Analytical Data
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基因名
TRIM72
- Application
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别名
MG53
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6ZMU5-1
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表达区间
S2-A477
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蛋白长度
Partial
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分子量
54.8 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TRIM72, a member of the TRIM (tripartite motif-containing) protein family, has gained significant attention in recent years due to its pivotal role in various biological processes, including muscle development, metabolism, and cellular stress response. Initially discovered for its involvement in skeletal muscle homeostasis, TRIM72 has been found to modulate autophagy and act as a critical regulator of inflammation and immune responses. The protein's unique structural features, characterized by a RING domain, two B-boxes, and a coiled-coil region, facilitate its function as an E3 ubiquitin ligase, allowing it to regulate protein turnover by tagging substrates for degradation. Given the association of TRIM72 dysfunction with several conditions, including muscular dystrophies and metabolic disorders, researchers are increasingly focusing on the therapeutic potential of TRIM72. Recombinant TRIM72 protein studies enable a deeper understanding of its molecular mechanisms, effects on cellular pathways, and potential as a biomarker or therapeutic target. Investigations utilizing TRIM72 reconstitution models highlight the implications of its activity in modulating key signaling pathways, offering insights into muscle regeneration and immune modulation. As research continues to elucidate the multifaceted roles of TRIM72, it presents exciting possibilities for developing novel strategies in treating related diseases, underscoring the significance of this protein in health and disease.












