Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When mouse Laminin I (Catalog # 3400-010-02) is coated at 10 μg/mL, Recombinant Mouse Integrin alpha 7 beta 1 binds with an apparent KD <0.5 nM. |
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Source | Chinese Hamster Ovary cell line, CHO-derived mouse Integrin alpha 7 beta 1 protein
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Accession # | |||||||||||||||
N-terminal Sequence | Phe34, Glu915 (Integrin alpha 7) & Gln21 predicted, No results obtained: sequencing might be blocked (Integrin beta 1) |
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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 under reducing conditions and visualized by silver stain. |
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Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 119 kDa (Integrin alpha 7, full length), 22.4 kDa (Integrin alpha 7, N-terminus starts at Glu915) & 86.5 kDa (Integrin beta 1). 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. |
SDS-PAGE | 123-157 kDa, 95-100 kDa & 38-42 kDa, reducing conditions |
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. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 400 μg/mL in PBS. |
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).
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