Myoglobin, Heme-free, Recombinant, Human

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.\n\nRecombinant 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.\n\nDimers and Aggregates: \n(same/less than) 1% as determined by silver-stained SDS-PAGE gel analysis.\n\nEndotoxin: \n(same/less than) 0.1ng/ug (IEU/ug) of Recombinant Myoglobin.\n\nStability and Stability: \nRecombinant Myo heme free although stable at 15 degrees C for 2 weeks, should be stored at 4 degrees C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

M9800-35H

Size

100ug

Form

Supplied as a liquid in PBS, pH 8.0 and 50mM phosphate-borate.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography.\n\nProc Natl Acad Sci U S A 2006 Mar 28;103(13):4924-9\n\n2. Comparison of creatine kinase activity and myoglobin blood level in acute myocardial infarction patients.\n\nBosn J Basic Med Sci 2006 Feb;6(1):19-23\n\n3. Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins.\n\nBiochemistry 2006 Mar 14;45(10):3170-7\n\n4. Stereoselective and driving-force-dependent photoinduced electron-transfer reactions of zinc myoglobin with optically active N,N'-dimethylcinchoninium and N,N'-dimethylcinchonidinium ions.\n\nJ Biol Inorg Chem 2006 Apr;11(3):316-24\n\n5. Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensors.\n\nJ Biol Chem 2006 Apr 14;281(15):10389-98\n\n6. Spectroscopic and photothermal study of myoglobin conformational changes in the presence of sodium dodecyl sulfate.\n\nBiomacromolecules 2006 Feb;7(2):476-82