carbohydrate

Galectin-8 LGALS8 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 62.8 kDa and the accession number is O00214.

Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis.

CHST5 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 70.1 kDa and the accession number is Q9QUP4.

Sedoheptulokinase (SHPK) belongs to the FGGY kinase family, and is mainly located in cytoplasm. SHPK is strongly expressed in liver, kidney and pancreas. It is expressed at lower levels in placenta and heart, and very weakly expressed in lung and brain. SHPK catalyzes the chemical reaction: ATP + sedoheptulose = ADP + sedoheptulose 7-phosphatecan, It can transform sedoheptulose to sedoheptulose 7-phosphate in the condition of ATP, and acts as a modulator of macrophage activation through control of glucose metabolism. In addition, It also can be down-regulated by LPS.

CHST9 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 17.66 kDa and the accession number is NP_113610.2.

ANXA4 Protein, Human, Recombinant (His & Myc & SUMO) is expressed in E. coli.

Carbohydrate sulfotransferase 15, also known as N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase, GalNAc4S-6ST, B-cell RAG-associated gene protein, CHST15 and BRAG, is a single-pass type II membrane protein which belongs to thesulfotransferase 1 family. CHST15 BRAG is expressed in B-cell-enriched tissues but not in fetal or adult thymus. It is expressed in fetal and adult spleen, lymph node, tonsil, bone marrow and peripheral leukocytes. It is not expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it colocalizes with RAG1. CHST15 BRAG is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO4) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. CHST15 BRAG may also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and or regulation of B-cell-specific RAG expression.

CHST11, also known as C4ST-1, belongs to the sulfotransferase 2 family. CHST11 localizes to the golgi membrane, and catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage, and is distributed on the surfaces of many cells and extracellular matrices. A chromosomal translocation involving CHST11 gene and IgH, t(12;14)(q23;q32), has been reported in a patient with B-cell chronic lymphocytic leukemia.

The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

Calcium phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. ANXA4 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 40.8 kDa and the accession number is P97429.

Galectin-3(LGALS3) is also known as Galactose-specific lectin 3, Mac-2 antigen, Carbohydrate-binding protein 35, Laminin-binding protein and Galactoside-binding protein. LGALS3 is highly expressed in early stages of papillary carcinoma, and lowly during tumor progression. LGALS3 is probably forms homo- or heterodimers and secreted by a non-classical secretory pathway and associates with the cell surface. LGALS3 plays an important role during the acquisition of vasculogenic mimicry and angiogenic properties. LGLAS3 takes part in an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.

Carbohydrate sulfotransferase 3, also known as Chondroitin 6-O-sulfotransferase 1, Chondroitin 6-sulfotransferase and CHST3, is a single-pass type II membrane protein which belongs to thesulfotransferase 1 family and Gal GlcNAc GalNAc subfamily. CHST3 is widely expressed in adult tissues. It is expressed in heart, placenta, skeletal muscle and pancreas. CHST3 is also expressed in various immune tissues such as spleen, lymph node, thymus and appendix. CHST3 catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. It is a chondroitin sulfate which constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. It can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. It may play a role in the maintenance of naive T-lymphocytes in the spleen. Defects in CHST3 are the cause of spondyloepiphyseal dysplasia Omani type (SED Omani type) which is an autosomal recessive disorder characterized by normal length at birth but severely reduced adult height (11-13 cm), severe progressive kyphoscoliosis, arthritic changes with joint dislocations, genu valgum, cubitus valgus, mild brachydactyly, camptodactyly, microdontia and normal intelligence. As a consequence of the arthropathy and the contractures, affected individuals develop restricted joint movement. Defects in CHST3 are also a cause of humerospinal dysostosis (HSD) which is characterized by bifurcation of the ends of the humerus, subluxation in the elbow joints, widened iliac bones, talipes equinovarus and coronal cleft vertebrae. Congenital, progressive heart disease, possibly with fatal outcome, is observed in some patients.

The Galectin family of proteins, with specificity for Nacetyllactosamine containing glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs).They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide; they can be secreted by one or more as yet unidentified non-classical secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications.

Ketohexokinase, also known as Hepatic fructokinase, is a member of the carbohydrate kinase PfkB family. It exits as a homodimer and most abundant in liver, kidney, gut, spleen and pancreas. Low levels also found in adrenal, muscle, brain and eye.This enzyme catalyzes conversion of fructose to fructose-1-phosphate. It is the first enzyme with a specialized pathway that catabolizes dietary fructose. Defects in KHK are the cause of fructosuria.

Microfibril-associated glycoprotein 4(MFAP4) is a secreted protein and contains 1 fibrinogen C-terminal domain, similarity to a bovine microfibril-associated protein. The protein has binding specificities for both collagen and carbohydrate. It is thought to be an extracellular matrix protein which is involved in calcium-dependent cell adhesion or intercellular interactions. The gene is located within the Smith-Magenis syndrome region.

Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Siglec-8 is expressed on eosinophils, basophils, and mast cells, and it shows a binding preference for the carbohydrate 6-O sulfated sLex. At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 115 aa cytoplasmic domain with two tyrosine based signaling motifs. Alternative splicing generates additional isoforms that either lack most of the second Ig-like domain or have a substituted cytoplasmic domain without the signaling motifs. Cross-linking of Siglec-8 inhibits Fc epsilon RI alpha induced mast cell degranulation. It also induces eosinophil apoptosis, an effect which is enhanced by the eosinophil-activating cytokines IL-5, IL-33, and GM-CSF.

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).

NKG2D is a type II transmembrane glycoprotein having an extracellular lectin-like domain. This domain lacks the recognizable calcium-binding sites found in true C-type lectins and binds protein rather than carbohydrate ligands. Human NKG2D is expressed on CD8 alpha beta T cells, gamma δ T cells, NK cells and NKT cells. NKG2D CD314 Protein, Human, Recombinant (hFc & Flag) is expressed in HEK293 mammalian cells with N-hFc-Flag tag. The predicted molecular weight is 43.4 kDa and the accession number is P26718.

Galectin-3, also known as Mac-2, L29, CBP35, and epsilon BP, is classified as a chimeric member of the Galectin superfamily and contains one carbohydrate recognition domain (CRD) linked to a nonlectin domain.Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity).

Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. That protein has no CMP-N-acetylneuraminate monooxygenase activity and is not able to convert CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells in vertebrates. However, it may play a role in Wnt signaling.

Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 77.7 kDa and the accession number is Q9BTY2.

Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway. REG3A Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 43.6 kDa and the accession number is Q06141.

Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. ASGR2 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 29.9 kDa and the accession number is P24721.

Catalyzes the transfer of CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1. Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity. May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes. Could be involved in brain development (Probable).

Phosphomannomutase 2, also known as PMM2 and CDG1, belongs to the eukaryotic PMM family. Phosphomannomutase 2 catalyzes the isomerization of mannose 6-phosphate to mannose 1-phosphate. Mannose 1-phosphate is a precursor to GDP-mannose necessary for the synthesis of dolichol-P-oligosaccharides. GDP-mannose can transfer its small sugar molecule called mannose to the growing oligosaccharide chain. Once the correct number of small sugar molecules are linked together to form the oligosaccharide, it can be attached to a protein. Phosphomannomutase 2 is also required for a number of critical mannosyl transfer reactions. Mutations in PMM2 gene have been shown to cause defects in the protein glycosylation pathway manifest as carbohydrate-deficient glycoprotein syndrome type I.

NAGA (Alpha-N-Acetylgalactosaminidase) is a Protein Coding gene. NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. It belongs to the glycosyl hydrolase 27 family. The antinociceptive effect of NAGA may involve the participation of endogenous opioid peptides and endogenous catecholamines. Normal alpha-NAGA is synthesized as a 52 kDa precursor which matures to a 49 kDa species through phosphorylation and carbohydrate trimming. Mutations in gene encoding alpha-NAGA cause a wide range of diseases, characterized by mild to severe clinical features. NAGA is widely expressed in the placenta, appendix, and other tissues. Diseases associated with NAGA include Kanzaki Disease and Schindler Disease, Type I.

B3GAT1 is the key enzyme during the biosynthesis of the carbohydrate epitope HNK-1, which is present on a number of cell adhesion molecules important in neurodevelopment. It adds a glucuronic residue to the terminal lactosamine residue (Gal beta 14GlcNAc) of a glycoprotein or glycolipid, which can be further sulfated to become the HNK1 epitope, a unique trisaccharide structure, HSO3-3GlcA beta 1-3Gal beta 1-4GlcNAc. The enzyme activity was found to be enhanced in the presence of sphingomyelin and phosphatidylinositol. The HNK1 carbohydrate epitope is characteristically expressed on a series of cell adhesion molecules in addition to some glycolipids in the extracellular matrix and on the cell surface in the nervous system, where it is involved in cell-cell and cell-substratum interaction and recognition during the development of the nervous system. Like most known glycosyltransferases, B3GAT1 is a type II Golgi-resident transmembrane protein with a short N-terminal cytoplasmic domain and a single pass transmembrane domain followed by an enzymatic domain in the lumen of Golgi apparatus. The enzyme activity was assayed using a phosphatase-coupled method.

Bone sialoprotein 2(IBSP) is a monomeric non‑collagenous member of the SIBLING family of extracellular matrix proteins. It is principally associated with the early stages of bone mineralization. Mouse IBSP is synthesized as a 324 amino acid (aa) precursor that contains a 16 aa signal sequence and a 308 aa mature region. The mature segment is divided into a basic N‑terminus (aa 17 ‑ 62), a central region (aa 63 ‑ 233), and an acidic C‑terminus (aa 234 ‑ 317). IBSP is highly glycosylated, sulfated and phosphorylated. Phosphorylation promotes HAp nucleation, while carbohydrate may regulate cell adhesion. IBSP binds tightly to hydroxyapatite, appears to form an integral part of the mineralized matrix. It is probably important to cell-matrix interaction and promotes Arg-Gly-Asp-dependent cell attachment.

