Integrin, alpha M (Complement Component 3 Receptor 3 Subunit) (ITGAM) Antikörper (FITC)

Antigen: Integrin, alpha M (Complement Component 3 Receptor 3 Subunit) (ITGAM)

Synonyme: CR3A, MO1A, CD11B, MAC-1, MAC1A, SLEB6, MGC117044, CR3, MAC1, Cd11b, Ly-40, Mac-1, Mac-1a, CD11b/CD18, F730045J24Rik, ITGAM, Itgam

Klonalität: Monoklonal (CBRM1-5)

Wirt: Maus

Reaktivität: Human

Konjugat: FITC

Applikation: Durchflusszytometrie (FACS)

Produktnummer: ABIN157660

Produktbeschreibung

Weitere Bezeichnung: CD11b (activated)

Isotyp: IgG1, kappa chain

Klon: CBRM1-5

Beschreibung: The CBRM1/5 antibody reacts with an activated form of human CD11b, a 165-170 kD type I transmembrane glycoprotein also known as alphaM integrin, Mac-1, CR3, and C3biR. CD11b non-covalently associates with integrin beta2 (CD18) and is expressed on granulocytes, monocytes/macrophages dendritic cells, NK cells, and subsets of T and B cells. CD11b/CD18 is critical for the transendothelial migration of monocytes and neutrophils, as well as adhesion, phagocytosis and neutrophil activation. CD11b/CD18 interacts with ICAM-1 (CD54), ICAM-2 (CD102), ICAM-4, CD14, CD23, heparin, iC3b, fibrinogen and Factor X. The CBRM1/5 antibody recognizes a subset of CD11b molecules on neutrophils and monocytes activated with chemoattractants or phorbol-esters. This antibody does not recognize non-activated CD11b. The epitope recognized by CBRM1/5 is contained in the I domain of the alpha chain. The CBRM1/5 antibody blocks cell adhesion to fibrinogen and ICAM-1. Distribution: Granulocytes, monocytes/macrophages, dendritic cells, NK cells, T cell subset, B cell subset Function: Adhesion, phagocytosis, chemotaxis, neutrophil activation Synonyms: Integrin alphaM chain, C3biR, CR3, Mac-1, Mo1 Structure: Integrin, type I transmembrane glycoprotein, associates with integrin beta2 (CD18), 165-170 KD

Anwendungen

Applikationshinweise: Additional reported applications (for the relevant formats) include: immunoprecipitation, and blocking of the binding of ICAM-1 and fibrinogen. The CBRM1/5 antibody binds specifically to the activated form of CD11b. The LEAF(TM) purified antibody (Endotoxin <0.1 EU/µg, Azide-Free, 0.2 µm sterile-filtered) is recommended for functional assays (ABIN157664). Each lot of this antibody is quality control tested by immunofluorescent staining with flow cytometric analysis. For immunofluorescent staining, the suggested use of this reagent is 20 µl per million cells or 20 µl per 100 µl of whole blood. It is recommended that the reagent be titrated for optimal performance for each application.

Reinigung: The antibody was purified by affinity chromatography, and conjugated with FITC under optimal conditions. The solution is free of unconjugated FITC.

Buffer: Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 0.2% (w/v) BSA (origin USA).

Lagerung: The antibody solution should be stored undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.

Forschungsgebiet: CD Antigene

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

PMA activated human granulocytes stained with CBRM1/5 FITC

Publikationen

Publikationen: Diamond, Springer: "A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen." in: The Journal of cell biology, Vol. 120, Issue 2, pp. 545-56, 1993 (PubMed).

Stewart, Thiel, Hogg: "Leukocyte integrins." in: Current opinion in cell biology, Vol. 7, Issue 5, pp. 690-6, 1996 (PubMed).

Petty, Todd: "Integrins as promiscuous signal transduction devices." in: Immunology today, Vol. 17, Issue 5, pp. 209-12, 1997 (PubMed).

Bryn, Mahic, Enserink et al.: "The cyclic AMP-Epac1-Rap1 pathway is dissociated from regulation of effector functions in monocytes but acquires immunoregulatory function in mature macrophages." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 176, Issue 12, pp. 7361-70, 2006 (PubMed).

Sithu, English, Olson et al.: "Membrane-type 1-matrix metalloproteinase regulates intracellular adhesion molecule-1 (ICAM-1)-mediated monocyte transmigration." in: The Journal of biological chemistry, Vol. 282, Issue 34, pp. 25010-9, 2007 (PubMed).