Recombinant Human FGB/Fibrinogen beta Protein, N-His

Reference: YHB99202
Product nameRecombinant Human FGB/Fibrinogen beta Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight46.49 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeThr108-Gln491
Aliases /SynonymsFGB, Fibrinogen beta chain
ReferenceYHB99202
NoteFor research use only.

Description of Recombinant Human FGB/Fibrinogen beta Protein, N-His

Introduction to Recombinant Human FGB/Fibrinogen beta Protein

Recombinant Human FGB/Fibrinogen beta Protein, also known as Fibrinogen beta chain, is a protein that is encoded by the FGB gene in humans. It is a member of the fibrinogen family of glycoproteins and is an essential component of the blood clotting process. This protein is produced through recombinant DNA technology, making it a valuable tool in various scientific and medical applications.

Structure of Recombinant Human FGB/Fibrinogen beta Protein

Recombinant Human FGB/Fibrinogen beta Protein is a large, complex protein with a molecular weight of approximately 56 kDa. It is composed of two identical beta chains, each containing 461 amino acids, and two different alpha chains (alpha and gamma) that are linked together by disulfide bonds. The beta chains are responsible for the formation of the fibrin clot, while the alpha and gamma chains play a role in the assembly of the fibrinogen molecule.

The primary structure of Recombinant Human FGB/Fibrinogen beta Protein is highly conserved among different species, indicating its importance in biological functions. It also contains multiple domains, including the fibrinogen C-terminal domain, the coiled-coil domain, and the fibrinogen-like domain, which are crucial for its function.

Activity of Recombinant Human FGB/Fibrinogen beta Protein

Recombinant Human FGB/Fibrinogen beta Protein is a key player in the blood clotting process, also known as hemostasis. When an injury occurs, platelets in the blood are activated and release various factors that lead to the formation of a blood clot. One of these factors is fibrinogen, which is converted into fibrin by the enzyme thrombin. Fibrin then forms a mesh-like structure, providing a scaffold for platelets and other blood cells to form a stable clot.

Additionally, Recombinant Human FGB/Fibrinogen beta Protein has been found to have other biological activities, such as promoting cell adhesion and migration, and modulating inflammatory responses. These activities make it a potential therapeutic target for various diseases, including cancer and cardiovascular disorders.

Application of Recombinant Human FGB/Fibrinogen beta Protein

Recombinant Human FGB/Fibrinogen beta Protein has a wide range of applications in both research and clinical settings. Its ability to form fibrin clots makes it a valuable tool in studying blood clotting mechanisms and developing treatments for bleeding disorders.

In addition, Recombinant Human FGB/Fibrinogen beta Protein is used in diagnostic assays to detect the presence of fibrinogen in blood samples. It is also used in the production of fibrin glue, a medical adhesive used in surgical procedures to promote wound healing.

Moreover, the diverse biological activities of Recombinant Human FGB/Fibrinogen beta Protein have led to its potential use in therapeutic applications. It has been studied as a potential treatment for chronic wounds, tissue repair, and as an anti-inflammatory agent.

Conclusion

In summary, Recombinant Human FGB/Fibrinogen beta Protein is a crucial protein involved in blood clotting and has various biological activities. Its structure, activity, and applications make it a valuable tool in both research and clinical settings. With further studies and advancements in technology, this protein has the potential to contribute to the development of new treatments for various diseases.

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