Reliatech

Description: ELISA

Description: A competitive ELISA for quantitative measurement of Human True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Human True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6R α and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant human IL-6 is a 20.9 kDa protein containing 184 amino acid residues.

Description: Interleukin 7 (IL-7), previously known as pre-B-cell growth factor and lymphopoietin-1, is expressed by adherent stromal cells from various tissues. Mouse IL-7 has approximately 65% amino acid sequence identity with human IL-7 and both proteins exhibit cross-species activity.

Description: Il-8 or CXCL8 was originally discovered and purified as a neutrophil chemotactic and activating factor. It was also referred to as neutrophil chemotactic factor (NCF), neutrophil activating protein (NAP), monocytederived neutrophil chemotactic factor (MDNCF), T lymphocyte chemotactic factor (TCF), granulocyte chemotactic protein (GCP) and leukocyte adhesion inhibitor (LAI). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes, and various tumor cell lines, can produce CXCL8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS, and viruses. CXCL8 is a member of the alpha (CXC) subfamily of chemokines, which also includes platelet factor-4, GRO, and IP10.

Description: Emilins (elastin microfibril interface located proteins) are extracellular matrix glycoproteins that localize to sites with proximity to elastin and microfibrils. They consist of an N-terminal cysteine-rich EMI domain and a conserved C-terminal gC1q-like domain. Emilin-1 is abundant in elastin-rich tissues such as blood vessels, skin, heart and lung. It influences placenta formation and initial organogenesis with a later role in interstitial connective tissue. Emilin-2 is larger than Emilin-1 and contains a unique proline-rich domain. It is likely involved in the process of elastogenesis. Multimerin-2 (also known as Emilin-3 or EndoGlyx-1) is expressed during embryonic development. Multimerin-1 (also known as Emilin-4) is expressed in platelets and the endothelium of blood vessels and may act as a carrier protein for platelet factor V. Emilin-5 is encoded by the Emilin-3 gene and is sometimes referred to as Emilin-3. It contains the N-terminal cysteine-rich EMI domain but lacks the C-terminal gC1q-like domain. Emilin-1 have been shown to be expressed in smooth muscle and other mesenchymal tissues and is localized at the proximity of elastin and microfibrils. Emilin-1 exerts an important role in lymphatic system, being a crucial structural molecule that regulates the formation of lymphatic capillaries and collectors. Emilin-1 through the interaction with the α4β1 integrin via the C-terminal gC1q domain exerts a negative effect on proliferation. It binds pro-TGFβ preventing its maturation to mature TGFβ in the extracellular space, therefore influencing the regulation of blood and lymph vessels formation and maintenance.

Description: ABCG2 is one of at least three human ATP binding cassette (ABC) transporters which can facilitate the export from cells of a wide range of chemically unrelated drug molecules. This capacity for multidrug transport is not only a confounding factor in chemotherapy, but is also one of the more perplexing phenomena in transporter biochemistry.

Description: Angiopoietin1 (Ang1) and Angiopoietin2 (Ang2) are two closely related secreted ligands which bind with similar affinity to Tie2, a receptor tyrosine kinase with immunoglobulin and epidermal growth factor homology domains expressed primarily on endothelial cells and early hematopoietic cells. Tie2 and angiopoietins have been shown to play critical roles in embryogenic angiogenesis and in maintaining the integrity of the adult vasculature. Ang1 cDNA encodes a 498 amino acid (aa) residue precursor protein that contains a coiledcoiled domain near the aminoterminus and a fibrinogen like domain at the Cterminus. Human Ang 1 shares approximately 97% and 60% aa sequence identity with mouse Ang1 and human Ang2, respectively. Ang1 activates Tie2 signaling on endothelial cells to promote chemotaxis, cell survival, cell sprouting, vessel growth and stabilization. Ang2 has alternatively been reported to be an antagonist for Ang1 induced Tie2 signaling as well as an agonist for Tie2 signaling, depending on the cell context.

Description: Placental alkaline phosphatase (PLAP) is a membrane enzyme mainly expressed in the placenta. PLAP is shown to be expressed in ovarian cancer (OV), however, there is little known about its expression in other cancers.

