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TRIM33 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, IF, E |
|---|---|
| Primary Accession | Q9UPN9 |
| Other Accession | NP_056990, 74027249 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | Predicted: 70, 124 kDa Observed: 70 kDa |
| Application Notes | TRIM33 antibody can be used for detection of TRIM33 by Western blot at 1 - 2 µg/mL. |
| Gene ID | 51592 |
|---|---|
| Target/Specificity | TRIM33; TRIM33 antibody is human, mouse and rat reactive. At least two isoforms of TRIM33 are known to exist. |
| Reconstitution & Storage | TRIM33 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
| Precautions | TRIM33 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TRIM33 |
|---|---|
| Synonyms | KIAA1113, RFG7, TIF1G |
| Function | Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade). |
| Cellular Location | Nucleus. Note=In discrete nuclear dots resembling nuclear bodies (By similarity). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000250|UniProtKB:Q99PP7, ECO:0000269|PubMed:25593309} |
| Tissue Location | Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
TRIM33 Antibody: TRIM24 (TIF1alpha), TRIM28 (TIF1beta), and TRIM33 (TIF1gamma) are three related cofactors belonging to the tripartite motif superfamily that interact with distinct transcription factors (1-2). The structure of TRIM33 is similar to TRIM24 and TRIM28, exhibiting multiple domains (RING finger, coiled coil, B boxes, PHD/TTC, and bromodomain) (3). TRIM33 functions in cell differentiation and development, playing a role in differentiation of hematopoietic cells (3). It interacts with the Smad2/3 transcription factor in hematopoietic, mesenchymal, and epithelial cell types to mediate different transcriptional effects in response to TGF-beta (4). It acts as an E3 ubiquitin-protein ligase and promotes SMAD4 ubiquitination (5).
References
Ransom DG, Bahary N, Niss K, et al. The zebrafish moonshine gene encodes transcriptional intermediary factor 1gamma, an essential regulator of hematopoiesis. PLoS Biol. 2004; 2:E237.
Herquel B, Ouararhni K, Khetchoumian K, et al. Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma. Proc. Natl. Acad. Sci. USA 2011; 108:8212-7.
He W, Dorn DC, Erdjument-Bromage H, et al. Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway. Cell 2006; 125:929-41.
Dupont S, Inui M, Newfeld SJ. Regulation of TGF-β signal transduction by mono- and deubiquitylation of Smads. FEBS Lett. 2012; 586:1913-20.
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