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Periostin (POSTN) is a secreted matricellular matrix protein encoded by POSTN gene, belonging to fasciclin domain-containing protein family and acting as central coordinator of extracellular matrix assembly and fibroblast activation. POSTN is predominantly secreted by stromal fibroblasts and reactive epithelial cells, carrying evolutionarily conserved integrin-binding fasciclin domains across species, serving as essential modulator for collagen crosslinking, cell-matrix adhesion and profibrotic signal amplification. POSTN-mediated matrix interaction exerts decisive effects on sustaining tissue tensile structure during repair, while driving progressive matrix deposition under sustained stress conditions. Furthermore, POSTN coordinates downstream signaling cascades governing fibroblast proliferation, inflammatory cell adhesion and epithelial phenotypic transition to regulate tissue scar formation. Distinct from other matricellular factors with restricted tissue distribution, POSTN carries unique non-redundant profibrotic functions across multiple organ systems, rendering it indispensable for wound remodeling and pathological fibrotic progression.
POSTN executes biological functions via anchoring to extracellular collagen fibrils and engaging cell-surface integrin receptors, stimulating fibroblast synthetic programs to promote matrix protein production and crosslinking. Its conserved fasciclin domains mediate stable matrix-cell linkage to amplify profibrotic signal transmission, balancing controlled tissue repair against excessive scar accumulation. POSTN participates in wide-ranging biological processes including collagen remodeling, fibroblast activation, inflammatory stromal infiltration and epithelial-mesenchymal shift. Elevated POSTN secretion disturbs matrix turnover equilibrium, triggering irreversible tissue fibrosis and supporting invasive phenotypic transformation in epithelial lesions. Therefore, POSTN constitutes a pivotal research target for matrix biology, organ fibrosis and tumor stromal progression mechanisms.
Fig. 1 Reciprocal paracrine loop mediated by POSTN exon17 isoform between cancer cells and CAFs; their secreted IL6/IL8 drive recruitment and polarization of CD163-positive TAMs, which in turn secret inflammatory cytokines to amplify malignant signaling.1
The biological functions of POSTN are focused on fasciclin domain-mediated integrin binding, collagen matrix stabilization and fibrotic phenotype regulation:
Creative Biolabs offers high-quality POSTN proteins via optimized expression systems, covering full-length POSTN and isolated fasciclin domain variants. These products retain native matrix-binding conformation and intrinsic integrin-interacting activity, suitable for collagen assembly, fibroblast signaling and anti-fibrotic compound screening. All POSTN proteins undergo rigorous quality control to guarantee consistent functional performance and reliable application across diverse research platforms.
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Creative Biolabs provides custom engineered POSTN stable cell lines, including overexpression and gene silencing models. These cell line models are optimized for matrix remodeling, fibrotic stromal phenotype and compound response profiling. Each cell line undergoes strict validation procedures to ensure steady target expression levels and uniform functional performance across multiple experimental scenarios.
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High-specificity recombinant antibodies targeting POSTN are developed with advanced antibody engineering workflows, without cross-reactivity against other fasciclin-containing matricellular proteins. These antibodies receive multi-scenario functional validation, applicable to protein expression profiling, extracellular matrix deposition detection, integrin-matrix binding assessment and fibrotic research, enabling precise characterization of POSTN expression patterns, tissue matrix distribution and functional modulation under physiological and pathological states.
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Beyond catalog products, Creative Biolabs offers specialized custom services for POSTN research:
POSTN is a secreted matricellular protein that binds collagen and cell integrins to regulate extracellular matrix assembly and drive fibroblast profibrotic activation.
POSTN is a master regulator of pathological matrix deposition; sustained expression drives irreversible organ fibrosis and stromal remodeling in proliferative lesions, establishing it as a vital research target.
No, all POSTN products and services are strictly for research use only, not intended for clinical diagnosis or treatment.
Offerings include POSTN proteins, high-specificity recombinant antibodies and custom stable cell lines for matrix remodeling and fibrotic disease research.
POSTN proteins undergo functional verification via collagen and integrin binding affinity assessment, fasciclin domain conformational stability evaluation.