Description
MASP1 Antibody | 19-799 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 20-300 of human MASP1 (NP_001870.3) .
Research Area: Immunology, Innate Immunity
Tested Application: WB
Application: WB: 1:500 - 1:2000
Specificiy: N/A
Positive Control 1: HeLa
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: Observed: 60kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: Mannan-binding lectin serine protease 1, 3421-, Complement factor MASP-3, Complement-activating component of Ra-reactive factor, Mannose-binding lectin-associated serine protease 1, MASP-1, Mannose-binding protein-associated serine protease, Ra-reactive factor serine protease p100, RaRF, Serine protease 5, Mannan-binding lectin serine protease 1 heavy chain, Mannan-binding lectin serine protease 1 light chain, MASP1, CRARF, CRARF1, PRSS5
User Note: Optimal dilutions for each application to be determined by the researcher.
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.