G-CSF Antikörper

Antigen: G-CSF

Klonalität: Monoklonal (BVD13-3A5)

Wirt: Ratte

Reaktivität: Human

Applikation: ELISA (Fangantikörper), ELISPOT (Fangantikörper), Neutralisierung (Neut), Immunhistochemie (IHC)

Produktnummer: ABIN160205

Produktbeschreibung

Immunogen: E. coli-expressed, recombinant human G-CSF

Format: Low endotoxin (sterile), Low-endotoxin, azide-free (LEAF)

Isotyp: IgG1, kappa chain  (Passende Sekundärantikörper)

Klon: BVD13-3A5

Beschreibung: Growth/differentiation/activating factor for neutrophils, proliferation/migration endothelial cells cells, synergistic with IL-3 growth of hematopoietic progenitors Macrophages, monocytes, neutrophils, fibroblasts, endothelial cells, bone marrow stromal cells Granulocyte - colony stimulating factor (G-CSF) is a potent stimulator of bone marrow cells especially those of neutrophilic granulocyte lineage. In addition, G-CSF can enhance the survival and activate the immunological functions of mature neutrophils. G-CSF is produced primarily by monocytes and macrophages upon activation by endotoxin, TNF-alpha or IFN-gamma. The BVD13-3A5 antibody reacts with human granulocyte-colony stimulating factor (G-CSF). The BVD13-3A5 antibody can neutralize the bioactivity of natural or recombinant G-CSF. Synonyms: Granulocyte-Colony Stimulating Factor, CSF-beta, Pluripoietin, Granulocytic neutrophil colony stimulating activity (G-CSA), Macrophage-granulocyte inducer-2 (MGI-2) Regulation: Upregulated by IL-1, IL-17, TNF-alpha, IFN-gamma, GM-CSF, downregulated by prostaglandin E2 Structure: Cytokine, 21 kD (Mammalian)

Anwendungen

Applikationshinweise: ELISA or ELISPOT Capture: The purified BVD13-3A5 antibody is useful as the capture antibody in a sandwich ELISA or ELISPOT assay, when used in conjunction with the biotinylated BVD11-37G10 antibody (ABIN160485) as the detecting antibody. The LEAF(TM) purified antibody is suggested for ELISPOT capture. Neutralization: The LEAF(TM) purified antibody (Endotoxin <0.1 EU/µg, Azide-Free, 0.2 µm sterile-filtered) is recommended for neutralization of human G-CSF bioactivity (ABIN160205). Additional reported applications (for the relevant formats) include: immunohistochemical staining of paraformaldehyde-fixed, saponin-treated frozen tissue sections, and immunocytochemistry. Each lot of this antibody is quality control tested by ELISA assay. For ELISA capture applications, a concentration range of 1-4 µg/ml is recommended. It is recommended that the reagent be titrated for optimal performance for each application.

Reinheit: LEAF

Reinigung: The antibody was purified by affinity chromatography.

Buffer: Phosphate-buffered solution, pH 7.2, containing no preservative. 0.2 µm filter sterilized. Endotoxin level is < 0.1 EU/µg of the protein (< 0.01 ng/µg of the protein) as determined by the LAL test.

Lagerung: The antibody solution should be stored undiluted at 4° C. This LEAF(TM) solution contains no preservative, handle under aseptic conditions.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

anti-G-CSF antibody

Publikationen

Publikationen: Abrams, Roncarolo, Yssel et al.: "Strategies of anti-cytokine monoclonal antibody development: immunoassay of IL-10 and IL-5 in clinical samples." in: Immunological reviews, Vol. 127, pp. Mai 24, 1992 (PubMed).

Negrin, Greenberg: "Therapy of hematopoietic disorders with recombinant colony-stimulating factors." in: Advances in pharmacology (San Diego, Calif.), Vol. 23, pp. 263-96, 1992 (PubMed).

Demetri, Griffin: "Granulocyte colony-stimulating factor and its receptor." in: Blood, Vol. 78, Issue 11, pp. 2791-808, 1991 (PubMed).

Sander, Andersson, Andersson: "Assessment of cytokines by immunofluorescence and the paraformaldehyde-saponin procedure." in: Immunological reviews, Vol. 119, pp. 65-93, 1991 (PubMed).

Andersson, Abrams, Bjoerk et al.: "Concomitant in vivo production of 19 different cytokines in human tonsils." in: Immunology, Vol. 83, Issue 1, pp. 16-24, 1995 (PubMed).

Schulz, Reeves, Hoad et al.: "Effect of mutations in the V3 loop of HIV-1 gp120 on infectivity and susceptibility to proteolytic cleavage." in: AIDS research and human retroviruses, Vol. 9, Issue 2, pp. 159-66, 1993 (PubMed).