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Also for TRKCT1 (NM_008746)
|This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids near the carboxyl terminus of mouse TrkCT1 protein.|
|human, mouse, rat
||ELISA: 1:5,000 - 1:20,000, WB: 1:1,000 - 1:10,000, IP: 1 ug
|0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2|
|This antibody is suitable for Cancer, Immunology and Nuclear Signaling research. TrkCT1, also named neurotrophic tyrosine kinase receptor type 3 (Ntrk3) non-catalytic isoform 2, is a non-catalytic isoform of TrkC, the high affinity receptor for Neurotrophin-3 (NT-3). This isoform lacks the kinase domain that is responsible for signaling by the full-length isoform. TrkCT1 is the product of an alternative splicing of Ntrk3 that leaves the extracellular and transmembrane domains intact but includes a shorter intracellular domain encoded by exons 13b and 14b. Recent studies indicate that the short cytoplasmic tail binds the scaffold protein Tamalin in a ligand-dependent manner and further activates the Arf6–Rac1 signaling pathway (Esteban et al., 2006).
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Western blot using affinity purified anti-TrkCT1 to detect over-expressed TrkCT1 in HEK293 cells (Lane 2, arrowhead). Lane 1 is a non-transfected control. Cell extracts were resolved by electrophoresis and transferred to nitrocellulose. The membrane was probed with the primary antibody at a 1:3,000 dilution. Personal Communication, V. Coppola, CCR-NCI, Frederick, MD.
Mouse cortex lysate was immunoprecipitated with anti-TrkCT1 antibody and further blotted with affinity purified anti-TrkCT1. Lane 1 is wild-type cortex lysate, Lane 2 is Tamalin knock-out cortex lysate, and Lane 3 is TrkCT1 knock-out cortex lysate. The membrane was probed with the primary antibody at a 1:6,000 dilution. Personal Communication, V. Coppola, CCR-NCI, Frederick, MD.
Western blot using affinity purified anti-TrkCT1 to detect endogenous TrkCT1 in mouse cortex lysate (Lane 1). Lane 2 is TrkCT1 knock-out cortex lysate. Cell extracts were resolved by electrophoresis and transferred to nitrocellulose. The membrane was probed with the primary antibody at a 1:6,000 dilution. Personal Communication, V. Coppola, CCRNCI, Frederick, MD.