Recombinant human vitronectin protein

(Qk120)

Product Background

Vitronectin is a glycoprotein found in the extracellular matrix (ECM) and blood plasma. It plays a crucial role in various physiological processes, including cell adhesion, migration, wound healing, and immune response regulation. Vitronectin interacts with various cell surface receptors and other ECM proteins, making it a key player in tissue remodeling and repair.

Vitronectin is involved in numerous biological processes, including cell adhesion and migration by binding to integrins, wound healing and tissue repair, regulation of proteolysis and fibrinolysis, immune response regulation, and angiogenesis by promoting the formation of new blood vessels and supporting tumorigenesis and metastasis.

In cell culture, vitronectin has been widely used due to its key roles in cell adhesion, proliferation, differentiation, and survival. It interacts with integrins and other cell surface receptors, creating a physiologically relevant microenvironment for various cell types, particularly in stem cell research and regenerative medicine. As a coating substrate, vitronectin promotes cell attachment, especially for epithelial cells, endothelial cells, and certain cancer cells. By binding to integrins, vitronectin enhances cell proliferation and survival through the activation of intracellular signaling pathways such as PI3K/AKT and MAPK. This attachment prevents anoikis, a form of cell death that occurs when cells detach from the ECM, ensuring the maintenance and expansion of cultured cells.

In stem cell applications, vitronectin is used for the culture and maintenance of iPSCs and ESCs, promoting their efficient differentiation into various lineages. It is also a key component of defined, xeno-free culture systems, eliminating the need for animal-derived products, reducing variability, and improving reproducibility in stem cell research.

In organoids technology, vitronectin plays a critical role in the development and maintenance of organoids due to its properties that enhance cell adhesion, proliferation, and differentiation. As a matrix scaffold, vitronectin supports the initial adhesion and aggregation of cells, essential for stable organoid structure formation. By binding to integrins such as αvβ3 and αvβ5 on cell surfaces, vitronectin facilitates cell clustering, a prerequisite for organoid growth. It activates integrin-mediated signaling pathways like PI3K/AKT and MAPK/ERK, promoting cell survival, proliferation, and differentiation, which are crucial for expanding progenitor cells and their differentiation within the organoid. Vitronectin has been implicated in the development of liver organoid.

In tissue engineering and regenerative medicine, vitronectin-coated scaffolds and biomaterials enhance cell attachment, proliferation, and differentiation, contributing to the development of functional tissue constructs. Additionally, vitronectin is used to prepare cells for cell therapy, ensuring their viability and functionality upon transplantation.

Vitronectin is particularly important for optimizing culture conditions in the manufacturing of serum-free media, compensating for the lack of adhesion-promoting factors typically provided by serum and supporting cell growth under defined conditions. The use of recombinant vitronectin ensures batch-to-batch consistency, which is critical for reproducibility in experimental and clinical applications.

Structurally, vitronectin is a multifunctional glycoprotein with a molecular weight of approximately 75 kDa. It comprises several domains, including the somatomedin B domain at the N-terminal, which is important for binding to the urokinase receptor and stabilizing the inactive form of plasminogen activator inhibitor-1 (PAI-1). The RCL (Ricinus communis agglutinin-like) domain is crucial for heparin binding, while the hemopexin-like repeats facilitate interactions with integrins and other ECM components. Vitronectin can undergo conformational changes that expose or hide specific binding sites, enabling it to interact with a wide range of ligands and receptors.

In summary, vitronectin plays a crucial role in various applications, particularly in stem cell and organoid applications, by providing a defined and supportive environment for stem cell maintenance, differentiation, and reprogramming. Its use enhances the reproducibility and efficiency of several cell cultures, making it a valuable tool in both research and therapeutic contexts.

Vitronectin protein is widely used in stem cell culture. It provides a defined environment that supports the maintenance of pluripotency and is suitable for feeder-free culture, expansion, differentiation, and reprogramming of stem cells.

Qkine vitronectin is a high-purity animal origin-free recombinant protein with a molecular weight of 47.8 kDa. It is carrier-free and protein tag-free, ensuring exceptional lot-to-lot consistency and compatibility with translational studies and iPSC-based model production for screening. Qkine recombinant vitronectin protein is ultra high-purity with exceptionally low residual endotoxins making it suitable for the reproducible culture of stem cells, primary cells, organoids, and use in sensitive neural differentiations.