Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Human Fibronectin
(Catalog #
4305-FNB)
is immobilized at 2 μg/mL, 100 μL/well, Recombinant Human Integrin alpha V beta 1 binds with an ED50 of 0.08-0.48 μg/mL. |
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Source | Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha V beta 1 protein
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N-terminal Sequence | Phe31 ( alpha V subunit) & Gln21 ( beta 1 subunit, inferred from enzymatic pyroglutamate treatment revealing Thr22) |
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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 | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 115 kDa ( alpha V subunit) & 86 kDa ( beta 1 subunit). 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 | 120-170 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 with Trehalose. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 500 μg/mL in water. |
Integrin alpha V beta 1 is one of five alpha V and twelve beta 1 containing Integrin family adhesion receptor heterodimers (1‑3). The non-covalent heterodimer of 170 kDa alpha V and 130 kDa beta 1/CD29 is present on cells that express both subunits, and dimer formation is dependant on the availability of the individual subunits (4). Since the alpha V and beta 1 subunits are widely expressed, the alpha V beta 1 heterodimer potentially forms in many cell types. The 962 aa human alpha V extracellular domain (ECD) shares 92‑95% aa sequence identity with mouse, rat and bovine alpha V, while the 708 aa human beta 1 ECD shares 92‑96% aa sequence identity with mouse, rat, bovine and feline beta 1. The alpha V ECD contains an N‑terminal beta ‑propeller structure, followed by domains termed thigh, calf-1 and calf-2 (1). The beta 1 ECD contains a vWFA domain, which participates in binding. Each subunit then has a transmembrane sequence and a short cytoplasmic tail. The dimer is folded when it is least active. Divalent cations and intracellular (inside-out) signaling convert it to its most active, extended and open conformation (1). alpha V integrins bind ligands that contain an RGD motif, including vitronectin, fibronectin and osteopontin (4‑9). The relatively weak binding affinity of alpha V beta 1 to vitronectin and fibronectin is thought to facilitate its activity in cyclic binding and release during cell migration (4, 5). In oligodendrocytes, astrocytes and pancreatic beta cells, alpha V beta 1 is expressed early in differentiation when cells are migrating and is down‑regulated when differentiation is complete (5‑7). alpha V beta 1 has also been found to be a receptor for angiopoietin-2 in Tie2-deficient glioma cells, and to mediate cell entry of viruses such as foot‑and‑mouth disease virus and human metaneumovirus (10‑12).
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