Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218).
生物活性
Immobilized Recombinant Human Myoglobin Protein (rp214420) at 1.0 μg/mL can bind Recombinant Myoglobin Antibody (Ab007432) with the EC50 of 4.7 ng/mL.
17.4 kDa, under reducing conditions; 16.8 & 17.5 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
液体
储存缓冲液
Lyophilized from 20mM Tris, 300mM NaCl, pH 8.0
浓度
见COA
复溶
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
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
-20℃ 存储6个月;收货后建议分装,避免反复冻融。
图片
Recombinant Human Myoglobin Protein (rp214420) - ELISA Immobilized Recombinant Human Myoglobin Protein (rp214420) at 1.0 μg/mL can bind Recombinant Myoglobin Antibody (Ab007432) with the EC50 of 4.7 ng/mL.
Recombinant Human Myoglobin Protein (rp214420) - SDS-PAGE 3 μg/lane of Recombinant Human Myoglobin Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 17.4 kDa under reducing conditions and 16.8 & 17.5 kDa under non-reducing conditions. Myoglobin is a protein consisting of a single alpha-helical structure containing a Heme group. It reversibly binds oxygen through pentacorated heme iron and releases oxygen in a timely and efficient manner as needed during periods of increased demand. The main reason for the existence of two conformations in the non-reducing state is related to the different spin states and coordination modes of iron (Fe) in the heme cogroup. (PubMed:30918256, PubMed:34679218)