Rhesus FCN1/FCNA (Fc Tag) recombinant protein

Rhesus FCN1/FCNA (Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

RP23-464C2.11; FCN1; FCNA; FICOLIN A; FCNM; FICOLIN 1

F7BW36

Human Cells

A DNA sequence encoding the rhesus FCN1 (XP_001098002.1) (Met1-Ala326) was expressed with the Fc region of human IgG1 at the C-terminus.

Rhesus

The recombinant rhesus FCN1 consists of 538 amino acids and predicts a molecular mass of 59.1 kDa.

> 90 % as determined by SDS-PAGE.