Serine (or cysteine) peptidase inhibitor, clade B, member 2 (SERPINB2), also known as plasminogen activator inhibitor type-2 (PAI-2), has primarily been known as a coagulation factor that inactivates a urokinase and tissue-type plasminogen activator in response to inflammatory stimuli. SERPINB2 may also play a role in cellular migration and senescence, tumorigenesis, and immunity. These SerpinB2R380A knock-in (KI) mice contain a CRISPR/Cas9 generated insertion of the R380A (arginine&gt;alanine at residue 380) mutation, resulting in a loss of enzymatic function. Homozygous SerpinB2R380A KI mice are viable and fertile. These mice may be useful for studying the enzymatic activity of SERPINB2 in cellular remodeling, fibrinolysis, autoimmune diseases, as well as innate and adaptive immunity responses.

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SerpinB2R380A knock-in (KI) mice contain a CRISPR/Cas9 generated insertion of the R380A (arginine&gt;alanine) mutation in the serine (or cysteine) peptidase inhibitor, clade B, member 2 (Serpinb2) gene, resulting in a loss of enzymatic function. This strain may be useful for studying the regulatory role of Serpinb2 in plasminogen activation, cell migration and immune response pathways.

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