MB
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Official Full Name
myoglobin
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Overview
This gene encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. The encoded protein is a haemoprotein contributing to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. At least three alternatively spliced transcript variants encoding the same protein have been reported. [provided by RefSeq, Jul 2008] -
Synonyms
MB; myoglobin; PVALB; myoglobgin;
- Recombinant Proteins
- Cell & Tissue Lysates
- Native Proteins
- Transfected Stable Cell Lines
- Protein Pre-coupled Magnetic Beads
- Others
- Bovine
- Cattle
- Chicken
- Dog
- Equine
- Horse
- Human
- Mouse
- Pig
- Rat
- Sheep
- Sperm Whale
- Zebrafish
- Bovine Heart
- Canine/Dog Heart
- E. coli
- E.coli
- Equine/Horse Heart
- HEK293
- HEK293 cells
- HEK293T
- Horse
- Human Cardiac
- Human Heart
- Mammalian Cell
- Mammalian cells
- Mouse Heart
- Muscle
- Rat Heart
- Skeletal muscle
- Yeast
- C
- His
- His (Fc)
- Avi
- Myc
- His|T7
- DDK
- N/A
- N
- GST
- T7
- Involved Pathway
- Protein Function
- Interacting Protein
MB involved in several pathways and played different roles in them. We selected most pathways MB participated on our site, such as Effects of nitric oxide, which may be useful for your reference. Also, other proteins which involved in the same pathway with MB were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Effects of nitric oxide |
MB has several biochemical functions, for example, heme binding, metal ion binding, oxygen binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MB itself. We selected most functions MB had, and list some proteins which have the same functions with MB. You can find most of the proteins on our site.
Function | Related Protein |
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heme binding | MPX;CYB5B;CYP11B2;BACH1;PGRMC2;FECH;CYP2C18;CYP2C9;CYP2K16 |
metal ion binding | GNA15;CSNK2B;ZIC5;ESCO1;ZFP750;EBF4;ZFP511;ZNF134;ATMIN |
oxygen binding | CYP2D6;HBAA;HBB;CYP2D26;CYP2C54;CYP2AA1;HBG1;CYP2C18;CYP2AA9 |
oxygen transporter activity | HBG1;CYGB2;HBA1;BA1;NGB;HBB-B2;CYGB;HBAD;HBBE3 |
MB has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MB here. Most of them are supplied by our site. Hope this information will be useful for your research of MB.
- Q&As
- Reviews
Q&As (7)
Ask a questionMyoglobin's structure, with a single heme group, allows it to bind oxygen tightly, facilitating its role in oxygen storage and release in muscle tissues.
Myoglobin is released into the bloodstream when muscle cells are damaged. In the context of a myocardial infarction (heart attack), damaged heart muscle cells release myoglobin, making it a quick, albeit non-specific, marker for muscle injury.
Myoglobin's affinity for oxygen remains relatively constant across various environmental conditions, ensuring a steady oxygen supply for muscles even under stress.
While mutations in the MB gene are rare, they can lead to myoglobinuria, a condition where myoglobin is present in the urine, often after intense muscle activity.
Elevated myoglobin levels in blood tests can indicate muscle injury, including myocardial infarction. However, since myoglobin is also found in skeletal muscles, it is often used in conjunction with other markers to diagnose heart attacks.
While both myoglobin and hemoglobin bind oxygen, myoglobin has a higher affinity for oxygen and does not exhibit cooperative binding. This allows myoglobin to release oxygen under conditions where hemoglobin cannot, such as during intense muscle activity.
The MB gene encodes the protein myoglobin, which is responsible for storing and releasing oxygen in muscle cells, especially in conditions of high oxygen demand.
Customer Reviews (3)
Write a reviewEffective in pull-down assay.
Perfect for my experiments.
High-quality product, very satisfied.
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