Galectin-14 is a member of the Galectin family of carbohydrate binding proteins. The members of Galectin family contain one or two carbohydrate recognition domains, which can bind β-Galactoside. LGALS14 is expressed intracellularly in placenta and eosinophils, and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation. Two alternatively spliced transcript variants encoding distinct isoforms have been observed.

Surfactant Pulmonary-Associated Protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that places it in a subset of pattern recognition proteins termed defense collagens. SP-D is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures and induced in cardiac smooth muscle and endothelial cells. It binds both secreted and transmembrane proteins that transduce its function. It binds human neutrophil defensins, modulating influenza anti-viral defense. It binds MD-2 LY96, a secreted protein that cooperates with Toll-like receptors (TLRs) in the response of macrophages to bacterial lipopolysaccharides (LPS) or cell wall components. It also binds macrophage CD14 and TLRs directly, blocking binding of LPS and down-regulating TNF-α secretion. SP-D binding of both SIRPα and the calreticulin CD91 complex on macrophages allows for a graded response to environmental challenge.

Fructose-1,6-bisphosphatase 1(FBP1) is a homotetramer protein and belongs to the FBPase class 1 family. It involves in carbohydrate biosynthesis; gluconeogenesis pathway. FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

Beta-1,4-galactosyltransferase 3 (B4GALT3) belongs to the glycosyltransferase 7 family. It is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. It is highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.

NKG2D is a type II transmembrane glycoprotein having an extracellular lectin-like domain. This domain lacks the recognizable calcium-binding sites found in true C-type lectins and binds protein rather than carbohydrate ligands. Human NKG2D is expressed on CD8 alpha beta T cells, gamma δ T cells, NK cells and NKT cells. NKG2D CD314 Protein, Human, Recombinant (hFc & Flag), FITC-Labeled is expressed in HEK293 mammalian cells with N-hFc-Flag tag. The predicted molecular weight is 43.4 kDa and the accession number is P26718.

Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate. Can also utilize propionate with a much lower affinity. Provides acetyl-CoA that is utilized mainly for oxidation under ketogenic conditions. Involved in thermogenesis under ketogenic conditions, using acetate as a vital fuel when carbohydrate availability is insufficient. ACSS1 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 75.1 kDa and the accession number is Q9NUB1.

Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc. ST3GAL3 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 54.9 kDa and the accession number is Q11203.

Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.

Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. ASGR1 Protein, Rat, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 31 kDa and the accession number is P02706.

INS (Insulin) is a Protein Coding gene. This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. The binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Diseases associated with INS include Hyperproinsulinemia and Maturity-Onset Diabetes Of The Young, Type 10. A multitude of mutant alleles with phenotypic effects has been identified, including insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10, and hyperproinsulinemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

GPD1 (Glycerol-3-Phosphate Dehydrogenase 1) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. GPD1 is a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. The encoded protein plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of dihydroxyacetone phosphate (DHAP) and reduced nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. It also reduces nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. Meanwhile, GPD1 and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria. Diseases associated with GPD1 include Hypertriglyceridemia, Transient Infantile, and Myopathy, Distal, 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.

Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes, endosomes, and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers, as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.

NKG2D is a type II transmembrane glycoprotein having an extracellular lectin-like domain. This domain lacks the recognizable calcium-binding sites found in true C-type lectins and binds protein rather than carbohydrate ligands. Human NKG2D is expressed on CD8 alpha beta T cells, gamma δ T cells, NK cells and NKT cells. NKG2D CD314 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with N-His-Avi tag. The predicted molecular weight is 19.0 kDa and the accession number is P26718.

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.

Galectins are a family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. Galectin-4 is a 36 kDa tandem-repeat galectin found throughout the gastrointestinal tract, but also present in well-differentiated breast and liver carcinomas. Galectin-4 expression is concentrated within microvilli in the gastrointestinal epithelium, where it can interact with CD3 and bind activated T cells in the lamina propria during intestinal inflammation.

Recombinant Murine TFF-2 is an 11.9 kDa polypeptide of 106 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds. The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma. It inhibits gastrointestinal motility and gastric acid secretion. As a structural component of gastric mucus, it possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains.

Human Galectin-3, also known as Mac-2, L29, CBP35, and epsilon BP, is classified as a chimeric member of the Galectin superfamily and contains one carbohydrate recognition domain (CRD) linked to a nonlectin domain.Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity).

Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.

Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA1 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 66.6 kDa and the accession number is Q99LJ1.