; 119.65 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Epitope: C-terminus

KLH-conjugated linear peptide corresponding to 17 amino acids from the C-terminal region of human E3 ubiquitin-protein ligase RNF31.

Concentration: Please refer to lot specific datasheet.

Affinity Purified

Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.