Rabbit anti-Human MASP1 Polyclonal Antibody

Uniprot Id

P48740

Target Species

Human

Target Name

MASP1

Target Full Name

Mannan-binding lectin serine protease 1

Target Function

Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.

Target Involvement

3MC syndrome 1 (3MC1)

Target Subcellular Location

Secreted.

Target Protein Families

Peptidase S1 family

Target Tissue Specificity

Protein of the plasma which is primarily expressed by liver.

Target Research Area

Immunology

Target Synonyms

MASP1; CRARF; CRARF1; PRSS5Mannan-binding lectin serine protease 1; EC 3.4.21.-; 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) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]

Target 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.