TRIM17 (Terf) is an E3 ubiquitin ligase that mediates Mcl-1 degradation and initiates apoptosis in neurons. Terf can also facilitate the degradation of ZWINT (a kinetochore protein) and decrease the proliferation of MCF7 breast cancer cells. Rabbit Anti-TRIM17 antibody recognizes human TRIM17.
Immunogen
Synthetic peptide directed towards the C terminal region of human TRIM17
Application
Rabbit Anti-TRIM17 (AB2) antibody is suitable for western blot applications at a concentration of 1.25 μg/ml.
Biochem/physiol Actions
TRIM17 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein is expressed almost exclusively in the testis, but its function is unknown. Multiple alternatively spliced transcript variants have been found for this gene.
Sequence
Synthetic peptide located within the following region: PKCPENGFWVVQLSKGTKYLSTFSALTPVMLMEPPSHMGIFLDFEAGEVS
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
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.
Journal of biochemistry, 151(2), 139-144 (2011-10-26)
Terf/TRIM17 is a tripartite motif protein that has been originally isolated from testis. Terf has been characterized to exhibit an E3 ubiquitin ligase activity and to undergo self-ubiquitination. The cellular function of terf and its substrates, however, remain elusive. In
Cell death and differentiation, 17(12), 1928-1941 (2010-06-19)
Accumulating data indicate that the ubiquitin-proteasome system controls apoptosis by regulating the level and the function of key regulatory proteins. In this study, we identified Trim17, a member of the TRIM/RBCC protein family, as one of the critical E3 ubiquitin
Cell death and differentiation, 20(2), 281-292 (2012-09-15)
Short-term proteasome inhibition has been shown to prevent neuronal apoptosis. However, the key pro-survival proteins that must be degraded for triggering neuronal death are mostly unknown. Here, we show that Mcl-1, an anti-apoptotic Bcl-2 family member, is degraded by the
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