ELISA Kits

Adiponectin(ADPN) is a hormone secreted by adipocytes that regulates energy homeostasis and glucose and lipid metabolism. Adiponectin is a new member of the family of soluble defense collagens, in hematopoiesis and immune responses. It is an important negative regulator in hematopoiesis and immune systems and raise the possibility that it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin is mapped to 3q27 and can protect the organism from systemic inflammation by promoting the clearance of early apoptotic cells by macrophages through a receptor-dependent pathway involving calreticulin. The standard product used in this kit is the product of gene recombination, consisting of 226(19-244) amino acids with the molecular mass of 36KDa after glycosylation.

Adiponectin(ADPN) is a hormone secreted by adipocytes that regulates energy homeostasis and glucose and lipid metabolism. Adiponectin is a new member of the family of soluble defense collagens, in hematopoiesis and immune responses. It is an important negative regulator in hematopoiesis and immune systems and raise the possibility that it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin is mapped to 3q27 and can protect the organism from systemic inflammation by promoting the clearance of early apoptotic cells by macrophages through a receptor-dependent pathway involving calreticulin.

Interleukin-20(IL-20) is a protein belonging to the IL-10 family of cytokines. IL-20 is produced by activated keratinocytes and monocytes and transmits an intracellular signal through two distinct cell-surface receptor complexes on keratinocytes and other epithelial cells. By radiation hybrid analysis, the IL20 gene was mapped to chromosome 1q32, where it is tightly linked to the IL10, IL19, and MDA7 genes within a 195-kb region, the IL10 family cytokine cluster. IL-20 regulates proliferation and differentiation of keratinocytes during inflammation, particularly inflammation associated with the skin. In addition, IL-20 also causes cell expansion of multipotential hematopoietic progenitor cells.

Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2(MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases(MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide(cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The sta

Survivin(also termed API4) belongs to the family of genes known as inhibitors of apoptosis, and it has been implicated in both prevention of cell death and control of mitosis. Survivin is prominently expressed in transformed cell lines and in all the most common human cancers of lung, colon, pancreas, prostate and breast in vivo. It is also found in approximately 50% of high-grade non-Hodgkin's lymphomas. Survivin encodes a deduced 142-amino acid protein and localizes on chromosome 17q25. The overexpression of it in cancer may overcome an apoptotic checkpoint and favour aberrant progression of transformed cells through mitosis. The standard product used in this kit is recombinant human Survivin with the molecular mass of 34 KDa.

Thrombospondin-2(TSP-2) is a protein that in humans is encoded by the THBS2 gene. And this gene is mapped to 6q27. The protein encoded by this gene belongs to the thrombospondin family. It is a disulfide-linked homotrimeric glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein has been shown to function as a potent inhibitor of tumor growth and angiogenesis. Studies of the mouse counterpart suggest that this protein may modulate the cell surface properties of mesenchymal cells and be involved in cell adhesion and migration. TSP-2 has been shown to interact with MMP2.

CD105, also called Endoglin, is a homodimeric membrane glycoprotein primarily associated with human vascular endothelium. It is also found on bone marrow proerythroblasts, activated monocytes, and lymphoblasts in childhood leukemia. Endoglin is a component of the transforming growth factor-beta(TGFB) receptor complex and binds TGFB1 with high affinity.1 CD105 gene is mapped to 9q34.1. The coding region of the gene contains 14 exons.2 The protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development. Furthermore, it also has a role in the balance of ALK1 and ALK5 signaling to regulate endothelial cell proliferation.3 Moreover, the elevated expression of endoglin in the surgically excised CNVMs suggested a persisting postmitotic activation in an advanced stage of neovascular tissue.4 The standard product used in this kit is extracellular

A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene. ADAM8 is localized to chromosome 10q26.3. This gene encodes a member of the ADAM (a disintegrin and metalloproteinase domain) family. Members of the ADAM family, such as ADAM8, are cell surface proteases involved in remodeling of extracellular matrix, cell migration, and processing of membrane-bound signaling molecules. They are characterized by disintegrin and metalloprotease domains that confer adhesive properties and proteolytic activities, respectively. And the protein encoded by this gene may be involved in cell adhesion during neurodegeneration.

Alpha-fetoprotein (AFP, α-fetoprotein; also sometimes called alpha-1-fetoprotein, alpha-fetoglobulin, or alpha fetal protein) is a protein that in humans is encoded by the AFP gene. The AFP gene is located on the q arm of chromosome 4 (4q25). AFP is the most abundant plasma protein found in the human fetus. Plasma levels decrease rapidly after birth but begin decreasing prenatally starting at the end of the first trimester. Normal adult levels are usually achieved by the age of 8 to 12 months. The function of AFP in adult humans is unknown; however, in rodents it binds estradiol to prevent the transport of this hormone across the placenta to the fetus. The main function of this is to prevent the virilization of female fetuses. As human AFP does not bind estrogen, its function in humans is less clear.