Mannan-Binding Lectin Serine Protease 1 (MAPS-1) expressed in E. Coli.
MASP-1 is 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. MASP-1 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. MASP-1 is also able to cleave fibrinogen and factor XIII and may be involved in coagulation.
From the laboratory of Lakshmi C. Wijeyewickrema, PhD, La Trobe University.
Product Type: | Protein |
Name: | MASP1CCP12SP Enzyme |
Accession ID: | P48740 |
Source: | Escherichia coli |
Molecular Weight: | 45072.58 (Predicted), around 16kDa and 28kDa on SDS-PAGE under reducing condition |
Amino Acid Sequence: | G298-N699 |
Purity: | >95%, by SDS-PAGE under reducing conditions and visualized by Coomassie Blue Stain |
Buffer: | 20 mM Tris, 150mM Nacl, pH7.5 |
Storage: | -80C |
Shipped: | Dry Ice |
If you publish research with this product, please let us know so we can cite your paper.