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Integrin subunit alpha 5 (ITGA5) is a single transmembrane integrin α subunit encoded by ITGA5 gene, which is mainly expressed on the surface of fibroblasts and epithelial cells, and can be specifically assembled with ITGB1 subunit to form a heterodimer functional complex. The protein structure includes a large extracellular spherical functional region, a single transmembrane spiral structure and a short cytoplasmic tail region, in which the extracellular spherical structural region has RGD ligand binding sites with stable metal ions, and the intracellular segment can adhere to the adhesion spot adaptor protein, thus realizing the functional coupling between extracellular matrix and intracellular skeleton signals. When ITGA5 and ITGB1 are assembled into a mature receptor complex, they can specifically recognize and bind the RGD characteristic sequence of fibronectin, mediate the anchoring connection between cells and extracellular matrix network, maintain the dynamic balance of cell migration rate in the process of tissue renewal and remodeling, and ensure the orderly progress of tissue repair and remodeling.
If the assembly of ITGA5-ITGB1 heterodimer is disordered and its function is lost, the cells will lose their stable adhesion ability to extracellular matrix, leading to the disorderly dissociation and uncontrolled migration of cells in the interstitial space. There is significant heterogeneity in fibronectin fiber density in different tissue regions. Cells can dynamically adjust the ligand binding ability by regulating the expression abundance of ITGA5 on the cell membrane surface, accurately adapt to the local matrix microenvironment characteristics, and avoid the adhesion homeostasis imbalance caused by excessive anchoring rigidity or complete detachment from the matrix. The highly conserved cationic binding site in the extracellular spherical domain of ITGA5 can form a stable coordination bond with the acidic amino acid residue of fibronectin RGD sequence, and metal ions in the physiological concentration range can directly regulate the ligand binding affinity, thus realizing the fine dynamic regulation of cell-matrix adhesion strength.
Sequence variants within ITGA5 extracellular head domains might disrupt metal coordination and lower fibronectin ligand affinity in primary tissue models. Other integrin alpha subunits recognize distinct ECM ligands and cannot fully replicate ITGA5’s preference for fibronectin RGD-containing multimers, even though they share similar globular fold architecture. ITGA5 only achieves full ligand recognition function after pairing with beta subunits and remains permanently embedded within lipid bilayers. Its single-pass topology separates extracellular matrix sensing domains from cytoplasmic signal transducers, granting the subunit dual potential to regulate cell anchoring and relay mechanical cues into intracellular response cascades. Sustained reduction of ITGA5 expression weakens cell-matrix linkage and disturbs ordered tissue turnover, making this integrin subunit a suitable research target for ECM remodeling analysis.
Fig. 1 Schematic representation of the ITGA5‑ITGB1 bidirectional signaling pathway, showing conformational transitions between inactive and active integrin states.1
The biological functions of integral membrane ITGA5 integrin alpha subunit are focused on metal-dependent ECM ligand capture and cytoplasmic adaptor linkage:
Creative Biolabs offers purified ITGA5 membrane protein samples produced under unified preparation workflows, including full-length ITGA5 constructs and isolated extracellular head domain variants. Truncated fragments cannot support complete RGD ligand recognition and focal adhesion coupling activity, while full-length forms fit ECM remodeling research. All batches receive uniform quality screening. Functional assessments may only be performed under simulated lipid bilayer microenvironment setups. Extracellular cation pocket structural features are preserved across batches for comparative ligand binding testing. Full-length ITGA5 membrane samples retain intact metal coordination residues post-purification, supporting reliable detection of transient fibronectin-integrin complexes in functional comparative analysis.
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Creative Biolabs provides cell research models with adjustable ITGA5 expression levels, suitable for structural observation of fibronectin-binding integrins and tissue turnover research. Sample assessment covers sustained membrane detection and fibronectin binding analysis, enabling side-by-side comparison of anchoring behavior under varying ITGA5 abundances. These cell models can be paired with ECM fiber visualization schemes to track cell detachment shifts linked to ITGA5 dosage changes.
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Anti-ITGA5 recombinant antibodies are generated via standardized workflows, compatible with fibroblast membrane localization mapping and integrin heterodimer complex identification. The antibody series supports multi-dimensional visualization of ITGA5 distribution within connective tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for ITGA5 research:
ITGA5 may act as a transmembrane integrin alpha subunit to form ITGB1 heterodimers and bind fibronectin RGD motifs for cell-matrix anchoring.
ITGA5 expression status might alter connective tissue anchoring stability, serving as a key mediator of ECM turnover homeostasis biological processes.
No, all ITGA5 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 ITGA5 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on fibronectin-dependent cell adhesion.
Laboratory analysis schemes may include ECM ligand binding assays to assess RGD recognition capacity under simulated lipid bilayer environments.