For the orders from outside of China: MOQ 15 plates, lead time: 2 weeks.The online Datasheet here is only a general version, for batch specific information please refer to the hard copy included in the product shipping package.
Quantitative determination of Human ficolin 1/FCN1
1. Capture Antibody 0.3 mg/mL of mouse anti-Human Ficolin-1 / Ficolin-A / FCN1 monoclonal antibody (in PBS, pH 7.4). Dilute to a working concentration of 1 μg/mL in PBS before coating. (Catalog: # 10930-MM05) 2. Detection Antibody 0.5 mg/mL of mouse anti-Human Ficolin-1 / Ficolin-A / FCN1 monoclonal antibody conjugated to horseradish-peroxidase (HRP) (in PBS, 50 % HRP-Protector, pH 7.4, store at 4℃). Dilute to working concentration of 0.1 μg/mL in detection antibody dilution buffer before use. (Catalog: # 10930-MM06) 3. Standard Each vial contains 38 ng of recombinant Human Ficolin-1 / Ficolin-A / FCN1. Reconstitute with 1 mL detection antibody dilution buffer. After reconstitution, store at -20℃ to -80℃ in a manual defrost freezer. A seven-point standard curve using 2-fold serial dilutions in sample dilution buffer, and a high standard of 2000 pg/mL is recommended.
This ficolin 1/FCN1 Matched ELISA Antibody Pair Set,Human is a solid phase sandwich ELISA for quantitative determination of Human ficolin 1/FCN1 . It contains Human ficolin 1/FCN1 capture antibody, Human ficolin 1/FCN1 detector antibody
and a highly purified
recombinant Human ficolin 1/FCN1 protein. This Pair Set is at affordable price for researchers.
This Matched ELISA Antibody Pair Set is shipped at ambient temperature.
Capture Antibody: Aliquot and store at -20℃ to -80℃ for up to 6 months from date of receipt. Avoid repeated freeze-thaw cycles. Detection Antibody: Store at 4℃ and protect it from prolonged exposure to light for up to 6 months from date of receipt. DO NOT FREEZE! Standard: Store lyophilized standard at -20℃ to -80℃ for up to 6 months from date of receipt. Aliquot and store the reconstituted Standard at -80℃ for up to 1 month. Avoid repeated freeze-thaw cycles.
Ficolins are humoral molecules of the innate immune systems which recognize carbohydrate molecules on pathogens, apoptotic and necrotic cells. The Ficolin family of proteins are characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. Ficolins are humoral molecules of the innate immune systems which recognize carbohydrate molecules on pathogens, apoptotic and necrotic cells. Three Ficolins have been identified in humans: L-Ficolin, H-Ficolin and M-Ficolin (also referred to as Ficolin-2, -3 and -1, respectively). They are soluble oligomeric defence proteins with lectin-like activity and they are structurally similar to the human collectins, mannan-binding lectin (MBL) and surfactant protein A and D. Dysfunction or abnormal expressions of Ficolins may involved in the pathogenesis of human diseases including infectious and inflammatory diseases, autoimmune disease and clinical syndrome of preeclampsia. They are soluble oligomeric defence proteins with lectin-like activity and they are structurally similar to the human collectins, mannan-binding lectin (MBL) and surfactant protein A and D. Upon recognition of the infectious agent, the Ficolins act through two distinct routes: initiate the lectin pathway of complement activation through attached serine proteases (MASPs), and a primitive opsonophagocytosis thus limiting the infection and concurrently orchestrating the subsequent adaptive clonal immune response. Ficolin-1 (FCN1) is predominantly expressed in the peripheral blood leukocytes.
Thiel S. (2007) Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins. Mol Immunol. 44(16): 3875-88.
Zhang XL, et al. (2008) Ficolins: structure, function and associated diseases. Adv Exp Med Biol. 632: 105-15.
Garred P, et al. (2009) MBL2, FCN1, FCN2 and FCN3-The genes behind the initiation of the lectin pathway of complement. Mol Immunol. 46(14): 2737-44.
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