Measured by its ability to cleave a colorimetric peptide substrate, Z-Lys-SBzl. The specific activity is >30,000 pmol/min/μg, as measured under the described conditions.
Measured by its ability to cleave a colorimetric peptide substrate, Z-Lys-SBzl. The specific activity is >30,000 pmol/min/μg, as measured under the described conditions.
Lyophilized from 10mM PBS, 5% Trehalose, 5% Mannitol, pH7.4.
复溶
Reconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
在 -20~-80℃ 下可保存 1 年以上。复溶后建议分装。避免冷冻/解冻循环。
图片
Recombinant Human Enteropeptidase/Enterokinase Protein (rp145565) - SDS-PAGE
2 μg/lane of Recombinant Human Enteropeptidase/Enterokinase Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the band at 46 - 49 (light chain) & 130 - 150 (heavy chain) kDa under reducing conditions and 120 - 150 kDa under non-reducing conditions.
Human enterokinase is synthesized as a single-chain precursor. It must undergo an autocatalytic or intermolecular cleavage to remove a linker peptide, thereby converting into the mature and active heterodimer. This functional form consists of a heavy chain and a light chain connected by a disulfide bond. The simultaneous presence of both the uncleaved precursor and the mature heterodimer in the sample indicates that the recombinant protein preparation is a partially processed mixture.