Analytical Data
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Gene name
TRIM48
- Application
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Alternative Names
TRIM48; RNF101; Tripartite motif-containing Protein 48; RING finger Protein 101
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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
Q8IWZ4
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Expression Region
1-208 aa
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AA Sequence
MNSGISQVFQ RELTCPICMN YFIDPVTIDC GHSFCRPCFY LNWQDIPILT QCFECIKTIQ QRNLKTNIRL KKMASLARKA SLWLFLSSEE QMCGIHRETK KMFCEVDRSL LCLLCSSSQE HRYHRHCPAE WAAEEHWEKL LKKMQSLWEK ACENQRNLNV ETTRISHWKA FGDILYRSES VLLHMPQPLN LALRAGPITG LRDRLNQF
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Molecular Weight
26.4 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
TRIM48, 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, including immune response, cell proliferation, and apoptosis. Characterized by its RING-finger domain, which is crucial for its E3 ubiquitin ligase activity, TRIM48 is involved in regulating protein stability and signaling pathways through ubiquitination. Research indicates that TRIM48 may play a pivotal role in the regulation of innate immunity and the cellular response to stress, thus influencing the progression of several diseases, including cancer and neurodegenerative disorders. Additionally, its involvement in viral pathogenesis suggests that TRIM48 could be a target for therapeutic interventions. Recent studies have highlighted its dual role in promoting and inhibiting inflammation, depending on the cellular context, making it an attractive focus for further investigation. Understanding the precise mechanisms and pathways modulated by TRIM48 could open new avenues for drug development and therapeutic strategies aimed at diseases where TRIM48 is implicated. Investigating the recombinant expression of TRIM48 provides critical insights into its functional characteristics and interactions, which are essential for unraveling its contributions to both normal physiology and disease states.
