Recombinant Mouse Integrin alpha 7 beta 1 Protein, CF

Recombinant Mouse Integrin alpha 7 beta 1 Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

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).

Related Research Areas

• Actin Stress Fibers and Focal Adhesions During EMT
• Adhesion Molecules
• Adhesion Molecules in Angiogenesis
• Adhesion Molecules on VSMC
• Integrins and Associated Molecules
• Muscle Stem Cell Markers
• Myogenesis Markers
• Myogenic Precursor Markers
• Skeletal Muscle Markers