mannose binding lectin

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.

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.

LMAN2 (Lectin, Mannose Binding 2, also known as VIP36) is a Protein Coding gene. This gene encodes a type I transmembrane lectin that shuttles between the endoplasmic reticulum, the Golgi apparatus, and the plasma membrane. The encoded protein binds high mannose type glycoproteins and may facilitate their sorting, trafficking, and quality control. The L-type lectin LMAN2 appears to be specifically required for the accumulation of GPRC5B in the Golgi complex and restriction of GPRC5B transport along the exosomal pathway. This may occur due to interference with the adaptor protein GGA1-mediated trans-Golgi network-to-endosome transport of GPRC5B. A Golgi-traversing pathway for the exosomal release of the cargo protein GPRC5B in which CD2AP facilitates the entry and LMAN2 impedes the exit of the flux, respectively.

LMAN2L Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 56.9 kDa and the accession number is Q9H0V9-1.

MASP1 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 93.0 kDa and the accession number is P48740.

MASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF.

MBL1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 25.8 kDa and the accession number is P39039-1.

MBL1 Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 50.5 kDa and the accession number is P19999.

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.

LMAN2L Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 31.4 kDa and the accession number is Q9H0V9-1.

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.

Chitin-binding lectin which is specific for N-acetylglucosamine oligomers. Chitin-binding lectin Protein, Viscum album, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 11.4 kDa and the accession number is P81859.

Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N-acetylglucosamine.

Mannose-binding lectin. Cyanovirin-N Protein, Nostoc ellipsosporum, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 15.0 kDa and the accession number is P81180.

Collectin-11 is a secreted protein that belongs to the COLEC10/COLEC11 family. Collectin-11 contains one C-type lectin domain and one collagen-like domain. Collectins play important roles in the innate immune system by binding to carbohydrate antigens on microorganisms, facilitating their recognition and removal. Collectin-11 binds to various sugars including fucose and mannose, but does not bind to glucose, N-acetylglucosamine and N-acetylgalactosamine. It has a higher affinity for fucose compared to mannose. Collectin-11 binds lipopolysaccharides (LPS). It also involved in fundamental development serving as a guidance cue for neural crest cell migration. Defects in Collectin-11 are the cause of 3MC syndrome type 2 (3MC2).

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.

Langerin (CD207) is a type II transmembrane glycoprotein which is member K of the C-type lectin domain family. Langerin is used as a marker for Langerhans cells (LCs) which represent the immature dendritic cells in the epidermis. Langerin is necessary and sufficient for Birbeck granule formation. Human langerin sequence contains a 43 aa cytoplasmic domain, a 21 aa transmembrane domain and a 264 aa extracellular domain (ECD) that contains a coiled-coil domain and a single C-type lectin domain. Human langerin shares 68%, 62%, 71% aa identity with mouse, rat and bovine langerin ECD, respectively. Trimerization greatly increases the lectin binding affinity. Langerin internalizes endogenous proteins such as type I procollagen. Internalization by LC is thought to lead to suppression of self reactions. Langerin also mediates endocytosis of non-peptide antigens containing mannose, N-acetyl glucosamine and fucose that are expressed by mycobacteria and fungae.

Mannose-binding lectin. Cyanovirin-N homolog Protein, Ceratopteris richardii, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 14.4 kDa and the accession number is P86326.

Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N-acetylglucosamine.

Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells.

Mannose-binding lectin.