• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When mouse Laminin I is coated at 10 μg/mL, Recombiant Mouse Integrin alpha 7 beta 1 binds with an apparent K    _D <0.5 nM.  

• Source

  Chinese Hamster Ovary cell line, CHO-derived

  Mouse Integrin alpha 7 (Phe34-Glu1033) Accession # NP_032424	His-Pro	GGGSGGGS	Acidic Tail	6-His tag
  Mouse Integrin beta 1 (Gln21-Asp728) Accession # P09055	His-Pro	GGGSGGGS	Basic Tail
  N-terminus				C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Phe34, Glu915 (Integrin alpha 7) & Gln21 predicted, No results obtained: sequencing might be blocked (Integrin beta 1)

• Structure / Form

  Noncovalently-linked heterodimer

• Predicted Molecular Mass

  119 kDa (Integrin alpha 7, full length), 22.4 kDa (Integrin alpha 7, N-terminus starts at Glu915) & 86.5 kDa (Integrin beta 1)

• SDS-PAGE

  123-157 kDa, 95-100 kDa & 38-42 kDa, reducing conditions

Background: Integrin alpha 7 beta 1

Integrin  alpha 7 beta 1, also called VLA‑7 (very late antigen‑7), is the major laminin‑binding integrin in cardiac and skeletal muscle (1‑4). The non‑covalent heterodimer is composed of ~150 kDa alpha 7 and 130 kDa beta 1/CD29 type I transmembrane glycoprotein subunits with short cytoplasmic tails (2). While alpha 7 pairs only with beta 1, twelve integrins share the beta 1 subunit (1‑5). The longest version of alpha 7 is the X1X2B form, encoding 1179 amino acids (aa). Six alternatively spliced 1116‑1160 aa isoforms of the alpha 7 subunits have short extracellular (X1, X2) or cytoplasmic (A, C) deletions. Isoforms are differentially expressed by tissue and developmental stage and may show preferences for specific laminins (3‑5). The beta 1 vWFA domain participates with the alpha 7 FG‑GAP motifs in ligand binding. The alpha 7 subunit is cleaved into extracellular heavy and transmembrane/cytoplasmic light chains (3). The mouse alpha 7 heavy chain shares 89%, 90%, 87% and 85% aa sequence identity with human, rat, feline and bovine  alpha 7, and the mouse beta 1 ECD shares 98% aa identity with rat and 93‑94% with human, bovine, porcine, ovine, canine and feline beta 1. The alpha 7 heavy chain in species other than mouse may also be cleaved at aa 603‑605 by a serine protease; fragments remain associated. This form enhances the active, unfolded and open conformation, promoting cell adhesion and spreading (1, 2, 6). Adhesion of alpha 7 beta 1 to laminin‑111 accounts for many of its effects, but alpha 7 beta 1 also binds most other laminins (5). It protects muscle from exercise‑induced damage, and its absence in humans or mice causes a form of muscular dystrophy (7‑9). alpha 7 beta 1 is also expressed in vascular smooth muscle (VSM), and is important for development of the cerebral vasculature (10). VSM cells show increased alpha 7 beta 1 expression and enhanced laminin binding in injury‑induced atherosclerosis or PDGF treatment (11, 12). Deletion of alpha 7 results in VSM hyperplasia, especially in response to injury (13).

• References:

1. Takada, Y. et al. (2007) Genome Biol. 8:215.

2. Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.

3. Ziober, B.L. et al. (1993) J. Biol. Chem. 268:26773.

4. Song, W.K. et al. (1993) J. Cell Sci. 106:1139.

5. Nishiuchi, R. et al. (2006) Matrix Biol. 25:189.

6. Liu, J. et al. (2008) J. Biol. Chem. 283:35668.

7. Mayer, U. et al. (1997) Nat. Genet. 17:318.

8. Boppart, M.D. et al. (2006) Am. J. Physiol. Cell. Physiol. 290:C1660.

9. Hodges, B.L. et al. (1997) J. Cell Sci. 110:2873.

10. Flintoff-Dye, N.L. et al. (2005) Dev. Dyn. 234:11.

11. Chao, J.T. et al. (2006) Am. J. Physiol. Cell. Physiol. 290:C972.

12. Chao, J.T. et al. (2004) Am. J. Physiol. Heart Circ. Physiol. 287:H381.

13. Welser, J.V. et al. (2007) Circ. Res. 101:672.

• Alternate Names:

  Integrin alpha 7 beta 1