Analytical Data
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Gene name
TRIM69
- Application
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Alternative Names
RFP-like domain-containing protein trimless RING finger protein 36 Tripartite motif-containing protein 69
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86WT6
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Expression Region
1-341aa
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Molecular Weight
66.3 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
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Protein Description
TRIM69 is a member of the tripartite motif (TRIM) protein family, which is recognized for its diverse roles in various cellular processes, including immune response, cell proliferation, and apoptosis. The TRIM family proteins are characterized by a RING finger domain, which is crucial for their E3 ubiquitin ligase activity, enabling them to modulate protein stability and function through ubiquitination. Research into TRIM69 is particularly significant due to its potential implications in cancer biology and infectious diseases. Initial studies have indicated that TRIM69 may play a role in regulating innate immunity by influencing the signaling pathways activated in response to viral infections. Additionally, TRIM69 has been implicated in modulating cellular stress responses, which could link it to oncogenic processes. Given the complex interplay between TRIM proteins and various signaling pathways, the recombinant expression of TRIM69 is essential for elucidating its functional mechanisms and biological significance. Producing TRIM69 as a recombinant protein allows for detailed structural and functional analyses, paving the way for understanding its interactions with other cellular proteins and components. Consequently, the exploration of TRIM69 can contribute to the development of targeted therapies aimed at leveraging its role in disease processes, making it a compelling subject for further research in molecular biology and therapeutic applications.
