Analytical Data
-
基因名
Cathepsin K
- Application
-
别名
CTSKCathepsin K; EC 3.4.22.38
-
种属
Cynomolgus
-
表达系统
E. coli
-
标签
N- His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P61276
-
表达区间
115-329aa
-
分子量
27.5 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
EPHX1, or epoxide hydrolase 1, is an important enzyme involved in the metabolism of epoxides, which are reactive compounds formed during the biotransformation of various xenobiotics and endogenous substances. This enzyme plays a crucial role in detoxifying potentially harmful epoxide intermediates, thus protecting cells from oxidative damage and contributing to overall metabolic homeostasis. Recent studies have underscored the significance of EPHX1 in drug metabolism and its association with various diseases, including cancers and cardiovascular disorders. The recombinant expression of EPHX1 protein has emerged as a valuable tool for studying its biochemical properties and functional roles in cellular pathways. By generating large quantities of pure EPHX1, researchers can investigate its substrate specificity, enzymatic activity, and interactions with other proteins. Furthermore, understanding the structure-function relationships of EPHX1 may provide insights into its regulatory mechanisms and potential therapeutic targets. Given its implications in drug development and personalized medicine, ongoing research on EPHX1 recombinant protein is essential for elucidating its role in human health and disease.
