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Recombinant Human Tripartite motif-containing protein 72 (TRIM72), partial
Recombinant Human Tripartite motif-containing protein 72 (TRIM72), partial
- 中文名称：
- Recombinant Human Tripartite motif-containing protein 72 (TRIM72), partial
- 英文名称：
- Recombinant Human Tripartite motif-containing protein 72 (TRIM72), partial
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA243737
- 规格：
- 0.02 mg (E-Coli)|0.1 mg (E-Coli)|1 mg (E-Coli)|5x1 mg (E-Coli)|
- 保存建议：
- The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20 degree C/-80 degree C.
The shelf life of lyophilized form is 12 months at -20 degree C/-80 degree C.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.
- 货期：
- 6-8周
- 纯度：
- Greater or equal to 85% purity as determined by SDS-PAGE.
- 产品形式：
- Liquid or Lyophilized powder
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, p
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
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 Ca2+-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
