Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized Collagen I at 10 µg/mL (100 µL/well) can bind Recombinant Human Integrin alpha 11 beta 1 with an apparent Kd <2.0 nM. Optimal dilutions should be determined by each laboratory for each application. |
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Source | Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha 11 beta 1 protein
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N-terminal Sequence | Phe23 ( alpha 11) & Gln21 (predicted, not observed) ( beta 1) |
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Structure / Form | Noncovalently-linked heterodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 134.6 kDa ( alpha 11) & 88.4 ( beta 1). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 160-180 kDa & 120-140 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
Integrin alpha 11 beta 1 is a noncovalent, heterodimeric collagen receptor that contains a 150 kDa alpha 11 subunit complexed to a 130 kDa beta 1/CD29 subunit. alpha 11 beta 1 is the only known alpha 11-containing integrin. By contrast, at least twelve alpha -integrins share the beta 1 subunit (1-5). alpha 11 beta 1 is expressed on fibroblasts from cornea, skin and periodontal ligament (3‑9). It is also expressed on mesenchymal stem cells and is considered a marker for non‑muscle mesenchymal tissue (3, 8‑10). Expression of alpha 11 beta 1 is stimulated by TGF‑ beta 1, activin A, and type I interferons, and down‑regulated by FGF-2 (6, 9‑11). The alpha 11 extracellular domain (ECD) contains a vWFA domain which includes the ligand binding site (2‑5). The beta 1 ECD also contains a vWFA domain, which participates in binding. Each subunit has a transmembrane sequence and a short cytoplasmic tail. The dimer assumes a folded configuration at "rest". Divalent cations and intracellular (inside‑out) signaling convert it to an active, extended and open conformation (1, 2). The 1120 amino acid (aa) human alpha 11 ECD shares 90‑93% aa sequence identity with mouse, rat, equine, canine and bovine alpha 11, while the 708 aa human beta 1 ECD shares 92‑96% aa sequence identity with rat, bovine, mouse, and feline beta 1. I domain-containing beta 1 integrins alpha 1 beta 1, alpha 2 beta 1, alpha 10 beta 1 and alpha 11 beta 1 all bind collagens (3‑5). alpha 11 beta 1 preferentially binds interstitial collagens such as type I (5, 8, 12). It can contract collagen matrices and influence inflammatory edema (3, 13). Depending on context, alpha 11 beta 1 can support or inhibit cell migration on collagen (7, 8). It is frequently up‑regulated in the stroma of lung adenocarcinomas and enhances tumorigenicity (14, 15).
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