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Cadherin 11(CDH11) is a type II single transmembrane cadherin encoded by CDH11 gene, which is specifically expressed on the cell membrane surface of connective tissue mesenchymal cells, osteoblasts and fibroblasts. CDH11 is anchored at the cell membrane, featuring a modular architecture consisting of extracellular functional segments, a single‑pass transmembrane segment and cytoplasmic tail region. The extracellular domain of the protein contains multiple cadherin repeat domains arranged in series, and each domain has calcium ion coordination sites, and at the same time contains a single transmembrane anchoring structure and a long intracellular sequence, which can be combined with cytoskeleton adaptor protein to realize the functional linkage between extracellular adhesion structure and intracellular skeleton system. CDH11 can form homologous trans-dimer structure between adjacent cells, and maintain the rigid folding conformation of extracellular domain by calcium ion coordination, which is the core structural basis for maintaining stable adhesion and connection between cells. If the folding of extracellular repeat domain of CDH11 is abnormal, it will directly lead to the disorder of adhesion structure of mesenchymal cells, which will lead to out-of-control cell migration behavior and destroy tissue homeostasis in the process of tissue remodeling. Different developmental stages of the body have different demands for tissue adhesion strength, and the expression abundance of CDH11 on the cell membrane surface can dynamically regulate the stability of cell connection, and accurately adapt to the physiological needs of controllable cell migration in interstitial space while maintaining the structural integrity of interstitial tissue. Each cadherin repeat unit of CDH11 contains highly conserved polar amino acid residues, which can specifically bind divalent cations. Cations bound in order along the extracellular domain chain can stabilize the linear extension conformation of the protein, which provides a guarantee for the assembly of homodimer between cells and the formation of stable adhesion connection.
The gene mutation of CDH11 extracellular repeat domain can destroy the calcium ion binding site, weaken the stability of homologous cell connection, and cause the defect of cell adhesion function in primary tissues. Although other members of the cadherin family also have conserved cationic coordination motifs, their cell expression patterns are significantly different, which cannot completely replace the specific adhesion regulation function of CDH11 in mesenchymal cells. At physiological rest, CDH11 is stably embedded in the lipid bilayer structure of cell membrane, and will not fall off to form soluble extracellular fragments. The topological structure of its single transmembrane accurately separates the extracellular adhesion functional area from the intracellular skeleton binding area, which makes CDH11 have dual regulatory functions of maintaining the adhesion integrity of connective tissue and mediating the mechanical signal transmission between cells. Continued down-regulation of CDH11 expression level on cell surface will destroy the structural integrity of mesenchymal cell layer and induce disorderly migration of cells. Therefore, CDH11 is a key target for the study of connective tissue remodeling mechanism and cell adhesion regulation.
Fig. 1 Schematic diagram of human CDH11, illustrating full‑length protein anchored to cell membrane, consisting of extracellular functional segments, single‑pass transmembrane region and cytoplasmic tail domain.1
The biological functions of integral membrane CDH11 type II cadherin are focused on cation-stabilized intercellular contact and cytoskeleton linkage:
Creative Biolabs offers purified CDH11 membrane protein samples produced under unified preparation workflows, including full-length CDH11 constructs and isolated extracellular repeat domain variants. Truncated fragments cannot support complete homotypic dimerization and cytoskeletal coupling activity, while full-length forms fit mesenchymal adhesion research. All batches receive uniform quality screening. Functional assessments may only be performed under simulated lipid bilayer microenvironment setups. Extracellular repeat calcium pocket structure is preserved across batches for comparative dimer interaction testing. Full-length CDH11 membrane samples retain intact cation coordination residues post-purification, supporting reliable detection of transient homodimer complexes in functional comparative analysis.
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Creative Biolabs provides cell research models with adjustable CDH11 expression levels, suitable for structural observation of type II cadherins and tissue remodeling research. Sample assessment covers sustained membrane detection and homotypic binding analysis, enabling side-by-side comparison of junction stability under varying CDH11 abundances. These cell models can be paired with tissue morphology observation schemes to track layer disassembly shifts linked to CDH11 dosage changes.
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Anti-CDH11 recombinant antibodies are generated via standardized workflows, compatible with fibroblast membrane localization mapping and cadherin homodimer complex identification. The antibody series supports multi-dimensional visualization of CDH11 distribution within bone and soft tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for CDH11 research:
CDH11 may act as a type II transmembrane cadherin to form calcium-dependent homotypic junctions and link cell contacts to intracellular cytoskeletons.
CDH11 expression status might alter connective tissue cohesive stability, serving as a key mediator of mesenchymal remodeling homeostasis biological processes.
No, all CDH11 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length CDH11 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on calcium-dependent cell adhesion.
Laboratory analysis schemes may include cadherin co-binding assays to assess junction formation capacity under simulated lipid bilayer environments.