• 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 # P43406	HP	GS Linker	Acidic Tail	HHHHHH
  Mouse Integrin beta 1 (Gln21-Asn728) Accession # P09055	His	GS Linker	Basic Tail
  N-terminus				C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Phe31 ( 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

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:

1. Hynes, R.O. (2002) Cell 110:673.

2. Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.

3. Argraves, W.S. et al. (1987) J. Cell Biol. 1025:1183.

4. Koistinen, P. and J. Heino (2002) J. Biol. Chem. 277:24835.

5. Kaido, T. et al. (2004) J. Biol. Chem. 279:17731.

6. Milner, R. et al. (1996) J. Neurosci. 16:7240.

7. Milner, R. et al. (2001) Mol. Cell. Neurosci. 18:108.

8. Koivisto, L. et al. (2000) Exp. Cell Res. 255:10.

9. Hu, D.D. et al. (1995) J. Biol. Chem. 270:26232.

10. Hu, B. et al. (2006) Cancer Res. 66:775.

11. Jackson, T. et al. (2002) J. Virol. 76:935.

12. Cseke, G. et al. (2009) Proc. Natl. Acad. Sci. USA 106:1566.

• Entrez Gene IDs:

  3685 (Human)

• Alternate Names:

  Integrin alpha V beta 1