TRIM24 Protein (AA 891-1012, partial) (His tag)
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- Target See all TRIM24 Proteins
- TRIM24 (Tripartite Motif Containing 24 (TRIM24))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 891-1012, partial
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Origin
- Human
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Source
- Yeast
- Purification tag / Conjugate
- This TRIM24 protein is labelled with His tag.
- Application
- SDS-PAGE (SDS)
- Sequence
- KKKTEGLVKL TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYS KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLENYFEEL LKNLYPEKRF PK
- Purification
- SDS-PAGE
- Purity
- > 90 %
- Top Product
- Discover our top product TRIM24 Protein
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Tripartite Motif Containing 24 (TRIM24) (AA 1-1050) protein (GST tag)
TRIM24 Origin: Human Host: Wheat germ Recombinant ELISA, WB, AA, AP
Tripartite Motif Containing 24 (TRIM24) (AA 896-1014) protein (His tag)TRIM24 Origin: Human Host: Escherichia coli (E. coli) Recombinant Greater than 95 % as determined by SDS-PAGE ELISA, WB
Tripartite Motif Containing 24 (TRIM24) (AA 432-569) protein (GST tag)TRIM24 Origin: Human Host: Wheat germ Recombinant ELISA, WB, AA, AP
Tripartite Motif Containing 24 (TRIM24) (AA 1-1050) protein (Strep Tag)Crystallography grade TRIM24 Origin: Human Host: Tobacco (Nicotiana tabacum) Recombinant >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, WB, SDS
Tripartite Motif Containing 24 (TRIM24) (AA 1-1051) protein (Strep Tag)Crystallography grade TRIM24 Origin: Mouse Host: Tobacco (Nicotiana tabacum) Recombinant ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, WB, SDS
Tripartite Motif Containing 24 (TRIM24) (AA 891-1012), (partial) protein (His-SUMO Tag)TRIM24 Origin: Human Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
Tripartite Motif Containing 24 (TRIM24) (AA 862-980) protein (His tag,DYKDDDDK Tag)TRIM24 Origin: Human Host: Escherichia coli (E. coli) Recombinant Bind, ScA
Tripartite Motif Containing 24 (TRIM24) (AA 891-1012), (partial) protein (His tag)TRIM24 Origin: Human Host: Yeast Recombinant > 90 % SDS
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.1-2 mg/mL
- Buffer
- 20 mM Tris-HCl based buffer, pH 8.0
- Storage
- -80 °C,4 °C,-20 °C
- Storage Comment
- Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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- Target
- TRIM24 (Tripartite Motif Containing 24 (TRIM24))
- Alternative Name
- TIF1A (TRIM24 Products)
- Synonyms
- TRIM24 Protein, PTC6 Protein, RNF82 Protein, TF1A Protein, TIF1 Protein, TIF1A Protein, TIF1ALPHA Protein, hTIF1 Protein, ptc6 Protein, rnf82 Protein, tf1a Protein, tif1 Protein, tif1a Protein, tif1alpha Protein, A130082H20Rik Protein, AI447469 Protein, D430004I05Rik Protein, TIF1-alpha Protein, TIF1alpha Protein, Tif1a Protein, tripartite motif containing 24 Protein, transcription intermediary factor 1-alpha Protein, tripartite motif containing 24 S homeolog Protein, tripartite motif-containing 24 Protein, TRIM24 Protein, trim24 Protein, LOC100548578 Protein, trim24.S Protein, Trim24 Protein
- Background
- Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes .
- Molecular Weight
- 16.48 kDa
- UniProt
- O15164
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