Recombinant Proteins
Product List
Myo Human w/o H
Myoglobin (Heme free) Human Recombinant
Myoglobin
Myoglobin Human
Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.
Myoglobin His Human
Myoglobin His Human Recombinant
MB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Myoglobin Human
Myoglobin Human Recombinant
Introduction
Myoglobin (Mb) is an iron- and oxygen-binding protein found predominantly in the cardiac and skeletal muscle tissue of vertebrates . It belongs to the globin superfamily of proteins and is structurally similar to hemoglobin, the oxygen-carrying protein in red blood cells . Myoglobin consists of a single polypeptide chain with 153 amino acids and a heme group that binds oxygen .
Key Biological Properties: Myoglobin has a high affinity for oxygen, which allows it to store and transport oxygen within muscle cells . It is a monomeric protein, meaning it consists of a single polypeptide chain .
Expression Patterns and Tissue Distribution: Myoglobin is primarily expressed in cardiac and skeletal muscle tissues . It is found in high concentrations in Type I (slow-twitch) muscle fibers, which are involved in endurance activities, and to a lesser extent in Type II (fast-twitch) muscle fibers . Myoglobin is also present in smooth muscle cells, although in lower concentrations .
Primary Biological Functions: The main function of myoglobin is to store and facilitate the transport of oxygen within muscle cells . This is crucial during periods of intense muscle activity when the demand for oxygen is high .
Role in Immune Responses and Pathogen Recognition: While myoglobin’s primary role is related to oxygen transport, it also plays a role in modulating nitric oxide homeostasis within muscle cells, which can influence immune responses .
Mechanisms with Other Molecules and Cells: Myoglobin binds oxygen on its heme group, which allows it to acquire oxygen from hemoglobin in the blood and transfer it to muscle tissues . This binding is facilitated by the high affinity of myoglobin for oxygen compared to hemoglobin .
Binding Partners and Downstream Signaling Cascades: Myoglobin interacts with various molecules, including nitric oxide and reactive oxygen species, which can influence cellular signaling pathways and muscle function .
Regulatory Mechanisms Controlling Expression and Activity: Myoglobin expression is regulated by several transcription factors, including MEF2, NFAT, and Sp1, which are activated by locomotor activity, intracellular calcium fluxes, and low oxygen tension . Post-translational modifications, such as phosphorylation, also play a role in regulating myoglobin activity .
Biomedical Research: Myoglobin is used as a model protein in structural biology due to its well-characterized structure . It has been instrumental in understanding protein folding and function.
Diagnostic Tools: Elevated levels of myoglobin in the blood can be used as a biomarker for muscle injury, including myocardial infarction (heart attack) .
Therapeutic Strategies: Research is ongoing to explore the potential of myoglobin as a therapeutic target for treating various cardiac and skeletal muscle disorders .
Role Throughout the Life Cycle: Myoglobin plays a critical role in muscle function throughout the life cycle. During development, it supports the growth and differentiation of muscle cells . In adulthood, it helps maintain muscle oxygenation during physical activity . In aging and disease, changes in myoglobin expression and function can impact muscle health and contribute to conditions such as heart failure and muscle atrophy .
