ELISA Kits

Angiotensin-converting enzyme(ACE) is a zinc-containing dipeptidyl carboxypeptidase widely distributed in mammalian tissues and is thought to play a critical role in blood pressure regulation. The predicted protein is identical, from residue 37 to its C terminus, to the second half or C-terminal domain of the endothelial ACE sequence. The protein sequence inferred consists of a 732-residue preprotein including a 31-residue signal peptide. The mature polypeptide has a molecular weight of 80,073. Although ACE has been studied primarily in the context of its role in blood pressure regulation, this widely distributed enzyme has many other physiological functions. The ACE gene encodes two isozymes. The somatic isozyme is expressed in many tissues, including vascular endothelial cells, renal epithelial cells, and testicular Leydig cells, whereas the testicular or germinal angiotensin-converting enzyme is expressed only in sperm. The standard product used in this kit is recombinant human ACE,

Angiotensin-converting enzyme(ACE), an exopeptidase, is a circulating enzyme that participates in the body's renin-angiotensin system(RAS), which mediates extracellular volume(i.e. that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. It is secreted by pulmonary and renal endothelial cells and catalyzes the conversion of decapeptide angiotensin I to octapeptide angiotensin II. Using a DNA marker at the growth hormone gene locus, which they characterized as 'extremely polymorphic' and which showed no recombination with ACE, ACE was mapped to 17q22-q24, consistent with the in situ hybridization mapping to 17q23. ACE, or kininase II, is a dipeptidyl carboxypeptidase that plays an important role in blood pressure regulation and electrolyte balance by hydrolyzing angiotensin I into angiotensin II, a potent vasopressor, and aldosterone-stimulating peptide. The enzyme is also able to inactivate bradykinin, a potent vasodilator.

Angiopoietin 1, also called ANG1 is a type of angiopoietin and is encoded by the gene ANGPT1. Angiopoietins are proteins with important roles in vascular development and angiogenesis. All angiopoietins bind with similar affinity to an endothelial cell-specific tyrosine-protein kinase receptor. This gene was mapped to 8q23.1. The protein encoded by this gene is a secreted glycoprotein that activates the receptor by inducing its tyrosine phosphorylation. It plays a critical role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme and inhibits endothelial permeability. The protein also contributes to blood vessel maturation and stability, and may be involved in early development of the heart.

E-Cadherin, also called Cadherin 1(CDH1), Uvomorulin or calcium-dependent adhesion protein, epithelial. E-cadherin is a Ca(2+)-dependent epithelial cell-cell adhesion molecule. Downregulation of E-cadherin expression often correlates with strong invasive potential and poor prognosis of human carcinomas. The gene spans a region of approximately 100 kb, and its location on chromosome 16q22.1. It contains 16 exons and a 65-kb-long intron 2. E-cadherin gene mutations may contribute to the development of diffusely growing gastric carcinomas. E-cadherin plays a central part in the process of epithelial morphogenesis and acts as a strong invasion suppressor in experimental tumor cell systems. The standard product used in this kit is recombinant gene expression with the molecular mass of 120KDa.

E-Cadherin, also called Cadherin 1(CDH1), Uvomorulin or calcium-dependent ashesion protein, epithelial. E-cadherin is a Ca(2+)-dependent epithelial cell-cell adhesion molecule. Downregulation of E-cadherin expression often correlates with strong invasive potential and poor prognosis of human carcinomas. The gene spans a region of approximately 100 kb, and its location on chromosome 16q22.1. It contains 16 exons and a 65-kb-long intron 2. E-cadherin gene mutations may contribute to the development of diffusely growing gastric carcinomas. E-cadherin plays a central part in the process of epithelial morphogenesis and acts as a strong invasion suppressor in experimental tumor cell systems.

Cardiotrophin-1(CT-1) is a member of the family of cytokines that includes leukemia inhibitory factor(LIF), ciliary neurotrophic factor(CNTF), oncostatin M(OSM), interleukin-6(IL6), and interleukin-11(IL11). And the CT-1 gene is mapped to 1p21-p13. The human CT-1 protein contains 201 amino acids and shares 80% amino acid identity with the 203-amino acid mouse CT-1 sequence; however, unlike the mouse protein, human CT-1 has 2 rather than 1 cys and has no N-glycosylation site. Despite lacking a signal sequence, secreted CT-1 and mouse CT-1 induce cardiac myocyte hypertrophy in cell culture and bind to both mouse and human LIFR but not to OSMR. Furthermore, A 1.7-kb CT-1 transcript was detected at high levels in heart, skeletal muscle, prostate, and ovary. Low levels were detected in lung, kidney, pancreas, thymus, testis, and small intestine, with little or no expression detected in brain, placenta, spleen, colon, and peripheral blood leukocytes. And it was also observed strong expressio

CCL1, Chemokine(C-C motif) ligand 1, is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The protein encoded by this gene is structurally related to the CXC subfamily of cytokines. Members of this subfamily are characterized by two cysteines separated by a single amino acid. This cytokine is secreted by activated T cells and displays chemotactic activity for monocytes but not for neutrophils. It binds to the chemokine receptor CCR8.

CCL1, Chemokine(C-C motif) ligand 1, is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The protein encoded by this gene is structurally related to the CXC subfamily of cytokines. Members of this subfamily are characterized by two cysteines separated by a single amino acid. This cytokine is secreted by activated T cells and displays chemotactic activity for monocytes but not for neutrophils. It binds to the chemokine receptor CCR8.

Monocyte chemotactic protein-1(MCP-1) is a member of the small inducible gene(SIG) family. It has been shown to play a role in the recruitment of monocytes to sites of injury and infection. By analysis of a panel of somatic cell hybrids, we have localized the MCP-1 gene, designated SCYA2, to human chromosome 17. In situ hybridization confirmed this assignment and further localized the gene to 17q11.2-q21.1. MCP-1 plays a unique and crucial role in the initiation of atherosclerosis and may provide a new therapeutic target in this disorder. Monocyte chemoattractant protein-1(MCP-1), regulated on activation, normal T cell expressed and secreted, and stimulation of monocytes from healthy carriers of the genotype GG with Mycobacterium tuberculosis antigens yielded higher MCP-1. The standard used in this kit is recombinant mouse MCP-1(Q24-R96) with the molecular mass of 8.5Kda.