TRIM23 Antibody (monoclonal) (M01)
Mouse monoclonal antibody raised against a partial recombinant TRIM23.
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
---|---|
Primary Accession | P36406 |
Other Accession | BC022510 |
Reactivity | Human |
Host | mouse |
Clonality | Monoclonal |
Isotype | IgG2b Kappa |
Clone Names | 2H4 |
Calculated MW | 64067 Da |
Gene ID | 373 |
---|---|
Other Names | E3 ubiquitin-protein ligase TRIM23, 632-, ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, RING finger protein 46, Tripartite motif-containing protein 23, TRIM23, ARD1, ARFD1, RNF46 |
Target/Specificity | TRIM23 (AAH22510, 1 a.a. ~ 110 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. |
Dilution | WB~~1:500~1000 |
Format | Clear, colorless solution in phosphate buffered saline, pH 7.2 . |
Storage | Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. |
Precautions | TRIM23 Antibody (monoclonal) (M01) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Background
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described.
References
1.Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense.Arimoto K, Funami K, Saeki Y, Tanaka K, Okawa K, Takeuchi O, Akira S, Murakami Y, Shimotohno K.Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15856-61. Epub 2010 Aug 19.
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