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Recombinant Human Arginase-1 Protein (His Tag)

Recombinant Human Arginase-1 Protein (His Tag)
  • Recombinant Human Arginase-1 Protein (His Tag)
  • Recombinant Human Arginase-1 Protein (His Tag)

Price: ¥3600.00 ¥1200.00

Size:
100 μg 20 μg
  • 表达系统: E.coli
  • 蛋白编码: P05089
别称
ARG1;Al;Arginase 1;Arginase liver
表达系统
E.coli
序列
Met1-Lys322
蛋白编码
P05089
种属
Human
计算分子量
36.9 kDa
表观分子量
38-40 kDa
标签
N-His
生物活性
Not validated for activity
纯度
> 90% as determined by reducing SDS-PAGE.
内毒素
< 10 EU/mg of the protein as determined by the LAL method
保存条件
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
运输条件
This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C.
制剂
Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
复溶方法
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
背景
Arginase 1, also known as liver arginase, is a binuclear manganese metalloenzyme. It is a key enzyme of the urea cycle that catalyses the conversion of L-arginine into L-ornithine and urea, the final cytosolic reaction of urea formation in the mammalian liver. Arginase 1 is abundantly expressed in liver, but it is also expressed in cells and tissues that lack a complete urea cycle, including lung. Arginase is a critical regulator of nitric oxide synthesis and vascular function. It is implicated in a variety of human diseases including vascular disease, pulmonary disease, infectious disease, immune cell function and cancer. In humans, hereditary defects in arginase result in an accumulation of arginine in the blood known as hyperarginemia. Arginase deficiency can also result in the accumulation of nitrogen in the form of ammonia, which results in hyperammonemia.
> 90 % as determined by reducing SDS-PAGE.


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