Protein Tag: C-His
Uniprot: P11226
Accession: P11226
Background: 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.
Bio Acitivity: Not validated for activity
Sequence: Glu21-Ile248
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 5% Threhalose, pH 7.2.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 25.1 kDa
Observed MW: 31 kDa
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