Human Ficolin-1 / Ficolin-A / FCN1 Protein (His Tag)
FCN1,FCNM
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| Catalog Number | P10930-H08H |
|---|---|
| Organism Species | Human |
| Host | Human Cells |
| Synonyms | FCN1,FCNM |
| Molecular Weight | The secreted recombinant human FCN1 comprises 308 amino acids with a predicted molecular mass of 33.6 kDa as estimated in SDS-PAGE under reducing conditions. |
| predicted N | Ala 30 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the human FCN1 (NP_001994.2) precursor (Met 1-Ala 326) was expressed with a C-terminal polyhistidine tag. |
| Bio-activity | Measured by its binding ability in a functional ELISA. 1. Immobilized FCN1 at 10 μg/ml can bind biotinylated recombinant human Fetuin-A with a linear range of 16-2000 ng/ml. 2. Immobilized FCN1 at 10 μg/ml can bind biotinylated recombinant mouse Fetuin-A with a linear range of 16-2000 ng/ml. |
| Research Area | Immunology |Signal Transduction |Cytoskeleton / ECM |Cell Adhesion |Lectin |C-tyep lectin | |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | 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. |
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