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MBP/MBL Antikörper (Mannan Binding Protein/Mannan Binding Lectin) Primary Antibody

MBP/MBL Reaktivität: Human BR, IA, IHC (fro), FACS, WB Wirt: Maus Monoclonal 3E7 unconjugated
Pubmed (5 Referenzen)
Produktnummer ABIN2191923
$797.69
Zzgl. Versandkosten $45.00
100 μg
Lieferung in 6 bis 8 Werktagen
  • Target Alle MBP/MBL Antikörper anzeigen
    MBP/MBL
    Reaktivität
    • 8
    • 2
    • 2
    • 1
    • 1
    Human
    Wirt
    • 6
    • 2
    • 1
    Maus
    Klonalität
    • 7
    • 2
    Monoklonal
    Konjugat
    • 7
    • 2
    Dieser MBP/MBL Antikörper ist unkonjugiert
    Applikation
    • 7
    • 4
    • 3
    • 3
    • 3
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    Blocking Reagent (BR), Immunoassay (IA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Flow Cytometry (FACS), Western Blotting (WB)
    Sterilität
    0.2 μm filtered
    Klon
    3E7
  • Applikationshinweise
    For Western blotting, flow cytometry and immunohistology dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50. For neutralization of biological activity dilutions have to be made according to the amounts MBL to be inactivated.
    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Buffer
    PBS (exact concentration is indicated on the label).
    Lagerung
    4 °C
    Informationen zur Lagerung
    Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one year.
    Haltbarkeit
    12 months
  • de Vries, Walter, Peutz-Kootstra, Wolfs, van Heurn, Buurman: "The mannose-binding lectin-pathway is involved in complement activation in the course of renal ischemia-reperfusion injury." in: The American journal of pathology, Vol. 165, Issue 5, pp. 1677-88, (2004) (PubMed).

    Nauta, Castellano, Xu, Woltman, Borrias, Daha, van Kooten, Roos: "Opsonization with C1q and mannose-binding lectin targets apoptotic cells to dendritic cells." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 173, Issue 5, pp. 3044-50, (2004) (PubMed).

    Nauta, Raaschou-Jensen, Roos, Daha, Madsen, Borrias-Essers, Ryder, Koch, Garred: "Mannose-binding lectin engagement with late apoptotic and necrotic cells." in: European journal of immunology, Vol. 33, Issue 10, pp. 2853-63, (2003) (PubMed).

    Hisano, Matsushita, Fujita, Endo, Takebayashi: "Mesangial IgA2 deposits and lectin pathway-mediated complement activation in IgA glomerulonephritis." in: American journal of kidney diseases : the official journal of the National Kidney Foundation, Vol. 38, Issue 5, pp. 1082-8, (2001) (PubMed).

    Matsushita, Takahashi, Hatsuse, Kawakami, Fujita: "Human mannose-binding protein is identical to a component of Ra-reactive factor." in: Biochemical and biophysical research communications, Vol. 183, Issue 2, pp. 645-51, (1992) (PubMed).

  • Target
    MBP/MBL
    Andere Bezeichnung
    Mbl (MBP/MBL Produkte)
    Synonyme
    COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, MBPD, pMBP-27, MBL1, cMBl, collectin, L-MBP, MBL-C, RaRF p28A, mbl, mannose binding lectin 2, mannose-binding lectin (protein C) 2, mannose-binding protein C-like, MBL2, Mbl2, LOC100911854
    Hintergrund
    Mannose Binding Lectin (MBL) also called mannose- or mannan-binding protein (MBP) is a member of the group of collectins. MBL is an oligomeric lectin that recognizes carbohydrates as mannose and N- acetylglucosamine on pathogens. MBL contains a cysteine rich, a collagen like and a carbohydrate recognition domain. It forms a complex with C1r/C1s like serine proteases designated MASPs that proteolytically cleave C4, C2 and C3. MBL is able to activate the complement pathway independent of the classical and alternative complement activation pathways. The MBL-MASP pathway (better known as the lectin pathway) is antibody and C1q-independent. MBL exhibits complement-dependent antibacterial activity and acts directly as an opsonic and therefore plays an important role in innate immunity. MBL is synthesized by hepatocytes and has been isolated from the liver or serum of various vertebrate species.
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