Cleaved-MASP-1 HC (R448) polyclonal antibody, anti-human

Background:
MASP1 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 (mannan binding lectin serine peptidase 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. Mannan binding lectin serine peptidase 1 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. Mannan binding lectin serine peptidase 1 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.

Research Area: Others

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

Immunogen: The antiserum was produced against synthesized peptide derived from human AMPK alpha around the phosphorylation site of Thr172. AA range:140-189

Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Formulation: Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Concentration: 1 mg/ml

Storage:
-20°C for 1 year