ELISA

Lipopolysaccharide binding protein is a protein that in humans is encoded by the LBP gene. This gene is mapped to 20q11.23. LBP is a soluble acute-phase protein that binds to bacterial lipopolysaccharide(or LPS) to elicit immune responses by presenting the LPS to important cell surface pattern recognition receptors called CD14 and TLR4. It is present in the cerebrospinal fluid of patients with pneumococcal meningitis. The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. LBP is made in the liver during the acute phase of infections and is thought to function as a carrier for LPS and to help control LPS-dependent monocyte responses.

Prostasin is a protein that in humans is encoded by the PRSS8 gene. It is a single-copy gene and mapped to 16p11.2. Prostasin is likely to be the more physiologically relevant protease. This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. Coexpression of Prostasin with either Xenopus or rat ENaC in Xenopus oocytes resulted in a 60% to 80% increase in amiloride-sensitive sodium currents, and that the addition of aprotinin, a serine protease inhibitor, completely prevented this activation. This enzyme is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine.

Prostasin is a protein that in humans is encoded by the PRSS8 gene. It is a single-copy gene and mapped to 16p11.2. Prostasin is likely to be the more physiologically relevant protease. This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. Coexpression of Prostasin with either Xenopus or rat ENaC in Xenopus oocytes resulted in a 60% to 80% increase in amiloride-sensitive sodium currents, and that the addition of aprotinin, a serine protease inhibitor, completely prevented this activation. This enzyme is highly expressed in prostate epithelia and is one of several proteolytic enzymes found in seminal fluid. The proprotein is cleaved to produce a light chain and a heavy chain which are associated by a disulfide bond. It is active on peptide linkages involving the carboxyl group of lysine or arginine.

Lipopolysaccharide binding protein is a protein that in humans is encoded by the LBP gene. This gene is mapped to 20q11.23. LBP is a soluble acute-phase protein that binds to bacterial lipopolysaccharide(or LPS) to elicit immune responses by presenting the LPS to important cell surface pattern recognition receptors called CD14 and TLR4. It is present in the cerebrospinal fluid of patients with pneumococcal meningitis. The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. LBP is made in the liver during the acute phase of infections and is thought to function as a carrier for LPS and to help control LPS-dependent monocyte responses.

Galectin-4, also known as LGALS4 or GAL4, is a protein that in humans is encoded by the LGALS4 gene. It is mapped to 19q13.2. Galectins are a family of animal lectins defined by an affinity for beta-galactoside-containing saccharides and by shared sequence elements. Galectin-4 is expressed as a 38-kD protein in the human colon adenocarcinoma T84 cell line. Galectin-4 is an S-type lectin that is strongly underexpressed in colorectal cancer, and this gene plays a role in cell adhesion. It has been found that decreased Galectin-4 expression occurs early in colorectal carcinogenesis.

DLL1(DELTA-LIKE 1), also known as DL1 or DELTA1, is a protein that in humans is encoded by the DLL1 gene. DLL1 is a human homolog of the Notch Delta ligand and is a member of the delta/serrate/jagged family. It plays a role in mediating cell fate decisions during hematopoiesis, and it is also important in cell-to-cell communication. This gene is mapped to chromosome 6q27, near a locus for type I diabetes. Functional analysis suggested that a soluble fusion protein containing the DSL domain of DLL1 and its adjacent 50 N-terminal amino acids increased the viability of hemopoietic cells but inhibited cell death. It has been found that DLL1 blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor.

Delta like ligand 4 is a protein that in humans is encoded by the DLL4 gene. It is mapped to 15q15.1. This gene is a homolog of the Drosophila delta gene. DLL4 is a transmembrane ligand for Notch receptors that shows restricted expression to endothelial cells (ECs), in particular to arteries and capillaries, and is involved in vascular development, and it also appeared to be a major trigger of Notch receptor activities previously implicated in arterial and vascular development. Mouse DLL4 could activate mouse Notch1 and mouse Notch4. DLL4 acts as a negative regulator of tumor angiogenesis, its blockade results in the striking uncoupling of tumor growth from vessel density, presenting a novel therapeutic approach even for tumors resistant to anti-VEGF therapies. In addition to it, this gene also plays an important role in promoting Th17 effector activity during mycobacterial challenge.

Galectin-2 is a protein that in humans is encoded by the LGALS2 gene. It is mapped to 22q13.1. The protein encoded by this gene is a soluble beta-galactoside binding lectin. The encoded protein is found as a homodimer and can bind to lymphotoxin-alpha. It has been found that a single-nucleotide polymorphism in Galectin-2 is significantly associated with susceptibility to myocardial infarction. This genetic substitution affects the transcriptional level of Galectin-2 in vitro, potentially leading to altered secretion of LTA, to which Galectin-2 binds, which would then affect the degree of inflammation.

Galectin-7, also known as GAL7, is a protein that in humans is encoded by the LGALS7 gene. This gene is mapped to 19q13.2. Galectins belong to a family of related beta-galactoside-binding lectins, also referred to as S-type or S-Lac lectins. Members of this family have been implicated in a variety of functions, including growth regulation, cell adhesion, migration, neoplastic transformation, and immune responses. Differential and in situ hybridizations indicate that this lectin is specifically expressed in keratinocytes. It has been found that expression of Galectin-7 was markedly upregulated in corneal epithelium after injury and that exogenous galectin-7 stimulated reepithelialization of corneal wounds.