SERPINB2 Human

The SERPINB2 gene is located on chromosome 18 in humans and encodes a protein that is primarily found as a 47 kDa non-glycosylated intracellular protein. Upon induction, it can be secreted as a 60 kDa glycoprotein . The glycosylated and non-glycosylated forms of SERPINB2 are similarly effective as inhibitors of urokinase-type plasminogen activator (uPA), which is the only proven physiological target of SERPINB2 .

SERPINB2 functions as an inhibitor of uPA, a serine protease involved in the degradation of the extracellular matrix and the activation of other proteases. By inhibiting uPA, SERPINB2 plays a crucial role in regulating processes such as tissue remodeling, cell migration, and inflammation . The inhibition mechanism involves the formation of a stable complex between SERPINB2 and uPA, which prevents uPA from interacting with its substrates .

SERPINB2 is involved in various physiological and pathological processes. It is expressed in a variety of tissues, including the placenta, monocytes, and macrophages. Its expression is upregulated in response to inflammatory stimuli, indicating its role in the immune response . Additionally, SERPINB2 has been implicated in several diseases, including gingivitis and pre-eclampsia .

Recombinant SERPINB2 is produced using various expression systems, such as E. coli, to facilitate its study and potential therapeutic applications. The recombinant protein retains the functional properties of the native protein, making it a valuable tool for research and drug development .

Due to its role in inhibiting uPA, SERPINB2 is of interest in cancer research, particularly in the context of tumor invasion and metastasis. By modulating the activity of uPA, SERPINB2 can potentially influence the invasive properties of cancer cells . Furthermore, its involvement in inflammatory responses makes it a target for studying inflammatory diseases and developing anti-inflammatory therapies .