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TRIP6 is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. Additionally we are shipping TRIP6 Proteins (6) and TRIP6 Kits (3) and many more products for this protein.
Showing 10 out of 88 products:
Cow (Bovine) Polyclonal TRIP6 Primary Antibody for WB - ABIN2784547
Johnson, Bai, Smith, Patel, Wang: Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase. in Cell 2007
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Human Monoclonal TRIP6 Primary Antibody for FACS, ELISA - ABIN1098130
Willier, Butt, Richter, Burdach, Grunewald: Defining the role of TRIP6 in cell physiology and cancer. in Biology of the cell / under the auspices of the European Cell Biology Organization 2011
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Human Monoclonal TRIP6 Primary Antibody for IF, WB - ABIN968789
Murthy, Clark, Fortin, Shen, Banville: ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. in The Journal of biological chemistry 1999
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Cow (Bovine) Polyclonal TRIP6 Primary Antibody for WB - ABIN2784548
Bai, Ohsugi, Abe, Yamamoto: ZRP-1 controls Rho GTPase-mediated actin reorganization by localizing at cell-matrix and cell-cell adhesions. in Journal of cell science 2007
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Human Polyclonal TRIP6 Primary Antibody for EIA, WB - ABIN783745
Kassel, Schneider, Heilbock, Litfin, Göttlicher, Herrlich: A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters. in Genes & development 2004
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Human Polyclonal TRIP6 Primary Antibody for ELISA, WB - ABIN563258
McMichael, Meyer, Lee: c-Src-mediated phosphorylation of thyroid hormone receptor-interacting protein 6 (TRIP6) promotes osteoclast sealing zone formation. in The Journal of biological chemistry 2010
the Trip6-GRIP1-myosin VI interaction and its regulation on F-actin network play a significant role in dendritic morphogenesis
TRIP6 overexpression promotes migration, invasion, and clonogenicity of Ewing's sarcoma cells
TRIP6 is involved in the regulation of nasopharyngeal carcinoma cell motility, and phosphorylation of tyrosine 55 residue plays an important regulatory role for this event
TRIP6 also promotes serum-induced reduction of nuclear p27(KIP1 (show CDKN1B Antibodies)) expression levels.
High TRIP6 expression is associated with malignant pleural mesothelioma.
TRIP6 is a nucleocytoplasmatic shuttle protein essential for the coordination of focal adhesion dynamics and transcriptional responses in lysophosphosphatidic (LPA (show APOA Antibodies)) and NF-kappaB (show NFKB1 Antibodies) signaling.
TRIP6 is an adaptor protein that regulates cell motility, antiapoptotic signaling and transcriptional activity. (Review)
TRIP6 promotes Fas (show FAS Antibodies)-mediated cell migration in apoptosis-resistant glioma cells. This effect is regulated via the Src (show SRC Antibodies)-dependent phosphorylation of TRIP6 at Tyr (show TYR Antibodies)-55.
the OIP-1 c-peptide is the functional domain of OIP-1
TRIP6 functions at a point of convergence between the activated LPA(2 (show LPAR2 Antibodies)) receptor and downstream signals involved in cell adhesion and migration
Our data suggest that TRIP6 regulates neural stem cell maintenance and it may be a new marker for neural stem cells.
Data show that OIP-1 (Trip6) is an important physiologic regulator of osteoclast development and may have therapeutic utility for bone diseases with high bone turnover.
TRIP6 is a critical downstream regulator of c-Src signaling and its phosphorylation is permissive for its presence in the sealing zone where it plays a positive role in osteoclast bone resorptive capacity
TRIP6 in lysophosphatidic acid signaling is regulated by c-Src (show SRC Antibodies)-mediated phosphorylation of TRIP6 at the Tyr (show TYR Antibodies)-55 residue.
nTrip6 interacts only with Fos family members. Consequently, nTrip6 is a selective coactivator for AP-1 dimers containing Fos. nTrip6 also assembles activated GR to c-Jun:c-Fos-driven promoters.
This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described\; however, not all variants have been fully characterized.
thyroid hormone receptor interactor 6
, thyroid receptor-interacting protein 6-like
, thyroid receptor-interacting protein 6
, OPA-interacting protein 1
, TR-interacting protein 6
, thyroid hormone receptor interacting protein 6
, zyxin related protein 1
, zyxin-related protein 1