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Recombinant Mouse Myoglobin protein (His tag) is a Mouse Full Length protein, in the 2 to 154 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE.

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Images

SDS-PAGE - Recombinant Mouse Myoglobin protein (His tag) (AB241238), expandable thumbnail

Key facts

Purity
>90% SDS-PAGE
Expression system
Yeast
Tags
His tag N-Terminus
Applications
SDS-PAGE
Biologically active
No

Amino acid sequence

G L S D G E W Q L V L N V W G K V E A D L A G H G Q E V L I G L F K T H P E T L D K F D K F K N L K S E E D M K G S E D L K K H G C T V L T A L G T I L K K K G Q H A A E I Q P L A Q S H A T K H K I P V K Y L E F I S E I I I E V L K K R H S G D F G A D A Q G A M S K A L E L F R N D I A A K Y K E L G F Q G

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Associated Products

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Target data

Function

Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:10468637, PubMed:11304494). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (By similarity). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:15132981).

Alternative names

Recommended products

Recombinant Mouse Myoglobin protein (His tag) is a Mouse Full Length protein, in the 2 to 154 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE.

Key facts

Purity
>90% SDS-PAGE
Expression system
Yeast
Applications
SDS-PAGE
Accession
P04247-1
Animal free
No
Species
Mouse
Concentration
Loading...
Storage buffer

pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

Sequence info

Amino acid sequence

G L S D G E W Q L V L N V W G K V E A D L A G H G Q E V L I G L F K T H P E T L D K F D K F K N L K S E E D M K G S E D L K K H G C T V L T A L G T I L K K K G Q H A A E I Q P L A Q S H A T K H K I P V K Y L E F I S E I I I E V L K K R H S G D F G A D A Q G A M S K A L E L F R N D I A A K Y K E L G F Q G
Accession
P04247
Protein length
Full Length
Predicted molecular weight
18.9 kDa
Amino acids
2 to 154
Nature
Recombinant
Tags
His tag N-Terminus

Specifications

Form
Liquid

General info

Function

Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:10468637, PubMed:11304494). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (By similarity). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:15132981).

Sequence similarities

Belongs to the globin family.

Storage

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

Myoglobin also known as MB is a small globular protein with a molecular weight of approximately 17 kDa. It functions as an oxygen-binding protein and is expressed mainly in cardiac and skeletal muscle tissue where it facilitates oxygen storage and transport. The myoglobin protein plays an important role in maintaining the oxygen supply needed during muscular contraction and intense physical activity.

Biological function summary

Myoglobin in muscle cells acts to store oxygen which provides a rapid release when required during muscle contraction. Myoglobin serves as a monomer and does not form part of a complex. Its structure allows it to temporarily store and relay oxygen where it is most required enhancing the often abrupt demands of muscles for oxygen. The ability of myoglobin to bind oxygen and release it under hypoxic conditions is central to its biological role in vertebrates.

Pathways

The function of myoglobin in aerobic respiration in muscles involves its participation in the oxygen transport pathway. This protein closely interacts with hemoglobin to mobilize oxygen effectively to mitochondria during muscle contraction. Unlike hemoglobin myoglobin has a hyperbolic oxygen dissociation curve which allows it to provide oxygen at lower partial pressures contributing significantly to the efficient metabolism during hypoxia or intense muscular exertion.

Associated diseases and disorders

Myoglobin plays a significant role in conditions such as rhabdomyolysis and myocardial infarction. Rhabdomyolysis a syndrome caused by muscle injury results in the release of myoglobin into the bloodstream. Myoglobin detection kits including myoglobin ELISA are essential tools for the diagnosis of these conditions. Moreover its rapid increase in plasma levels after heart muscle damage enables its use as an early marker for myocardial infarction. Myoglobin's interaction with proteins like creatine kinase provides valuable information on muscle damage and cardiac events.

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1 product image

  • SDS-PAGE - Recombinant Mouse Myoglobin protein (His tag) (ab241238), expandable thumbnail

    SDS-PAGE - Recombinant Mouse Myoglobin protein (His tag) (ab241238)

    (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab241238.

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Product protocols

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