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The protein encoded by RNF139 is a multi-membrane spanning protein containing a RING-H2 finger. Additionally we are shipping Ring Finger Protein 139 Proteins (4) and many more products for this protein.
Showing 10 out of 56 products:
Human Monoclonal RNF139 Primary Antibody for WB - ABIN393698
Lee, Brauweiler, Rudolph, Hooper, Drabkin, Gemmill: The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. in Molecular cancer research : MCR 2010
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Human Polyclonal RNF139 Primary Antibody for ELISA, WB - ABIN564886
Brauweiler, Lorick, Lee, Tsai, Chan, Weissman, Drabkin, Gemmill: RING-dependent tumor suppression and G2/M arrest induced by the TRC8 hereditary kidney cancer gene. in Oncogene 2007
Show all 4 references for 564886
Human Monoclonal RNF139 Primary Antibody for IHC (p), ELISA - ABIN564887
Adams, Simms, Abdelhamed, Dawe, Szymanska, Logan, Wheway, Pitt, Gull, Knowles, Blair, Cross, Sayer, Johnson: A meckelin-filamin A interaction mediates ciliogenesis. in Human molecular genetics 2012
Cow (Bovine) Polyclonal RNF139 Primary Antibody for WB - ABIN2774685
Poland, Azim, Folsom, Goldfarb, Naeem, Korch, Drabkin, Gemmill, Plon: A constitutional balanced t(3;8)(p14;q24.1) translocation results in disruption of the TRC8 gene and predisposition to clear cell renal cell carcinoma. in Genes, chromosomes & cancer 2007
interaction with Bag1 (show BAG1 Antibodies) then shifts hERG (show KCNH2 Antibodies) degradation to the membrane-anchored E3 ligase TRC8 and its E2-conjugating enzyme Ube2g2 (show UBE2G2 Antibodies), as determined by siRNA screening
TRC8 and TMEM129 are endoplasmic reticulum-associated degradation ubiquitin E3 ligases for viral and cellular targeting of MHC class I. (Review)
TRC8 suppresses tumorigenesis through targeting heme oxygenase-1 (show HMOX1 Antibodies) for ubiquitination and degradation.
TRC8 function may provide a regulatory link between the lipid and protein biosynthetic pathways.
TRC8 modulation of sterol response element binding protein activity comprises a novel regulatory link between growth control and the cholesterol/lipid homeostasis pathway.
The presence of diploid and tetraploid tumor cells with and without TRC8 deletions on the nontranslocated chromosome suggest that loss of the remaining normal allele of TRC8 may contribute to tumor development at later stages.
TRC8 is a novel sterol-sensing endoplasmic reticulum membrane protein (show SLC39A6 Antibodies) that hinders SREBP-2 (show SREBF2 Antibodies) processing through interaction with SREBP-2 (show SREBF2 Antibodies) and SCAP (show SH2D2A Antibodies), regulating its own turnover rate by means of its E3 ubiquitin ligase (show MUL1 Antibodies) activity
Data show that the TRC8 E3 ligase is required for MHC I dislocation from the ER and identify a new complex associated with mammalian ERAD.
The protein encoded by this gene is a multi-membrane spanning protein containing a RING-H2 finger. This protein is located in the endoplasmic reticulum, and has been shown to possess ubiquitin ligase activity. This gene was found to be interrupted by a t(3:8) translocation in a family with hereditary renal and non-medulary thyroid cancer. Studies of the Drosophila counterpart suggested that this protein may interact with tumor suppressor protein VHL, as well as with COPS5/JAB1, a protein responsible for the degradation of tumor suppressor CDKN1B/P27KIP.
ring finger protein 139
, E3 ubiquitin-protein ligase RNF139
, multiple membrane spanning receptor TRC8
, patched related protein translocated in renal cancer
, translocation in renal carcinoma on chromosome 8 protein
, RING finger protein 139