Analytical Data
-
基因名
CRKL
- Application
-
别名
V-Crk Sarcoma Virus CT10 Oncogene Homolog(avian)-Like
-
种属
Human
-
表达系统
E. coli
-
标签
N-His
-
纯度
Greater than 95% as determined by SDS-PAGE.
-
蛋白编号
P46109
-
表达区间
Met1~Glu303
-
分子量
42kDa
-
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
Vps29, a key component of the retromer complex, plays a critical role in intracellular trafficking and endosomal sorting, particularly in the retrieval of proteins from endosomes to the trans-Golgi network. The retromer complex is essential for maintaining cellular homeostasis by regulating the recycling of transmembrane proteins, thereby influencing various cellular processes including signaling pathways, nutrient transport, and membrane protein composition. Dysfunction of Vps29 has been implicated in several neurodegenerative diseases, such as Alzheimer’s, where impaired endosomal trafficking contributes to the accumulation of misfolded proteins. Research on Vps29 recombinant protein involves elucidating its structural properties and understanding its functional mechanisms within the retromer complex. These studies aim to uncover how Vps29 interacts with other retromer components and its role in protein sorting. Such insights can facilitate the development of targeted therapeutic strategies for diseases associated with retromer dysfunction and may provide a framework for drug discovery aimed at enhancing protein recycling mechanisms within the cell. By generating and characterizing Vps29 in a recombinant form, researchers can further investigate its biochemical properties, interactions, and potential as a therapeutic target to correct trafficking defects in various pathological conditions.