Description: Angiopoietin2 (Ang2; also ANGPT2) is a secreted glycoprotein that plays a complex role in angiogenesis and inflammation. Mature Ang2 is 478 amino acids (aa) in length. It contains one coiledcoil domain (aa 166-248) that mediates multimerization, and a C-terminal fibrinogen like domain (aa 275-495) that mediates receptor binding. Under reducing conditions, secreted monomeric Ang2 is 65-66 kDa in size. Under nonreducing conditions, both natural and recombinant Ang2 form 140 kDa dimers, 200 kDa trimers, and 250-300 kDa tetramers and pentamers. Alternate splicing generates a short isoform that lacks 52 amino acids (aa) preceding the coiledcoil domain. Mature human Ang2 shares 86% aa sequence identity with mouse and rat Ang2. Ang2 is widely expressed during development, but it is restricted postnatally to highly angiogenic tissues such as the placenta, ovaries, and uterus. It is particularly abundant in vascular endothelial cells (EC) where it is stored in intracellular WeibelPalade bodies. Both Ang2 and the related Angiopoietin1 (Ang1) are ligands for the receptor tyrosine kinase Tie2. While Ang1 is a potent Tie2 agonist, Ang2 may act as either a Tie2 antagonist or agonist, depending upon its state of multimerization. The higher the order of oligomer, the more effective Ang2 becomes as a Tie2 agonist. The short isoform appears to block the binding of either Ang1 or full-length Ang2 to Tie2. Ang2 functions as a proangiogenic factor, although it can also induce EC death and vessel regression. Upon its release from quiescent EC, it regulates vascular remodeling by promoting EC survival, proliferation, and migration and destabilizing the interaction between EC and perivascular cells. Ang2 is required for postnatal vascular remodeling, and it cooperates with Ang1 during lymphatic vessel development. It mediates the upregulation of ICAM1 and VCAM1 on EC, which facilitates the adhesion of leukocytes during inflammation. Ang2 is upregulated in both the endothelium and tumor cells of several cancers as well as in ischemic tissue. Its direct interaction with Integrins promotes tumor cell invasion. Ang2 also promotes the neuronal differentiation and migration of subventricular zone progenitor cells.

Description: FAP is a 760 amino acid long type II transmembrane glycoprotein. It contains a very short cytoplasmic N terminal part (6 amino acids), a transmembrane region (amino acids 7–26), and a large extracellular part with an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.[9][10]A soluble form of FAP, which lacks the intracellular and transmembrane part, is present in blood plasma.[11] FAP is a non-classical serine protease, which belongs to the S9B prolyl oligopeptidase subfamily. Other members of the S9B subfamily are DPPIV, DPP8 and DPP9.[12] FAP is most closely related to DPPIV (approximately 50% of their amino acids are identical). The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice.[10] FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity.

Description: Alpha-1-fetoprotein (AFP), also alphafoetoprotein or α1-foetoprotein, is a glycoprotein in mammals that is produced during human embryonic development in the course of pregnancy by the entodermal tissue and fetal liver, or in adults especially in tumor cells of the liver. Physiologically, alpha-1 fetoprotein has the function of a fetal transport protein, particularly transporting copper, nickel, fatty acids, and bilirubin in fetal blood plasma. AFP is structurally closely related to the transport proteins albumin, vitamin D-binding protein, and afamine. Production begins in the four-week-old embryo, is highest in the twelfth to sixteenth weeks, and stops almost completely after birth. In the adult, plasma levels are usually less than 40 ng/ml.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue-nonspecific). The first three are located together on chromosome 2, whereas the tissue-nonspecific form is located on chromosome 1. The product of this gene is a membrane-bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization. However, mice that lack a functional form of this enzyme show normal skeletal development.

Description: This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse immunized with ecombinant human Akt2.

Description: This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse immunized with ecombinant human Akt3.

Description: Activated leukocyte cell adhesion molecule (ALCAM) is a typeI membrane glycoprotein that is a member of the immunoglobulin superfamily. It is also known as CD166, MEMD, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat.

Description: Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP3 (stromelysin1), can degrade a broad range of substrates including collagen α chains, aggrecan, laminin, fibronectin, elastin, casein, α1 antitrypsin, myelin basic protein, IL1β, IGFBP3, pro MMP1, pro MMP7, pro MMP8, pro MMP9 and pro MMP13. MMP3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP3 may be divided into several distinct domains; a prodomain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexinlike) domain.

Description: Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican. MMP7 is implicated in the activation of other proteinases such as plasminogen, MMP1, MMP2, and MMP9. In addition to its roles in connective tissue remodeling and cancer, MMP7 also regulates intestinal α-defensin activation in innate host defense, releases tumor necrosis factorα in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP7 is the smallest of the MMPs and consists of two domains: a prodomain that is cleaved upon activation and a catalytic domain containing the zincbinding site.

Description: Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNFα and GM-CSF. MMP8 is capable of cleaving types I, II and III triplehelical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, βcasein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis, MMP8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP8 consists of several domains: a prodomain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexinlike domain. MMP8 is heavily glycosylated.