Analytical Data
-
基因名
TRIC
- Application
-
别名
MARVELD2; DFNB49; MARVD2; MRVLDC2; MARVEL Domain Containing Protein 2; Deafness,Autosomal Recessive 49
-
种属
Human
-
表达系统
E. coli
-
标签
N-His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q8N4S9
-
表达区间
Leu363~Ser558
-
分子量
27&25&23kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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
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.
