MBL2/COLEC1 Protein, Mouse (HEK293, Fc)

MBL2/COLEC1 Protein, a calcium-dependent lectin, binds to mannose, fucose, and N-acetylglucosamine on microorganisms, activating the lectin complement pathway. It also binds to late apoptotic cells, apoptotic blebs, and necrotic cells, aiding their uptake by macrophages. MBL2 forms an oligomeric complex with homotrimers and interacts with MASP1, MASP2, MEP1A, and MEP1B. It plays a crucial role in immune defense, targeting microbial invaders and clearing apoptotic and necrotic cells. MBL2/COLEC1 Protein, Mouse (HEK293, Fc) is the recombinant mouse-derived MBL2/COLEC1 protein, expressed by HEK293 , with N-mFc labeled tag. The total length of MBL2/COLEC1 Protein, Mouse (HEK293, Fc) is 226 a.a., with molecular weight of ~50.6 KDa.

MBL2 (mannose-binding lectin 2), also known as COLEC1, is a calcium-dependent lectin that plays a crucial role in innate immune defense. This protein binds to mannose, fucose, and N-acetylglucosamine on various microorganisms, thereby activating the lectin complement pathway. Additionally, MBL2 binds to late apoptotic cells, apoptotic blebs, and necrotic cells, facilitating their uptake by macrophages. The protein forms an oligomeric complex composed of three or more homotrimers and interacts with MASP1 and MASP2. Furthermore, MBL2 interacts with MEP1A and MEP1B, potentially inhibiting their catalytic activity. Overall, MBL2 emerges as a key player in the immune response, recognizing and targeting microbial invaders while contributing to the clearance of apoptotic and necrotic cells.

Mouse

HEK293

N-mFc

P41317 (E19-D244)

17195  [NCBI]

Approximately 50.6 kDa.

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.