Taiy Chemical
Fibronectin CS-1 Fragment (1978-1985)
Synonym Fibronectin CS-1 Fragment (1978-1985)
Species Human
Protein Accession P02751
Purity Greater than 95%
Endotoxin Level < 0.1 EU per 1 μg of protein
Biological Activity No information available
Expression System E. coli
Fusion Tag None
Predicted Molecular Mass Approximately 1.5 kDa
Formulation Lyophilized from a 0.2 μm filtered solution in PBS
Reconstitution Reconstitute in water to a concentration of 0.1-1.0 mg/ml
Storage & Stability Store at -80°C. Avoid repeated freeze-thaw cycles.
FAQ
What is the Fibronectin CS-1 Fragment (1978-1985) and how does it work?

Fibronectin is a high-molecular-weight glycoprotein that plays a crucial role in cell adhesion, growth, migration, and differentiation. It is found in the extracellular matrix (ECM) and in plasma, and it is vital for wound healing and embryonic development, among other biological processes. The CS-1 fragment of fibronectin refers specifically to a particular sequence within the molecule that is known to interact with certain cell surface receptors, such as integrins. Integrins are transmembrane receptors that facilitate cell-ECM adhesion, signaling, and the dynamic restructuring of the cellular cytoskeleton. The CS-1 region is particularly interesting because of its role in enhancing cell adhesion and migration, which are critical processes in both normal development and disease states, including cancer metastasis and inflammation.

The Fibronectin CS-1 Fragment (1978-1985) typically refers to a small peptide fragment derived from the larger fibronectin molecule. This fragment retains the bioactivity of the specific region it represents. It is often used in research settings to study how cells interact with the ECM and to elucidate the signaling pathways involved. By doing so, researchers can discover how cell behavior is influenced by changes in the ECM, which has implications for understanding tissue regeneration as well as pathological conditions where ECM remodeling is a feature.

Moreover, this fragment can be utilized to modulate cell behavior in a controlled manner, such as promoting cell adhesion in tissue engineering applications. Such a capacity can be highly valuable for engineering biomaterials that need to integrate seamlessly with the surrounding tissue, for instance, in wound healing dressings or surgical implants. The sequence of the CS-1 fragment binds specifically to the α4β1 integrin, a crucial receptor expressed on the surface of immune cells and some cancer cells, which makes it especially notable in research exploring therapeutic interventions. As a result, applications of the fibronectin CS-1 fragment extend into designing peptides for enhanced cell adhesion properties in synthetic scaffolds and biomedical devices, making it a versatile tool in both experimental settings and potential clinical applications.

In terms of cancer research, the CS-1 fragment's role in cell migration and invasion makes it a target for developing anti-metastatic therapies. Since cancer metastasis involves the detachment of cancer cells from the primary tumor, migration through the ECM, and subsequent colonization of distant tissues, understanding and potentially disrupting this process via the fibronectin pathway could pave the way for new treatment strategies. Thus, the Fibronectin CS-1 Fragment not only serves as a significant model for studying cell-ECM interactions but also represents a potential focus for therapeutic innovation.

How is the Fibronectin CS-1 Fragment used in laboratory research?

The Fibronectin CS-1 Fragment (1978-1985) is a powerful tool in laboratory research, enabling scientists to explore a variety of cellular processes and interactions between cells and their microenvironment. Its primary use lies in its ability to mimic the fibronectin domain that interacts with the α4β1 integrin receptor, which has been implicated in a range of biological activities, including cell adhesion, migration, and signaling. Researchers employ this fragment to dissect these fundamental aspects of cell biology in both normal and pathological contexts.

One of the most common applications of the fibronectin CS-1 fragment in laboratory research is in cell adhesion assays. These assays are essential for understanding how cells adhere to their surroundings, which is critical in maintaining tissue structure and function. By coating culture plates with the CS-1 fragment, researchers can quantitatively assess how different cell types adhere compared to other ECM proteins. This is particularly useful for screening the effects of genetic modifications, drugs, or other treatments that might alter cell adhesion properties.

Moreover, the CS-1 fragment is valuable in studying cell migration. Given its interaction with integrins, it plays a key role in facilitating cell movement across surfaces, which is a central principle in processes such as wound healing and cancer metastasis. By employing migration assays, researchers can observe and analyze the movement of cells on CS-1-coated substrates, which helps elucidate the signaling pathways involved in cell motility and determine how cells respond to various chemoattractants or inhibitors.

Another critical application of the CS-1 fragment is in the field of tissue engineering. When integrated into biomaterial scaffolds, the CS-1 fragment can enhance the adhesion of specific cells to the scaffolds, which is crucial for the development of engineered tissues and regenerative medicine applications. By attracting and holding cells at the site where regeneration is required, the CS-1 fragment facilitates the formation of new, functional tissue, enhancing the healing process.

The CS-1 fragment also serves as a model for understanding pathological processes such as inflammation and cancer. For example, its interactions with integrins expressed on immune cells can be studied to gain insights into how immune cells migrate to sites of inflammation or how cancer cells might exploit these pathways for metastasis. This makes it an attractive target for developing therapeutic interventions that can either block or enhance these interactions depending on the disease context.

In summary, the Fibronectin CS-1 Fragment is a versatile research tool that plays an integral role in numerous experimental setups aimed at deciphering the complex communication network between cells and their microenvironment. Its applications extend from basic biological research to practical implementations in therapeutic development and tissue engineering, underscoring its significance in modern biomedical research.

What are the implications of using the Fibronectin CS-1 Fragment in cancer research?

