The human recombinant Fibrinogen Silencer Binding Protein is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain consisting of 322 amino acids. It has a molecular mass of approximately 37.2 kDa. The recombinant protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification through proprietary chromatographic techniques .
FSBP functions as a transcriptional repressor by down-regulating the expression of the fibrinogen gamma chain. It achieves this by interacting with the amyloid precursor protein-binding family A member 1 (APBA1), also known as X11alpha. The X11alpha/FSBP complex sends signals to the nucleus to repress the promoter activity of glycogen synthase kinase-3 beta (GSK3B) . This interaction is significant because GSK3B is involved in various cellular processes, including the regulation of glycogen metabolism and neuronal cell development.
The repression of the fibrinogen gamma chain by FSBP is essential for maintaining proper fibrinogen levels in the body. Fibrinogen is a critical protein involved in blood clotting, and its dysregulation can lead to various disorders, including thrombosis and bleeding disorders. By regulating fibrinogen levels, FSBP plays a vital role in maintaining hemostasis and preventing abnormal blood clot formation .
The human recombinant Fibrinogen Silencer Binding Protein is used in various research applications, including studies on gene regulation, protein-protein interactions, and the development of therapeutic interventions for diseases related to fibrinogen dysregulation. Its availability in a recombinant form allows researchers to study its function and mechanism in a controlled environment, providing valuable insights into its role in cellular processes .
The recombinant FSBP protein is typically stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to store the protein at -20°C with the addition of a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), to prevent degradation. It is important to avoid multiple freeze-thaw cycles to maintain the protein’s stability and functionality .