Analytical Data
-
基因名
TL1A/TNFSF15 Trimer
- Application
-
别名
TL1A; VEGI-251; TNFSF15; TL1; VEGI; VEGI192A
-
种属
Mouse
-
表达系统
HEK293
-
标签
N-His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q5UBV8
-
表达区间
A61-L252
-
分子量
27-29 kDa and 30-33 kDa
-
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
TL1A, also known as TNFSF15, is a member of the tumor necrosis factor (TNF) superfamily that plays a critical role in immune regulation and inflammatory responses. This protein is primarily expressed in the vascular endothelium and local immune cells, and it is known to interact with its receptor, DLK1, to influence T cell activation and proliferation. Research has increasingly focused on TL1A due to its involvement in various autoimmune and inflammatory diseases, such as Crohn’s disease and ulcerative colitis, where it is linked to the pathogenesis and progression of these conditions. The study of TL1A/TNFSF15 trimeric recombinant proteins has gained significance, as understanding their structure and function can provide insights into the mechanisms of immune regulation. Moreover, the potential therapeutic applications of targeting TL1A in disease settings represent a promising avenue for intervention. By producing and characterizing TL1A trimers, researchers aim to dissect its molecular interactions and elucidate its role in modulating the immune response, thereby paving the way for novel treatment strategies that could alleviate the burden of inflammatory diseases. Additionally, the development of TL1A-based biomolecules could facilitate the design of biomarkers or therapeutic agents aimed at tuning immune responses in various pathological contexts.












