mbl 2

Mannose-binding Lectin (MBL) is an acute phase protein bearing to the family of collectins produced by the liver as a monomer that forms a triple helix. Once released in serum, it further polymerizes forming dimers to octamers. The degree of serum polymerization is critical for the biological activity of MBL. MBL has higher affinity to microbial polysaccharides or their glycoconjugates. MBL was shown earlier to bind cell surfaces of bacteria, fungi, protozoa and viruses and acts as an acute-phase plasma protein (APP) during infection and inflammation. MBL activates the lectin-complement pathway, promotes opsonophagocytosis and modulates inflammation.

Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. MASP2 Protein, Rat, Recombinant (His) is expressed in Baculovirus insect cells with C-6xHis tag. The predicted molecular weight is 79.2 kDa and the accession number is Q9JJS8.

Mannan Binding Lectin/MBL2 Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with mFc tag. The predicted molecular weight is 50.6 kDa and the accession number is P41317.

Mannan Binding Lectin/MBL2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.3 kDa and the accession number is P41317.

Mannose-Binding Protein C (MBP-C) belongs to the Collectin family of innate immune defense proteins. MBL binds to an array of carbohydrate patterns on pathogen surfaces. Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an α-helical coiled-coil neck domain and a carboxy terminal C-type Lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associates into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins exist in rodents and other animals. Human MBL-2 is 25 kDa. Human MBL-2 is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region, a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates.

Mannan Binding Lectin/MBL2 Protein, Human, Recombinant is expressed in CHO mammalian cells. The predicted molecular weight is 24 kDa and the accession number is P11226.

Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. MBL2 Protein, Rat, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 30.0 kDa and the accession number is P08661.

The pathogenesis of severe acute respiratory disease syndrome (SARS) is not fully understood. One case-control study has reported an association between susceptibility to SARS and mannan-binding lectin (MBL) in China. As the downstream protein of MBL, variants of the MBL-associated serine protease-2 (MASP2) gene may be associated with SARS coronavirus (SARS-CoV) infection in the same population.

Glycosyl transferase 25 domain 2 (GLT25D2) is a glucosyltransferase enzyme expressed only at low levels in the nervous system. Glycosyltransferases are enzymes that act as a catalyst for the transfer of a monosaccharide unit from an activated nucleotide sugar (also known as the glycosyl donor ) to a glycosyl acceptor molecule, usually an alcohol. Glycosyl transferases transfer glycosyl groups onto their substrate. Localization partially defines their function. Glt25D2 enzyme showed a strong galactosyltransferase activity toward various types of collagen and toward the serum mannose-binding lectin MBL which contains a collagen domain.