Target intelligence / Profile preview

Serpin peptidase inhibitor clade B member 12 (SERPINB12)

Target
SERPINB12
Molecular classification
Proteinase inhibitor, Serpin superfamily (Serpin peptidase inhibitors), Clade B (ovalbumin) serpin, Intracellular serine protease inhibitor
01

Overview

SERPINB12 (serpin peptidase inhibitor, clade B [ovalbumin], member 12) is a broadly expressed, intracellular protease inhibitor of the serpin superfamily, with highest expression in epithelial tissues and cells exposed to the external environment (e.g., lung, gastrointestinal tract, reproductive tract, and skin)[1][3]. Its main biological function is the inhibition of trypsin-like serine proteases (e.g., granzyme A, hepsin, trypsin, plasmin), thereby protecting cells and tissues from protease-mediated injury and maintaining barrier integrity[1][3]. Biochemical studies confirm it acts as a slow-binding protease inhibitor, forming stable covalent complexes with its targets[1][3]. Beyond canonical protease inhibition, SERPINB12 may also have a role in transcriptional control and cell differentiation, by participating in multiprotein complexes such as those with hSLFN12[1]. However, it is not currently regarded as a druggable therapeutic target and there are no clinically approved drugs or biomarkers linked to it. Its wide tissue distribution and expression patterns suggest a fundamental cytoprotective function especially in epithelial cells, but direct clinical implications remain largely uncharacterized[1][3].

Other names
Serpin B12SERPINB12YukopinYUKOPINserine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 12serpin peptidase inhibitor, clade B (ovalbumin), member 12
02

Biological functions

Protease inhibition (primarily trypsin-like serine proteases such as granzyme A, hepsin, trypsin, plasmin)Negative regulation of protein catabolic processCellular defense; barrier protection of epithelial cellsPotential regulation of gene expression and transcription in association with proteins such as hSLFN12Cell differentiation
03

Disease associations

Cancer (linked to epithelial barrier protection, and, by analogy with other serpins, possible relevance in tumor progression; however, no direct evidence for driver mutations or approved biomarker use)Other (protective roles in tissues exposed to endogenous/exogenous proteases; direct clinical disease associations are largely speculative or not described for human disease)

Beyond the preview

Go deeper on Serpin peptidase inhibitor clade B member 12 (SERPINB12).

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Full profile access

Explore the programs pursuing this target and their development progress.

  • Drug candidates
  • Developers
  • Development stage

Clinical trials

Full profile access

Follow the clinical studies evaluating therapies directed at this target.

  • Trial design
  • Status
  • Readouts

Competitive landscape

Full profile access

Compare approaches across drug candidates, modalities, and indications.

  • Programs
  • Modalities
  • Indications

Literature & evidence

Full profile access

Investigate the research and source evidence behind target biology and development.

  • Publications
  • Sources
  • Analysis

Patents

Full profile access

Explore patent activity around therapies and technologies addressing this target.

  • Patents
  • Assignees
  • Technologies

Research & analysis

Full profile access

Connect target biology, drug development, and emerging evidence in your research.

  • Biology
  • Development news
  • Analysis

Bring the full picture into focus.

See how Gosset can support your research on Serpin peptidase inhibitor clade B member 12 (SERPINB12).

Explore the full profile

Gosset Free

Get started with Gosset.

Enter your work email and we’ll be in touch with next steps.

Work email preferred.

Book a call