Analytical Data
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Gene name
TRIC
- Application
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Alternative Names
MARVELD2; DFNB49; MARVD2; MRVLDC2; MARVEL Domain Containing Protein 2; Deafness,Autosomal Recessive 49
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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
Q8N4S9
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Expression Region
Leu363~Ser558
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Molecular Weight
27&25&23kDa
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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
TRIC (Tripartite Motif Containing Protein) is a family of proteins known for their role in various cellular processes, particularly in the regulation of signal transduction, ubiquitination, and gene expression. Research into TRIC proteins has gained traction due to their involvement in critical biological functions, including immune response, cell differentiation, and developmental processes. Recent studies have demonstrated that TRIC proteins can modulate protein interactions and stability, influencing the activity of essential signaling pathways. Furthermore, abnormalities in TRIC protein expression have been linked to diverse diseases, such as cancer and autoimmune disorders, highlighting their potential as therapeutic targets. The structural complexity of TRIC proteins, characterized by the presence of distinct motifs that facilitate their multifunctionality, presents both challenges and opportunities for researchers. Understanding the precise mechanisms through which TRIC proteins operate could lead to significant advancements in biomedical science, paving the way for novel intervention strategies in disease management. Overall, the ongoing investigation into TRIC proteins promises to enhance our comprehension of cellular dynamics and their implications for human health.
