MFAP3 Human

MFAP3 was first cloned and characterized by Abrams et al. in 1995 . The protein is found in microfibrils, which are either associated with elastin or exist independently. These microfibrils are essential for the extracellular matrix’s structural framework, contributing to tissue elasticity and resilience .

MFAP3 has two known isoforms:

1. A longer isoform consisting of 362 amino acids with a molecular weight of approximately 40 kDa.
2. A shorter isoform with 216 amino acids, weighing around 24 kDa .

MFAP3 plays a pivotal role in the formation and maintenance of elastic fibers, which are vital for the elasticity of tissues such as skin, lungs, and blood vessels. The protein’s interaction with other microfibrillar components, including fibrillins and lysyl oxidase, underscores its importance in maintaining the extracellular matrix’s integrity .

Recombinant human MFAP3 is produced using human embryonic kidney cells (HEK293). This recombinant form is often used in research to study the protein’s function and its role in various biological processes. The recombinant protein is typically purified to high standards, ensuring its suitability for various experimental applications .

Recombinant MFAP3 is used in various research areas, including:

• Neuroscience: It has been shown to inhibit neurite outgrowth in rat embryonic cortical neurons, making it a valuable tool for studying neural development and regeneration .
• Cell and Tissue Culture: The protein’s role in the extracellular matrix makes it a crucial component in studies related to tissue engineering and regenerative medicine .

Recombinant MFAP3 is typically lyophilized and can be reconstituted in PBS. It is stable for up to 12 months when stored at -20 to -70°C. After reconstitution, it remains stable for up to one month at 2 to 8°C under sterile conditions .