| Reactivity | MuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Measured by the ability of the immobilized protein to support the adhesion of CHO Chinese hamster ovary cells transfected with ICAM-1. The ED50 for this effect is 0.4-1.6 μg/mL. |
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| Source | Chinese Hamster Ovary cell line, CHO-derived mouse Integrin alpha M beta 2 protein
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| N-terminal Sequence | Phe17 (Integrin alpha M) & Gln24 predicted, No results obtained: sequencing might be blocked (Integrin beta 2) |
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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 with silver staining |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 130 kDa (Integrin alpha M) & 83 kDa (Integrin beta 2). 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. |
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| SDS-PAGE | 155-180 kDa & 95-105 kDa, reducing conditions |
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| Publications |
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| 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 with silver staining |
| Reconstitution Instructions | Reconstitute at 400 μg/mL in PBS. |
Integrin alpha M beta 2, also called MAC‑1 or complement receptor type 3 (CR3), is one of three leukocyte beta 2 integrins. The non‑covalent heterodimer of 170 kDa alpha M/CD11b and 95 kDa beta 2/CD18 integrin subunits is expressed mainly on myeloid and natural killer cells (1‑6). The alpha M vWFA or I‑domain, which contains adhesion sites, forms the N‑terminal head region with the alpha M beta ‑propeller and the beta 2 vWFA domain. Unlike most integrins, the calf domain of alpha M is lectin‑like and binds carbohydrates (7). Each subunit has a transmembrane sequence and a short cytoplasmic tail. The 1089 amino acid (aa) mouse alpha M/CD11b ECD shares 87% aa sequence identity with rat, and 70‑74% with human, equine, bovine, feline, and canine alpha M ECD. A potential mouse alpha M isoform lacks 117 aa within the beta ‑propeller. The 679 aa mouse beta 2/CD18 ECD shares 91% aa sequence identity with rat, and 80‑82% with human, bovine, canine, and porcine beta 2 ECD. Like other integrins, alpha M beta 2 has multiple activation states (1‑3). In the presence of divalent cations and "inside‑out" signaling, alpha M beta 2 is fully active and extended. In the inactive state, the heterodimer flexes in the center at the alpha M thigh and calf domains and beta 2 I‑EGF domains, impeding access to adhesion sites. Active alpha M beta 2 binds an unusually large number of adhesion partners, including the complement opsonin fragment iC3b, coagulation proteins fibrinogen, plasminogen and factor X, extracellular matrix (ECM) proteins fibronectin, laminin and collagen, and cell surface ICAMs, myelin basic protein and DC-SIGN (3, 4, 7). alpha M beta 2 lectin-like adhesion partners include heparin, bacterial lipopolysaccharides, and GPI‑linked glycoproteins such as uPAR and Fc gamma RIIIB (3, 7). Binding of platelet JAM‑C links platelets with myeloid and dendritic cell (DC) alpha M beta 2 and recruits these cells to inflamed or injured endothelium, while neutrophil alpha M beta 2 adheres to RAGE on inflamed endothelium; both are atherogenic events (3, 8, 9). However, activation of alpha M beta 2 inhibits alternative activation of macrophages and atherosclerotic foam cell formation (3, 10). alpha M beta 2 can either suppress or allow constitutive neutrophil apoptosis, depending on its ligand and activation state (3, 11, 12). Deletion of mouse alpha M causes defects in neutrophil adhesion and degranulation, while mutations of human or mouse beta 2 cause leukocyte adhesion deficiency (LAD‑1) and susceptibility to bacterial infections (3, 12, 13).
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