Overview
Mouse myoglobin is a heme-containing protein primarily found in skeletal and cardiac muscle tissues. It functions as an oxygen storage molecule, facilitating oxygen diffusion to mitochondria during periods of high metabolic demand. Structurally, it consists of a single polypeptide chain with a porphyrin ring that binds oxygen. Myoglobin is highly conserved across species, making mouse myoglobin a valuable model for studying human myoglobin-related conditions. In research, mouse myoglobin is widely used to investigate muscle function, oxygen transport mechanisms, and diseases such as myoglobinuria. Its small size and stability make it suitable for various biochemical assays and structural studies. Recombinant mouse myoglobin is commonly produced in E. coli for laboratory use.
Physical and Chemical Properties
Mouse myoglobin has a molecular weight of approximately 17 kDa and exhibits a characteristic reddish-brown color due to its heme group. The protein is stable under physiological pH and temperature conditions but can denature under extreme conditions. It has a high affinity for oxygen, which it binds reversibly. Myoglobin is soluble in aqueous solutions and buffers, making it easy to handle in laboratory settings. Its absorption spectrum features a Soret band at around 410 nm, which is useful for quantification and purity assessment. The protein’s stability and solubility are influenced by pH, ionic strength, and the presence of reducing agents.
Main Applications
Mouse myoglobin is primarily used in biomedical research to study muscle physiology and oxygen transport. It serves as a model protein for understanding myoglobin-related disorders, such as rhabdomyolysis and myoglobinuria. Researchers also use it to develop diagnostic assays for muscle damage and oxidative stress. In the pharmaceutical industry, mouse myoglobin is employed in drug development to evaluate compounds that modulate oxygen binding or release. Additionally, it is used in educational settings to teach protein biochemistry and enzymology. Its applications extend to biotechnology, where it is studied for potential use in oxygen-carrying therapeutics.
Safety and Storage
Mouse myoglobin is generally considered safe to handle under standard laboratory conditions. However, it should be treated as a potential allergen, and direct contact with skin or mucous membranes should be avoided. Proper personal protective equipment, such as gloves and lab coats, is recommended. For storage, lyophilized mouse myoglobin should be kept at -20°C in a dry environment. Reconstituted solutions should be aliquoted to avoid repeated freeze-thaw cycles, which can degrade the protein. Long-term storage in liquid form is not recommended unless stabilized with glycerol or other cryoprotectants.
B2B Procurement Guide
When procuring mouse myoglobin for B2B purposes, buyers should prioritize purity (typically ≥95%) and source (recombinant or native). Recombinant myoglobin is often preferred for consistency and scalability. Suppliers should provide detailed certificates of analysis, including data on endotoxin levels and biological activity. Price varies based on purity, quantity, and supplier reputation. Bulk purchases may offer cost savings, but buyers should ensure proper storage and handling to maintain product integrity. Reliable suppliers often offer technical support and customization options, such as labeling or conjugation services for specific research needs.
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