The utilization of the Fibronectin CS-1 Fragment in cancer research holds profound implications for understanding tumor biology and developing innovative therapeutic strategies. At the core of its significance is its ability to interact with the α4β1 integrin, a receptor often upregulated in various cancers, thus influencing key processes such as adhesion, migration, and angiogenesis, which are essential for tumor progression and metastasis.

A primary area of research involving the CS-1 fragment is its role in cancer cell migration and invasion. Cancer metastasis involves the detachment of cancer cells from the primary tumor, their invasion through the surrounding extracellular matrix (ECM), entry into the circulatory or lymphatic systems, and subsequent colonization at distant sites. The CS-1 fragment, by virtue of its interaction with integrins, can modulate these processes. Integrins, when engaged by ligands like the CS-1 fragment, activate signaling pathways that lead to the reorganization of the cytoskeleton and the establishment of new focal adhesions, processes that are critical for cell movement. By understanding these interactions, researchers can identify new targets for therapeutic intervention, potentially halting or slowing metastasis.

Furthermore, the CS-1 fragment's involvement in angiogenesis—the formation of new blood vessels—adds another layer of importance. Tumors require a blood supply to receive nutrients and oxygen, and integrins play a significant role in regulating angiogenesis. The interaction between integrins and the CS-1 fragment can either promote or inhibit angiogenesis, depending on the context. This duality offers potential therapeutic pathways: inhibiting angiogenesis can starve the tumor of nutrients, while promoting it can enhance the delivery of drugs within the tumor.

The CS-1 fragment is also pivotal in the tumor microenvironment's dynamics. Tumors are not merely composed of cancer cells; they also include a mix of stromal cells, immune cells, and ECM components, all of which interact in complex ways to support tumor growth and suppress immune responses. By modulating integrin pathways with the CS-1 fragment, researchers are able to explore how the tumor microenvironment can be altered to support anti-tumor immunity or disrupt tumor-stromal interactions, two strategies that could yield significant therapeutic dividends.

Additionally, studies using the CS-1 fragment help in understanding drug delivery mechanisms within tumors. Integrins can be utilized to target nanoparticles or other drug carriers to specific sites within the body, and the CS-1 fragment, by binding to α4β1 integrin, offers a mechanism to direct these therapeutic agents precisely to the tumor site, enhancing efficacy and reducing side effects.

In conclusion, the Fibronectin CS-1 Fragment serves as a key research tool in cancer biology, offering insights into cell-ECM interactions and potential therapeutic avenues. By dissecting its role in cell migration, angiogenesis, and the tumor microenvironment, researchers are poised to make significant advancements in cancer treatment strategies, underscoring the importance of the CS-1 fragment in both the experimental and clinical realms.

How does the Fibronectin CS-1 Fragment impact wound healing and tissue regeneration research?

The Fibronectin CS-1 Fragment plays a critical role in advancing research related to wound healing and tissue regeneration, offering insights into the complex mechanisms governing these processes and providing potential avenues for therapeutic intervention. Wound healing is a sophisticated biological response to tissue injury that involves a highly orchestrated series of events, including hemostasis, inflammation, proliferation, and remodeling. Fibronectin is a critical component of the extracellular matrix (ECM) implicated in various stages of tissue repair, and the CS-1 fragment, in particular, has specific interactions that make it influential in this context.

One of the core applications of the CS-1 fragment in wound healing research is its ability to facilitate cell adhesion and migration. These processes are crucial at the initial stages of wound healing, where cells such as fibroblasts migrate into the wound bed, proliferate, and lay down a new matrix that forms the structural basis for tissue regeneration. The CS-1 fragment binds to the α4β1 integrin, which is expressed in fibroblasts and immune cells. The binding enhances fibroblast migration and adhesion at the wound site, accelerating the formation of granulation tissue and subsequent tissue remodeling.

Moreover, the fibroblast interaction with the CS-1 fragment can influence collagen deposition and alignment, factors that are critical for restoring tissue integrity and functional properties. In wound healing research, modifying materials with the CS-1 fragment can improve these parameters, leading to faster and more efficient wound closure.

The CS-1 fragment also plays a pivotal role in modulating immune responses during wound healing. Integrins, along with their ligands like the CS-1 fragment, are key in the recruitment and function of immune cells to the wound site. These cells must respond swiftly to clear debris and pathogens and to signal the influx of cells that will participate in tissue repair. By influencing integrin-signaling pathways, the CS-1 fragment can moderate the activity and migration of these immune cells, creating an environment conducive to healing and minimizing chronic inflammation.

In the sphere of tissue regeneration, the CS-1 fragment's application extends to its incorporation into biomaterials and scaffolds designed for regenerative medicine. When scaffolds are functionalized with the CS-1 fragment, they exhibit enhanced cell-binding capacities, promoting the attachment and proliferation of progenitor cells essential for tissue engineering. This property is especially advantageous in developing synthetic grafts or implants intended to replace or repair damaged tissues, where effective integration with host tissue is paramount.

Additionally, the CS-1 fragment's interaction with vascular cells is significant in regenerative medicine, particularly concerning the neovascularization of engineered tissues. This neovascularization ensures a viable supply of nutrients and oxygen necessary for cell survival and tissue maintenance. By influencing endothelial cell behavior, the CS-1 fragment can enhance the vascularization of scaffolds, further supporting tissue growth and regeneration.

In summary, the Fibronectin CS-1 Fragment is an invaluable asset in wound healing and tissue regeneration research. It facilitates a better understanding of cell-matrix interactions and provides practical tools for developing therapeutic strategies aimed at improving healing outcomes. Whether through enhancing cell adhesion, migration, modulating immune responses, or engineering advanced biomaterials for tissue regeneration, the CS-1 fragment underpins significant advances in our ability to repair and regenerate tissues effectively.
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