Analytical Data
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Gene name
TRIM7
- Application
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Alternative Names
TRIM7；GNIP；RNF90；E3 ubiquitin-Protein ligase TRIM7
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9C029
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Expression Region
1-511aa
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AA Sequence
MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP
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Molecular Weight
64.1 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
TRIM7, a member of the tripartite motif (TRIM) protein family, has garnered significant attention in recent years due to its potential roles in various biological processes and diseases. This protein is characterized by an N-terminal RING finger domain, followed by two B-box domains and a coiled-coil region, which are important for its E3 ubiquitin ligase activity. Research has shown that TRIM7 is involved in the regulation of immune responses, cellular signaling pathways, and the response to viral infections. Its ability to modulate protein stability through ubiquitination highlights its importance in maintaining cellular homeostasis and influencing pathophysiological conditions. In cancer, TRIM7 has been implicated in tumor progression and metastasis, making it a potential target for therapeutic intervention. Furthermore, studies suggest that TRIM7 might interact with various signaling molecules, influencing processes such as apoptosis and inflammation. Given its widespread implications in health and disease, understanding the structure and function of TRIM7, including the development of recombinant TRIM7 proteins, presents a valuable opportunity for advancing our knowledge in molecular biology and therapeutic strategies. Researchers are motivated to explore TRIM7's functional mechanisms and its relevance in clinical contexts, paving the way for future studies that may contribute to novel treatments for diseases associated with TRIM7 dysregulation.
