Analytical Data
-
基因名
LRRC15
-
简介
LRRC15 protein actively modulates SARS-CoV-2 infectivity by directly interacting with the spike protein, inhibiting ACE2(+) cell infection. While not an entry receptor, LRRC15, expressed on nearby cells, sequesters virions, and its direct interaction with the spike protein's RBD domain leads to virion sequestration at the cell surface. LRRC15 Protein, Human (HEK293, His-Avi) is the recombinant human-derived LRRC15 protein, expressed by HEK293 , with C-Avi, C-His labeled tag.
- Application
-
别名
LIB; LRRC15
-
种属
Human
-
表达系统
HEK293
-
标签
C-Avi;C-8*His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q8TF66-1
-
表达区间
Y22-G538
-
蛋白长度
Extracellular Domain
-
分子量
70-80 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
LRRC15, or Leucine-rich repeat-containing protein 15, is a member of the leucine-rich repeat protein family, which plays a significant role in various biological processes, including cell adhesion, immune response, and extracellular matrix interaction. Recent studies have highlighted LRRC15's potential involvement in fibrosis and cancer progression, particularly in the context of tumor microenvironments. Its expression has been found to be upregulated in several types of tumors, suggesting a role in promoting tumorigenesis. Investigating recombinant LRRC15 proteins can provide crucial insights into its structural and functional properties, aiding in the understanding of its mechanistic pathways. Moreover, as a potential biomarker, LRRC15 may offer new therapeutic targets for treating fibrotic diseases and cancers. The study of this protein is essential for elucidating its interactions with other cellular components and understanding its implications in disease states. Furthermore, the development of recombinant forms of LRRC15 can facilitate the exploration of its properties in vitro and in vivo, potentially leading to novel diagnostic or therapeutic strategies. Overall, the research surrounding LRRC15 is burgeoning, with its promise in biomedical applications garnering increasing attention from the scientific community.
