| Product Name | Cleaved-MASP-1 HC (R448) Polyclonal Antibody |
|---|---|
| Description | This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants. |
| Synonyms | MASP1; CRARF; CRARF1; PRSS5; Mannan-binding lectin serine protease 1; Complement factor MASP-3; Complement-activating component of Ra-reactive factor; Mannose-binding lectin-associated serine protease 1; MASP-1; Mannose-binding protein-asso |
| Host | Rabbit |
| Immunogen | Synthesized peptide derived from the Internal region of human MASP-1 HC |
| Isotype | IgG |
| Reactivity | Human |
| Applications | ELISA, WB |
| Form | PBS with 0.02% sodium azide,0.5% BSA and 50% glycerol pH 7.4. |
| Uniprot | P48740 |
| Background | This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants. |
| Supplier | Elabscience |
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