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>   首页   >   产品   >   一抗   >   干细胞   >   TRIM33 Antibody (C-term)   

TRIM33 Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - TRIM33 Antibody (C-term) AP12056b
    TRIM33 Antibody (C-term) (Cat. #AP12056b) western blot analysis in MDA-MB435 cell line lysates (35ug/lane).This demonstrates the TRIM33 antibody detected the TRIM33 protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q9UPN9
Other Accession Q99PP7, NP_148980.2, NP_056990.3
Reactivity Human
Predicted Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 122533 Da
Antigen Region 1095-1125 aa
Additional Information
Gene ID 51592
Other Names E3 ubiquitin-protein ligase TRIM33, 632-, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G
Target/Specificity This TRIM33 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1095-1125 amino acids from the C-terminal region of human TRIM33.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTRIM33 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

The protein encoded by this gene is thought to be a transcriptional corepressor. However, molecules that interact with this protein have not yet been identified. The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined.

REFERENCES

Bai, X., et al. Cell 142(1):133-143(2010)
Howard, P.W., et al. Biochem. Biophys. Res. Commun. 396(3):674-678(2010)
Vincent, D.F., et al. PLoS Genet. 5 (7), E1000575 (2009) :
Dupont, S., et al. Cell 136(1):123-135(2009)
Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)

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