CD11/CD18 (24) Mouse Monoclonal Antibody
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Leukocyte Cd11/Cd18 Integrins: Biological and Clinical Relevance
review Haematologica 1995; 80:161-175 LEUKOCYTE CD11/CD18 INTEGRINS: BIOLOGICAL AND CLINICAL RELEVANCE Antonino Mazzone, Giovanni Ricevuti Dipartimento di Medicina Interna e Terapia Medica, Università di Pavia, IRCCS Policlinico S. Matteo, Pavia, Italy ABSTRACT The integrin family consists of a series of related Ͱͱ heterodimers (subunits of 95,000-200,000 Mw) involved in a variety of cell-matrix and cell-cell adhesion functions. Leukocyte adhesion has biological importance in numerous processes involving host defense. The CD11/CD18 integrins are differentiated antigens which play a critical role in this mechanism. CD11a/CD18 are apparent on early progenitors of all myeloid and erythroid cells. CD11b/CD18 and CD11c/CD18 are more restricted antigens normally expressed on monocytes, macrophages, PMN and natural killer cells. Activated granulocytes and monocytes express far more CD11b/CD18 than the other two antigens: 6 to 8҂105 CD11b/CD18 molecules appear on maximally activated granulocytes. These integrins and in particular the ͱ2 subunit are lacking in a genetic disease. On the other hand, they are funda- mental in numerous physiological processes and in various hematological and cardiovascular dis- eases. The biochemical characterization and behavior of the CD11/CD18 complex in various clini- cal conditions are the subject of this review. Key words: CD11/CD18, integrins, leukocytes ell adhesion molecules play an important role in leukocyte-endothelial cell interac- ͱ1 subfamily (also called VLA proteins) each 1-3 ͱ Ctions. In the immune system these contain the 1 subunit in association with one molecules encourage leukocyte-endothelial cell of at least nine different Ͱ subunits. In the ͱ2 interactions and orchestrate many other types of subfamily, there are three distinct Ͱ subunits cell interactions through a variety of adhesion which associate with ͱ2 (CD11/CD18). -
CD11/CD18 (24) FITC FITC Labeled Mouse Monoclonal Antibody
Product Data Sheet IMQ-84601_2015.09-v1 CD11/CD18 (24) FITC FITC Labeled Mouse Monoclonal Antibody Catalog Number: IMQ-84601 Size: 50 µl (1 mg/ml) Class: Monoclonal Type: Antibody Clone: 24 Host / Isotype: Mouse / IgG1 Immunogen: Fibronectin-purified human monocytes Myeloma / fusion Cells from immunized Balb/c mice were fused with the Sp2/0-Ag.14 myeloma partners: cell line Species Reactivity: Human Specificity: This antibody recognises integrin alpha L,M,X/Beta 2 (CD11/CD18). Integrins are heterodimeric cell surface receptors composed of alpha and beta subunits which mediate cell-cell and cell-extracellular matrix attachments. Integrin beta2 (CD18) associates with integrin alpha L (CD11a) to form the leukocyte function- associated antigen-1 (LFA-1) with integrin alpha M (CD11b) to form Complement Receptor 3 (CR3) and with integrin alpha X (CD11c) to form Complement Receptor 4 (CR4). Each integrin receptor can bind various Intercellular adhesion molecules (ICAMs). Aberrant integrin expression has been found in many epithelial tumours. Changes in integrin expression have been shown to be important for the growth and early metastatic capacity of melanoma cells. Purification: Purified on protein A from tissue culture supernatant. Format: Purified IgG conjugated to Fluoroscein using Innova Biosciences Lightning- Link®, supplied in Phosphate buffered saline (PBS) containing 0.09% Sodium azide Applications: Flow Cytometry, Immunocytochemistry, Immunofluorescence Dilutions: Optimal antibody dilution should be determined by titration Storage: Store stock solution of the antibody at 2-8 °C in the dark. Do not freeze. References: Hogg N, et al. An anti-human monocyte/macrophage monoclonal antibody, reacting most strongly with macrophages in lymphoid tissue. -
Β2 Integrins—Multi-Functional Leukocyte Receptors in Health and Disease
International Journal of Molecular Sciences Review β2 Integrins—Multi-Functional Leukocyte Receptors in Health and Disease Monika Bednarczyk, Henner Stege, Stephan Grabbe and Matthias Bros * Department of Dermatology, University Medical Center Mainz, Langenbeckstraße 1, 55131 Mainz, Germany; [email protected] (M.B.); [email protected] (H.S.); [email protected] (S.G.) * Correspondence: [email protected]; Tel.: +49-6131-17-9846 Received: 6 January 2020; Accepted: 14 February 2020; Published: 19 February 2020 Abstract: β2 integrins are heterodimeric surface receptors composed of a variable α (CD11a-CD11d) and a constant β (CD18) subunit and are specifically expressed by leukocytes. The α subunit defines the individual functional properties of the corresponding β2 integrin, but all β2 integrins show functional overlap. They mediate adhesion to other cells and to components of the extracellular matrix (ECM), orchestrate uptake of extracellular material like complement-opsonized pathogens, control cytoskeletal organization, and modulate cell signaling. This review aims to delineate the tremendous role of β2 integrins for immune functions as exemplified by the phenotype of LAD-I (leukocyte adhesion deficiency 1) patients that suffer from strong recurrent infections. These immune defects have been largely attributed to impaired migratory and phagocytic properties of polymorphonuclear granulocytes. The molecular base for this inherited disease is a functional impairment of β2 integrins due to mutations within the CD18 gene. LAD-I patients are also predisposed for autoimmune diseases. In agreement, polymorphisms within the CD11b gene have been associated with autoimmunity. Consequently, β2 integrins have received growing interest as targets in the treatment of autoimmune diseases. -
Integrin Beta-2
UCSD MOLECULE PAGES doi:10.6072/H0.MP.A004263.01 Volume 2, Issue 2, 2013 Copyright UC Press, All rights reserved. Review Article Open Access Integrin beta-2 Ashok Reddy Dinasarapu1, Anjana Chandrasekhar1, George Hajishengallis2, Shankar Subramaniam3 Integrins are heterodimeric transmembrane (TM) glycoproteins containing one each of α and β subunit, which are held together by non-covalent forces. Integrin β2 (CD18) is the β subunit for four heterodimers: αDβ2, αXβ2, αMβ2 and αLβ2. Integrin β2 family plays an essential role in leukocyte recruitment and activation during inflammation. Structurally, while most part of the αβ dimer is extracellular, both the subunits traverse the plasma membrane and terminate as short cytoplasmic domains. Each heterodimeric integrin exists on the cell surface mainly in an inactive (bent) form until they receive stimulating signals from other receptors (via inside-out signaling), and the end result of integrin activation is a shift in integrin conformation from a bent to an extended one. The binding of cytoplasmic proteins to α- and/or β-subunit carboxy-terminal tails is an essential part of the activation process, as these interactions stabilize the extended integrin conformation and provide connections to the cytoskeleton. The binding of extracellular ligand to the extended form of integrin (via outside-in signaling) triggers a large variety of signal transduction events that modulate cell behaviors such as adhesion, proliferation, survival or apoptosis, shape, polarity, motility, and differentiation, mostly through effects on the cytoskeleton. The receptors αMβ2 (Complement Receptor type 3, CR3) and αXβ2 (Complement Receptor type 4, CR4) are regarded to be the most important mediators for complement-driven phagocytosis.