Analytical Data
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Gene name
TRIM40
- Application
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Alternative Names
TRIM40; RNF35; Tripartite motif-containing Protein 40; Probable E3 NEDD8-Protein ligase; RING finger Protein 35
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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
Q6P9F5
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Expression Region
1-258 aa
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AA Sequence
MIPLQKDNQE EGVCPICQES LKEAVSTNCG HLFCRVCLTQ HVEKASASGV FCCPLCRKPC SEEVLGTGYI CPNHQKRVCR FCEESRLLLC VECLVSPEHM SHHELTIENA LSHYKERLNR RSRKLRKDIA ELQRLKAQQE KKLQALQFQV DHGNHRLEAG PESQHQTREQ LGALPQQWLG QLEHMPAEAA RILDISRAVT QLRSLVIDLE RTAKELDTNT LKNAGDLLNR SAPQKLEVIY PQLEKGVSEL LLQPPQKL
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Molecular Weight
29.3 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
Related Products
Protein Description
TRIM40, a member of the TRIM (Tripartite Motif-containing) protein family, has garnered significant attention in recent years due to its potential role in various biological processes, including cell proliferation, differentiation, and apoptosis. This E3 ubiquitin ligase is involved in the regulation of protein stability and signaling pathways, impacting fundamental cellular functions. Research has indicated that TRIM40 plays a prominent role in innate immunity and has been implicated in the pathogenesis of several diseases, including cancer and autoimmune disorders. Its ability to modulate the immune response by interacting with various signaling molecules makes it a promising candidate for therapeutic interventions. Furthermore, studies have shown that TRIM40 can influence the antiviral response by regulating the degradation of specific proteins involved in viral replication and immune evasion. This has led to increased interest in understanding its molecular mechanisms and functional properties. The development of recombinant TRIM40 proteins has facilitated in vitro studies, allowing researchers to analyze its interactions and implications in disease contexts more thoroughly. Considering the intricate roles of TRIM proteins in cellular regulation, the comprehensive study of TRIM40 could provide valuable insights into novel therapeutic strategies and contribute to the understanding of its function in health and disease.
