Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Integrin alpha V beta 1 is coated at 5 μg/mL, Human Fibronectin (Catalog # ) binds with an apparent K d <0.1 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived
Mouse Integrin alpha V
(Phe31-Val988)
Accession # P43406HP GS Linker Acidic Tail HHHHHH Mouse Integrin beta 1
(Gln21-Asn728)
Accession # P09055His GS Linker Basic Tail N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisPhe31 ( alpha V subunit) & Gln21 predicted ( beta 1 subunit), No results obtained: sequencing might be blocked
Structure / Form
Noncovalently-linked heterodimer
Predicted Molecular Mass
115 kDa ( alpha V subunit) & 86.4 kDa ( beta 1 subunit)
SDS-PAGE
115-165 kDa, reducing conditions
7705-AV |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 400 μg/mL in PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: Integrin alpha V beta 1
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 dependent 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 958 aa mouse alpha V extracellular domain (ECD) shares 92‑95% aa sequence identity with human and bovine alpha V, while the 708 aa mouse beta 1 ECD shares 98% aa identity with rat and 93‑94% aa identity with human, bovine, porcine, ovine, canine 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).
References:
Hynes, R.O. (2002) Cell 110:673.
Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.
Argraves, W.S. et al. (1987) J. Cell Biol. 1025:1183.
Koistinen, P. and J. Heino (2002) J. Biol. Chem. 277:24835.
Kaido, T. et al. (2004) J. Biol. Chem. 279:17731.
Milner, R. et al. (1996) J. Neurosci. 16:7240.
Milner, R. et al. (2001) Mol. Cell. Neurosci. 18:108.
Koivisto, L. et al. (2000) Exp. Cell Res. 255:10.
Hu, D.D. et al. (1995) J. Biol. Chem. 270:26232.
Hu, B. et al. (2006) Cancer Res. 66:775.
Jackson, T. et al. (2002) J. Virol. 76:935.
Cseke, G. et al. (2009) Proc. Natl. Acad. Sci. USA 106:1566.
Entrez Gene IDs:
3685 (Human)
Alternate Names:
Integrin alpha V beta 1
