Recombinant Mouse Myoglobin Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9974P

Recombinant Mouse Myoglobin Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9974P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Host Species Mouse
Accession P04247
Synonym MB MGC13548 MYG_HUMAN Myoglobin
Description Recombinant Mouse Myoglobin Protein (His tag) was expressed in Yeast. It is a Full length protein
Source Yeast
Molecular Weight 19 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Protein Families Globin family
Database References

Gene Functions References

  1. The authors here unravel a novel role of cardiac myoglobin in governing fatty acid metabolism to ensure the physiological energy production through beta-oxidation, preventing myocardial lipid accumulation and preserving cardiac functions. PMID: 28230173
  2. Inhibition of mammalian target of rapamycin (mTOR) activation using rapamycin restored Mb mRNA expression to control levels. Lipid supplementation had no effect on Mb gene expression. Thus, IGF-1-induced anabolic signaling can be a strategy to improve muscle size under mild hypoxia, but lowers Mb gene expression PMID: 28862673
  3. the novel cancer-associated MB splice variants exhibited increased expression in tumor cells subjected to experimental hypoxia; the novel gene regulatory mechanisms unveiled in this study support the idea of a non-canonical role of MB during carcinogenesis PMID: 24026678
  4. Myoglobin overexpression inhibits reperfusion in the ischemic mouse hindlimb through impaired angiogenesis but not arteriogenesis PMID: 24095922
  5. Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion. PMID: 23962643
  6. Show a high capacity of myoglobin-deficient mice to adapt to catecholamine induced cardiac stress which is associated with activation of a distinct cardiac gene expression program. PMID: 20145201
  7. Endogenous nitrite reduction to NO. via the heme globin myoglobin enhances blood flow and matches O(2) supply to increased metabolic demands under hypoxic conditions. PMID: 22685116
  8. Myoglobin is present in the murine vasculature and contributes significantly to nitrite-induced vasodilation PMID: 20889759
  9. myoglobin constitutes the important barrier that efficiently protects the heart from nitrosative stress PMID: 12665503
  10. Findings demonstrate that myoglobin serves as an important cytoplasmic buffer of iNOS-derived NO, which determines the functional consequences of iNOS overexpression. PMID: 12775582
  11. myoglobin is an important cytoplasmic cardiac hemoprotein that functions in regulating NO homeostasis within cardiomyocytes. PMID: 12881221
  12. The role of myoglobin as intracellular nitric oxide(NO) scavenger is small, and increase in mitochondrial superoxide in SOD heterozygous mice may cause decrease NO bioavailability and alter control of myocardial O2 consumption by NO. PMID: 12919935
  13. analysis of amyloid-forming apomyoglobin mutant W7FW14F PMID: 14701846
  14. Mb is a key element influencing redox pathways in cardiac muscle to functionally and metabolically protect the heart from oxidative damage. PMID: 15132981
  15. importance of oxygen supply and nitric oxide scavenging by myoglobin is clearly demonstrated at the conscious animal level PMID: 15817640
  16. lack of myoglobin causes a biochemical shift in cardiac substrate utilization from fatty acid to glucose oxidation. PMID: 15817884
  17. In myoglobin-containing mouse heart endogenous chromophores interfere with Fura-2 fluorometry in myocardial ischemia. PMID: 17316820
  18. testosterone and training have differential effects on the concentration of myoglobin in some, but not all muscles PMID: 18548256
  19. myoglobin and the heme globin family subserve a critical function as an intrinsic nitrite reductase that regulates responses to cellular hypoxia and reoxygenation. PMID: 18632562
  20. Hypoxia reprograms calcium signaling and regulates myoglobin expression. PMID: 19005161


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed