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Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 µg per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Application Notes:
Additional reported applications (for the relevant formats) include: intracellular flow cytometry1, ELISA1, and immunofluorescence microscopy2.
Application References:
1. Huynh T, et al. 2001. Scand. J. Immunol. 54:146. 2. Kirchgessner H, et al. 2001. J. Exp. Med. 193:1269.
Extracts from peripheral blood mononuclear cells were resolved by electrophoresis, transferred to nitrocellulose, and probed with mouse monoclonal antibody against TRIM. Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.
TRIM is a 30 kD disulfide-linked protein also known as T cell receptor interacting molecule. TRIM is a type III membrane protein containing a very short extracellular domain (8 amino acids). TRIM is highly expressed in T cells with some expression also observed in NK cells. TRIM is a signaling adaptor molecule that links extracellular and intracellular signaling. The TRIM protein is phosphorylated by Src kinases and associates with the PI3K regulatory subunit α after phosphorylation. TRIM has also been shown to associate with TCRα,β, and ?. The TRIM-4 monoclonal antibody recognizes human TRIM and has been shown to be useful for Western blotting, intracellular staining by flow cytometry, and immunofluorescence staining.
Other Names:
T cell receptor-interacting molecule
Structure:
Type III membrane protein, 30 kD disulfide-linked dimeric phosphoprotein
Distribution:
T cells, lower expression levels in NK cells
Function:
Links extracellular and intracellular signaling pathways in T cell activation
Modification:
Tyrosine phosphorylation by Src kinases
Interaction:
TCRβ, PI3K regulatory subunit α, TCR?, TCRα
Antigen References:
1. Bruyns E, et al. 1998. J. Exp. Med. 188:561. 2. Hubener C, et al. 2000. Immunogenetics 51:154.
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-TRIM
Extracts from peripheral blood mononuclear cells were resolved by electrophoresis, transferred to nitrocellulose, and probed with mouse monoclonal antibody against TRIM. Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.
