MASP1
Reactivité: Humain
Hôte: Lapin
Polyclonal
FITC
Indications d'application
For Western blotting 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 1:10. The antibody does not work in Western blotting of reduced samples.
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C
Stockage commentaire
Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one year.
Date de péremption
12 months
Schwaeble, Dahl, Thiel, Stover, Jensenius: "The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation complex encoded by two genes." dans: Immunobiology, Vol. 205, Issue 4-5, pp. 455-66, (2002) (PubMed).
Matsushita, Kuraya, Hamasaki, Tsujimura, Shiraki, Fujita: "Activation of the lectin complement pathway by H-ficolin (Hakata antigen)." dans: Journal of immunology (Baltimore, Md. : 1950), Vol. 168, Issue 7, pp. 3502-6, (2002) (PubMed).
Hajela, Kojima, Ambrus, Wong, Moffatt, Ferluga, Hajela, Gál, Sim: "The biological functions of MBL-associated serine proteases (MASPs)." dans: Immunobiology, Vol. 205, Issue 4-5, pp. 467-75, (2002) (PubMed).
Endo, Takahashi, Kuraya, Matsushita, Stover, Schwaeble, Fujita: "Functional characterization of human mannose-binding lectin-associated serine protease (MASP)-1/3 and MASP-2 promoters, and comparison with the C1s promoter." dans: International immunology, Vol. 14, Issue 10, pp. 1193-201, (2002) (PubMed).
Kuraya, Matsushita, Endo, Thiel, Fujita: "Expression of H-ficolin/Hakata antigen, mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 by human glioma cell line T98G." dans: International immunology, Vol. 15, Issue 1, pp. 109-17, (2002) (PubMed).
Matsushita, Endo, Hamasaki, Fujita: "Activation of the lectin complement pathway by ficolins." dans: International immunopharmacology, Vol. 1, Issue 3, pp. 359-63, (2001) (PubMed).
Three pathways of complement activation have been reported: the antibody-dependent classical pathway, the antibody-independent alternative pathway and the lectin pathway. Activation of each pathway involves formation of serine protease complexes, which results in activation of the central complement component C3. In the lectin pathway, mannose binding-lectin (MBL)-associated serine proteases (MASP) form complexes with polymeric lectin molecules which are involved in pattern recognition. Upon binding of the recognition molecules to carbohydrates on the surface of microorganisms, MASP are converted to their active forms and initiate complement activation. Three types of human MASP have been reported. MASP- 1, MASP-2 and MASP-3. MASP-1 appears to cleave the second complement component C2, but not C4. The proteolytic activities of MASP-1 are inhibited by C1-inhibitor. Furthermore MASP-1 has a reactivity profile very similar to that of thrombin. MASP-1 is able to catalyse the formation of cross-linked fibrin. Participation of MASP-1 in cross- linked fibrin clot formation causes release of a chemotactic factor representing a biologically significant activity of MASP-1. The alternative-splicing product from MASP-1 gene is called MASP-3. MASP-1 is associated with smaller MBL oligomers whereas MASP-3 is found on larger oligomers. The substrate of MASP-3 is unknown. The antibody recognizes the heavy chain common to both MASP-1 and MASP-3.