Recombinant Mouse Myoglobin Protein (Tagged)

Name: Recombinant Mouse Myoglobin Protein (Tagged)
Brand: Beta LifeScience
SKU: BLA-9975P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Mouse
Accession	P04247
Synonym	MB MGC13548 MYG_HUMAN Myoglobin
Description	Recombinant Mouse Myoglobin Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	GLSDGEWQLVLNVWGKVEADLAGHGQEVLIGLFKTHPETLDKFDKFKNLK SEEDMKGSEDLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIP VKYLEFISEIIIEVLKKRHSGDFGADAQGAMSKALELFRNDIAAKYKELG FQG
Molecular Weight	22 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	KEGG: mmu:17189 STRING: 10090.ENSMUSP00000019037 UniGene: Mm.404074

Gene Functions References

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
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
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
Myoglobin overexpression inhibits reperfusion in the ischemic mouse hindlimb through impaired angiogenesis but not arteriogenesis PMID: 24095922
Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion. PMID: 23962643
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
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
Myoglobin is present in the murine vasculature and contributes significantly to nitrite-induced vasodilation PMID: 20889759
myoglobin constitutes the important barrier that efficiently protects the heart from nitrosative stress PMID: 12665503
Findings demonstrate that myoglobin serves as an important cytoplasmic buffer of iNOS-derived NO, which determines the functional consequences of iNOS overexpression. PMID: 12775582
myoglobin is an important cytoplasmic cardiac hemoprotein that functions in regulating NO homeostasis within cardiomyocytes. PMID: 12881221
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
analysis of amyloid-forming apomyoglobin mutant W7FW14F PMID: 14701846
Mb is a key element influencing redox pathways in cardiac muscle to functionally and metabolically protect the heart from oxidative damage. PMID: 15132981
importance of oxygen supply and nitric oxide scavenging by myoglobin is clearly demonstrated at the conscious animal level PMID: 15817640
lack of myoglobin causes a biochemical shift in cardiac substrate utilization from fatty acid to glucose oxidation. PMID: 15817884
In myoglobin-containing mouse heart endogenous chromophores interfere with Fura-2 fluorometry in myocardial ischemia. PMID: 17316820
testosterone and training have differential effects on the concentration of myoglobin in some, but not all muscles PMID: 18548256
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
Hypoxia reprograms calcium signaling and regulates myoglobin expression. PMID: 19005161

FAQs

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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.