ELISA

Tetranectin, also called TNA, is a protein that in humans is encoded by the CLEC3B gene. It is mapped to 3p21.31. Tetranectin, a tetrameric protein isolated from human plasma, has 4 identical and noncovalently bound polypeptide chains, each of 181 amino acid residues. It has a specific binding affinity for sulfated polysaccharides and the kringle 4 of plasminogen. The plasma concentration of tetranectin is reduced in patients with various malignancies. Tetranectin is a plasminogen-binding protein that is induced during the mineralization phase of osteogenesis. Thus, tetranectin is a candidate gene for human disorders affecting bone and connective tissue.

Thioredoxin is a class of small redox proteins known to be present in all organisms. It is mapped to 9q31.3. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. They can also act as electron donors to peroxidases and ribonucleotide reductase. Thioredoxin is a 12-kD oxidoreductase enzyme containing a dithiol-disulfide active site. It plays a role in many important biological processes, including redox signaling. This gene also plays a central role in humans and is increasingly linked to medicine through their response to reactive oxygen species (ROS). VDUP1 is a key stress-responsive inhibitor of Thioredoxin activity in cardiomyocytes.

CD320(cluster of differentiation 320), also known as 8D6A or TCBLR, is a human gene. It is mapped to chromosome 19p13.2. This gene encodes the transcobalamin receptor that is expressed at the cell surface. It mediates the cellular uptake of transcobalamin bound cobalamin(vitamin B12), and the expression of CD320 enhanced B-cell proliferation and immunoglobulin secretion. Mutations in this gene are associated with methylmalonic aciduria. It has been found that antagonists of the CD320 signaling pathway may counter the growth of follicular lymphomas or other tumors that metastasize to lymphoid follicles. CD320 is also a specific receptor for uptake of TCN2-bound cobalamin.

Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene. It is mapped to 9q34.3. The ficolin family of proteins are characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. Ficolins have a crucial role in defense against pneumococcal infection through the lectin complement pathway. Ficolin 1 is predominantly expressed in the peripheral blood leukocytes, and has been postulated to function as a plasma protein with elastin-binding activity.

Ficolin-2, which was initially identified as L-ficolin, is a protein that in humans is encoded by the FCN2 gene. The product of this gene belongs to the ficolin family of proteins. This family is characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. It is mapped to 9q34.3. This gene is predominantly expressed in the liver, and has been shown to have carbohydrate binding and opsonic activities. Serum concentration of ficolin-2 varies considerably in healthy individuals. FCN2 promoter polymorphisms were associated with marked changes in theficolin-2 serum concentration.

Ficolin-3, also known as HAKA1, is a protein that in humans is encoded by the FCN3 gene. It is mapped to 1p36.11. The protein can activate the complement pathway in association with MASPs and sMAP, thereby aiding in host defense through the activation of the lectin pathway. Ficolin-3 is expressed as a 35-kD protein that reacts with systemic lupus erythematosus sera. Ficolin-3 does not bind fibronectin(FN1), elastin(ELN), or zymosan, and the lectin activity of the Ficolin-3 is calcium independent. Homozygosity for the variant in the FCN3 gene results in a recessive complement deficiency syndrome.

The interleukin-18 receptor 1(IL-18R1), also known as CDw218a(cluster of differentiation w218a) or IL18RA, is an interleukin receptor of the immunoglobulin superfamily. The protein encoded by this gene is a cytokine receptor that belongs to the interleukin 1 receptor family. This gene along with four other members of the interleukin 1 receptor family, including IL1R2, IL1R1, ILRL2(IL-1Rrp2), and IL1RL1(T1/ST2), form a gene cluster on chromosome 2q. This receptor specifically binds interleukin 18(IL18), and is essential for IL18 mediated signal transduction. IFN-alpha and IL12 are reported to induce the expression of this receptor in NK and T cells.

Lumican, also known as LUM, is a protein which in humans is encoded by the LUM gene. This gene is a member of the small interstitial proteoglycan gene(SIPG) family, and it is a keratan sulfate proteoglycan which presents large quantities in the corneal stroma and in interstitial collagenous matrices of the heart, aorta, skeletal muscle, skin, and intervertebral discs. Lumican is mapped to 12q21.33, it interacts with collagen and limits growth of fibrils in diameter. In the cornea, Lumican not only interacts with collagen molecules to limit fibril growth, but also plays a critical role in the regular spacing of fibrils and acquisition of corneal transparency by virtue of its keratan sulfate-containing glycosaminoglycan side chains LDC.

Lumican, also known as LUM, is a protein which in humans is encoded by the LUM gene. This gene is a member of the small interstitial proteoglycan gene(SIPG) family, and it is a keratan sulfate proteoglycan which presents large quantities in the corneal stroma and in interstitial collagenous matrices of the heart, aorta, skeletal muscle, skin, and intervertebral discs. Lumican is mapped to 12q21.33, it interacts with collagen and limits growth of fibrils in diameter. In the cornea, Lumican not only interacts with collagen molecules to limit fibril growth, but also plays a critical role in the regular spacing of fibrils and acquisition of corneal transparency by virtue of its keratan sulfate-containing glycosaminoglycan side chains LDC.