R0281
RNF11 human
recombinant, expressed in E. coli (histidine-tagged), ≥90% (SDS-PAGE), buffered aqueous solution
Synonym(s):
CGI-123, MGC51169, RING Finger Protein 11, SID1669
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About This Item
UNSPSC Code:
12352200
recombinant
expressed in E. coli (histidine-tagged)
assay
≥90% (SDS-PAGE)
form
buffered aqueous solution
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... RNF11(26994)
Biochem/physiol Actions
RNF11 (RING Finger Protein 11) is a RING E3 ubiquitin ligase with potential to mediate ubiquitination and subsequent proteolysis. RNF11 binds numerous proteins in a variety of cellular pathways, including TGFβ and EGFR signaling. RNF11 expression is elevated in breast and prostate cancer. RNF11 may represent an important target for novel cancer therapies.
Physical form
Solution in 50 mM Tris, pH 7.5, 150 mM NaCl, 1 mM DTT, and 30% glycerol (w/v).
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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Instructions
Michael K Connor et al.
Molecular cancer research : MCR, 3(8), 453-461 (2005-08-27)
Ring finger proteins serve many vital functions within the cell. We have identified RNF11, a novel 154-amino acid ring finger-containing protein, which is elevated in breast cancer. Within its ring finger domain, RNF11 contains an AKT phosphorylation site (T135) that
Michael K Connor et al.
Oncogene, 23(11), 2089-2095 (2004-03-17)
The identification of novel tumor-associated genes represents an important area of cancer research. To that end, we have discovered a number of genes whose expression is altered in breast tumors. One of these genes has been identified as the ring
Angelika Burger et al.
Neoplasia (New York, N.Y.), 8(8), 689-695 (2006-08-24)
Defects in ubiquitin E3 ligases are implicated in the pathogenesis of several human diseases, including cancer, because of their central role in the control of diverse signaling pathways. RING E3 ligases promote the ubiquitination of proteins that are essential to