| Reactivity | MuSpecies Glossary |
| Applications | Binding Activity |
| Details of Functionality | Measured by its ability to bind with Mannan in a functional ELISA. |
| Source | Mouse myeloma cell line, NS0-derived mouse MBL-2 protein Glu19-Asp244 |
| Accession # | |
| N-terminal Sequence | Glu19 |
| Structure / Form | Oligomer |
| Protein/Peptide Type | Recombinant Proteins |
| Gene | Mbl2 |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 24 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
|
| SDS-PAGE | 30 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Mannan binding lectin (MBL) belongs to the collectin family of innate immune defense proteins, which binds to an array of carbohydrate patterns on pathogen surfaces (1, 2). Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an alpha -helical coiled-coil neck domain and a carboxy terminal C-type (Ca++-dependent) lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined byN-terminal disulfide bridges. These homotrimers further associates into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins (MBL-1, also known as S-MBP or MBL-A and MBL-2, also known as L-MBP or MBL-C) exist in rodents and other animals, only one functional MBL protein is present in humans. Mouse MBL-2 shares about 52% and 60% amino acid sequence identity with mouse MBL-1 and human MBL, respectively.
In mouse, MBL-1 and MBL-2 are the only collectins that can activate complement via the lectin complement pathway (1, 2). Serum oligomeric MBL associates with MBL-associated serine protease (MASP) proenzymes. The MBL-MASP proenzyme complex preferentially interact with sugar patterns containing mannose, glucose, L-fucose, or N-acetyl-glucosamine present at a terminal nonreducing postion on the cell surface of various pathogens and certain tumor cells. This interaction induces pro-enzyme activation and the triggering of the complement cascade, resulting in opsonization and pathogen removal via humoral and cellular immune responses. MBL does not recognize self-components or glycoproteins from other higher animals due to the presence of terminal sialic acid or galactose that interrupts the repeating carbohydrate structures (3). A number of membrane receptors for MBL, including C1q phagocytic receptor (C1qRp), calreticulin (also known as C1qR), and CR1 (CD35), have been described. Interactions with these receptors may also be important in stimulating phagocytosis (1, 2).
Mouse MBL-1 and MBL-2 are produced primarily in the liver and are secreted into the blood stream. In addition, mouse MBL-1 is also expressed in lung, kidney and testis while MBL-2 is expressed in kidney, thymus and small intestine (1, 4, 5).
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