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AB316414

Recombinant Human Myoglobin Protein Standard (His tag)

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Recombinant Human Myoglobin Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >80%, suitable for sELISA, SDS-PAGE.

View Alternative Names

Myoglobin, Nitrite reductase MB, Pseudoperoxidase MB, MB

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Sandwich ELISA - Recombinant Human Myoglobin Protein Standard (His tag) (AB316414)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Human Myoglobin Protein Standard (His tag) (AB316414)

Sandwich ELISA with the capture antibody dilution at 2 ug/mL and detector antibody dilution at 0.5 ug/mL.

SDS-PAGE - Recombinant Human Myoglobin Protein Standard (His tag) (AB316414)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Myoglobin Protein Standard (His tag) (AB316414)

SDS-PAGE analysis of ab316414

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

sELISA, SDS-PAGE

applications

Biologically active

No

Accession

P02144

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.3 - 7.5 Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.

Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.

The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

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Sequence info

[{"sequence":null,"proteinLength":"Fragment","predictedMolecularWeight":"18.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P02144","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

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.

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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Specifications

Form

Liquid

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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 : 30918256, PubMed : 34679218). 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 (PubMed : 32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed : 34679218).

Sequence similarities

Belongs to the globin family.

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Product protocols

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Target data

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 : 30918256, PubMed : 34679218). 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 (PubMed : 32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed : 34679218).
See full target information MB
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