85-1451-69　［取扱停止］Myoglobin, Recombinant, Human, Heme-free 1mg　M9800-35H

特徴

• Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O(2) by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation. Functionally, myoglobin is well accepted as an O(2)-storage protein in muscle, capable of releasing O(2) during periods of hypoxia or anoxia. Myoglobin is also thought to buffer intracellular O(2) concentration when muscle activity increases and to facilitate intracellular O(2) diffusion by providing a parallel path that augments simple diffusion of dissolved O(2). The use of gene targeting and other molecular biological techniques has revealed important new insights into the developmental and environmental regulation of myoglobin and provided additional functions for this hemoprotein such as scavenging nitric oxide and reactive O(2) species.
• Recombinant Human Myoglobin heme free produced in E. coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67kD. Recombinant Human Myo heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques.
• Dimers and Aggregates:≤1% as determined by silver-stained SDS-PAGE gel analysis.
• Endotoxin:≤ 0.1ng/ug (IEU/ug) of Recombinant Myoglobin.
• Stability and Stability:Recombinant Myo heme free although stable at 15°C for 2 weeks, should be stored at 4°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.