关键信息
-
基因名
Ephrin-A2/EFNA2
- 应用
-
别名
CEK7-ligand; CEK7-L; ELF-1; LERK-6
-
种属
Rat
-
表达系统
HEK293
-
标签
C-hFc
-
纯度
Greater than 95% as determined by reducing SDS-PAGE.
-
蛋白编号
F1MA19
-
表达区间
R21-S183
-
蛋白长度
Partial
-
分子量
55 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.
质检流程
相关产品
背景信息
Ephrin-A2 (EFNA2), a member of the ephrin family of proteins, plays a crucial role in cell-cell communication and signaling, specifically in developmental processes and tissue homeostasis. It is known to interact with Eph receptors, which are tyrosine kinase receptors that mediate various biological functions, including cell migration, adhesion, and angiogenesis. The study of EFNA2 is particularly important in the context of cancer, as its abnormal expression has been linked to tumor progression and metastasis. Researchers have focused on recombinant EFNA2 protein to better understand its structural and functional properties, as well as its role in various signaling pathways. By producing recombinant EFNA2 in laboratory settings, scientists can investigate its interactions with Eph receptors and other binding partners, providing insights into the molecular mechanisms underlying its biological functions. Furthermore, understanding the implications of EFNA2 in disease states could pave the way for novel therapeutic approaches in cancer and other conditions where cell signaling is disrupted. Overall, the exploration of Ephrin-A2/EFNA2 recombinant protein is a vital step toward elucidating its potential as a target for therapeutic intervention and for unraveling the complexities of Ephrin-Eph signaling dynamics in health and disease.
