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TRIM72 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q6ZMU5 |
|---|---|
| Clone Names | 100408357 |
| Gene ID | 493829 |
|---|---|
| Other Names | Tripartite motif-containing protein 72, Mitsugumin-53, Mg53, TRIM72 (HGNC:32671), MG53 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TRIM72 (HGNC:32671) |
|---|---|
| Synonyms | MG53 |
| Function | Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). |
| Cellular Location | Cell membrane, sarcolemma. Cytoplasmic vesicle membrane. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. |
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Provided below are standard protocols that you may find useful for product applications.
Background
TRIM72 is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
References
Park, E.Y., et al. Proteins 78(3):790-795(2010)Han, S., et al. Hum. Mol. Genet. 18(6):1171-1180(2009)Martin, J., et al. Nature 432(7020):988-994(2004)
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