Analytical Data
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Gene name
TRIM72
- Application
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Alternative Names
MG53
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZMU5-1
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Expression Region
S2-A477
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Protein Length
Partial
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Molecular Weight
54.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
