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anti-Human TRAF3IP1 Antibodies:
anti-Rat (Rattus) TRAF3IP1 Antibodies:
anti-Mouse (Murine) TRAF3IP1 Antibodies:
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Cow (Bovine) Polyclonal TRAF3IP1 Primary Antibody for WB - ABIN610989
Garchon, Djabiri, Viard, Gajdos, Bach: Involvement of human muscle acetylcholine receptor alpha-subunit gene (CHRNA) in susceptibility to myasthenia gravis. in Proceedings of the National Academy of Sciences of the United States of America 1994
Show all 3 Pubmed References
Human Polyclonal TRAF3IP1 Primary Antibody for WB - ABIN525608
Texier, Toedt, Gorza, Mans, van Reeuwijk, Horn, Willer, Katsanis, Roepman, Gibson, Ueffing, Boldt: Elution profile analysis of SDS-induced subcomplexes by quantitative mass spectrometry. in Molecular & cellular proteomics : MCP 2014
Human Polyclonal TRAF3IP1 Primary Antibody for ELISA - ABIN449740
Niu, Murata, Watanabe, Kawakami, Yoshimura, Inoue, Puri, Kobayashi: MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation. in FEBS letters 2003
Human Polyclonal TRAF3IP1 Primary Antibody for IHC, IHC (p) - ABIN4361697
Bizet, Becker-Heck, Ryan, Weber, Filhol, Krug, Halbritter, Delous, Lasbennes, Linghu, Oakeley, Zarhrate, Nitschké, Garfa-Traore, Serluca, Yang, Bouwmeester, Pinson, Cassuto, Dubot, Elshakhs, Sahel et al.: Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization. ... in Nature communications 2015
Traf3ip1 is a negative regulator of microtubule stability. Microtubule defects caused by traf3ip1 KO are associated with altered epithelialization/polarity in renal cells and with pronephric cysts and microphthalmia in zebrafish embryos.
Data show that elipsa encodes a coiled-coil polypeptide that localizes to cilia, and that it interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8 (show RAB8A Antibodies), a small GTPase (show RACGAP1 Antibodies), known to localize to cilia.
Mutations in TRAF3IP1 are identified in patients with nephronophthisis and retinal degeneration. The identified mutations result in mild ciliary defects in patients and reveal a role of IFT54 as a negative regulator of microtubule stability via MAP4 (show MAP4 Antibodies).
MIP-T3 functions as a negative regulator of the innate type I interferon response by preventing TRAF3 (show TRAF3 Antibodies) from forming protein complexes with critical downstream transducers and effectors of antiviral response.
Data show that MIP-T3 protein level is highly regulated; mainly mediated by the ubiquitin-proteasome system.
The interaction of MIP-T3 with both actin filaments and microtubule suggested that MIP-T3 may play an important role in regulation of cytoskeleton dynamics in cells.
These results suggest that MIP-T3 is a novel inhibitor of IL-13 (show IL13 Antibodies) signaling and may be a useful molecule in ameliorating various conditions in which IL-13 (show IL13 Antibodies) plays a central role.
Homozygous Traf3ip1 mutants are not viable and have both neural developmental defects and polydactyly, phenotypes typical of mutants with ciliary assembly defects.
Data show that overexpression of IFT54/Traf3ip1 displaces IFT20 (show IFT20 Antibodies) from the Golgi apparatus. IFT54s effect on IFT20 (show IFT20 Antibodies) is a dominant negative phenotype caused by its overexpression.
Play an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity).
TRAF3-interacting protein 1
, TNF receptor-associated factor 3 interacting protein 1
, TRAF3-interacting protein 1-like
, interleukin 13 receptor alpha 1-binding protein-1
, interleukin-13 receptor alpha 1-binding protein 1
, microtubule interacting protein that associates with TRAF3
, microtubule-interacting protein associated with TRAF3
, microtubule-interacting protein that associates with TRAF3