Recombinant Human SERPINI2 protein is a Human Full Length protein, in the 21 to 405 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
MEPI, PI14, SERPINI2, Serpin I2, Myoepithelium-derived serine protease inhibitor, Pancpin, Pancreas-specific protein TSA2004, Peptidase inhibitor 14, PI-14
Recombinant Human SERPINI2 protein is a Human Full Length protein, in the 21 to 405 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 0.32% Tris HCl
ab182804 is expressed in E.coli as inclusion bodies. The final product was refolded and chromatographically purified.
Belongs to the serpin family.
SERPINI2 also known as Neuroserpin is a serine protease inhibitor with a molecular weight of approximately 44 kDa. This protein plays an important role in inhibiting proteolytic enzymes in the nervous system and other tissues. It is primarily expressed in the pancreas but it is also found in the central nervous system particularly in organs like the brain and spinal cord. The protein showcases moderate expression in tissues including lungs and kidneys reflecting its widespread regulatory functions across diverse physiological environments.
SERPINI2 interacts closely with serine proteases like tissue plasminogen activator to maintain cellular homeostasis by preventing excessive proteolysis. This regulatory action is important in processes such as fibrotic response maintaining extracellular matrix integrity and facilitating normal cellular turnover. SERPINI2 operates by forming complexes with its target proteins inhibiting their proteolytic activity and therefore modulating various cellular activities especially where proteolysis needs to be checked to prevent tissue damage.
SERPINI2 finds itself involved in regulatory pathways including the fibrinolytic system and the inflammatory response system. Its modulation of plasminogen activator activity links SERPINI2 to the plasminogen activation pathway essential for processes like tissue remodeling and repair. Additionally it shares functional interactions with proteins like plasminogen activator inhibitor 1 (PAI-1) working in tandem to optimize fibrinolytic balance and influence the turnover of the extracellular matrix.
SERPINI2 has been implicated in conditions such as pancreatic cancer and respiratory diseases like chronic obstructive pulmonary disease (COPD). In pancreatic cancer altered regulation of SERPINI2 has been associated with tumor progression due to changes in proteolytic control within the tumor microenvironment. Furthermore in respiratory disorders it connects to proteins like alpha-1-antitrypsin where dysregulated protease inhibition can exacerbate tissue destruction and inflammation common features of COPD.
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