Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

Uniprot No.

P04247

Research Area

Cancer

Alternative Names

Mb; Myoglobin

Species

Mus musculus (Mouse)

Source

Mammalian cell

Expression Region

2-154aa

Target Protein Sequence

GLSDGEWQLVLNVWGKVEADLAGHGQEVLIGLFKTHPETLDKFDKFKNLKSEEDMKGSEDLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEIIIEVLKKRHSGDFGADAQGAMSKALELFRNDIAAKYKELGFQG
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

21.9 kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The region for expressing recombinant Mouse Mb (Myoglobin) contains amino acids 2-154. This Mb (Myoglobin) protein is theoretically predicted to have a molecular weight of 21.9 kDa. This Mb (Myoglobin) recombinant protein is manufactured in mammalian cell. The N-terminal 10xHis tag and C-terminal Myc tag was fused into the coding gene segment of Mb (Myoglobin), making it easier to detect and purify the Mb (Myoglobin) recombinant protein in the later stages of expression and purification.

Mouse myoglobin (Mb) is a globular protein encoded by the Mb gene. Like its human counterpart, mouse myoglobin is primarily expressed in muscle tissues, where it plays a crucial role in oxygen storage and transport. Myoglobin is a heme-containing protein, with a single heme group per molecule that binds oxygen, allowing for its storage and release within muscle cells. This facilitates efficient oxygen supply to working muscles during periods of increased activity. Myoglobin is an essential component of the oxygen homeostasis machinery in muscle tissues. Research on mouse myoglobin helps to understand its role in oxygen metabolism, muscle function, and its implications in various physiological processes.

Target Background

Function

Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Gene References into Functions

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

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Protein Families

Globin family

Database Links

KEGG: mmu:17189

STRING: 10090.ENSMUSP00000019037

UniGene: Mm.404074

Code	CSB-MP013529MO
Abbreviation	Recombinant Mouse Myoglobin protein
MSDS	MSDS Datasheet
Size	$660
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Mouse Myoglobin (Mb)

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Target Background

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