Description: ELISA based test for quantitative detection of EM (Anti-endometrial Antibody IgG)

Description: ELISA based test for quantitative detection of ASA (Anti-sperm Antibody IgG)

Description: ELISA based test for quantitative detection of Mg (Mycoplasma Genitalium Antibody IgG)

Description: ELISA based test for quantitative detection of Mh (Mycoplasma Hominis Antibody IgG)

Description: ELISA based test for quantitative detection of Ct (Chlamydia Trachomatis Antibody IgG)

Description: ELISA based test for quantitative detection of MV (Measles Virus Antibody IgG)

Description: ELISA based test for quantitative detection of TB (Mycobacterium Tuberculosis Antibody IgG)

Description: OVA Detection ELISA

Description: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral S (Spike) protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. The M protein (Membrane protein, Matrix protein) is another major structural viral protein. It is an integral membrane protein involved in the budding of the viral particles and interacts with S protein and the nucleocapsid protein. The SARS E protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. ACE2, the SARS receptor, normally plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis.;;For images please see PDF data sheet

Description: Anthrax infection is initiated by the inhalation, ingestion, or cutaneous contact with Bacillus anthracis endospores. B. anthracis produces three polypeptides that comprise the anthrax toxin: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA binds to two related proteins on the cell surface; these are termed tumor epithelial marker 8 (TEM8)/anthrax toxin receptor (ATR) and capillary morphogenesis protein 2 (CMG2). PA is cleaved into two fragments by a furin-like protease after receptor binding. The bound fragment binds both LF and EF; the resulting complex is then endocytosed into the cell which allows the release of LF and EF into the cytoplasm. These toxins are usually sufficient to cause rapid cell death, and often the death of the infected organism. LF is the primary toxin of anthrax and functions as a highly specific protease that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family near their amino terminus, interfering with MAPK signaling and inducing apoptosis . EF is a calmodulin and Ca++-dependent adenylate cyclase responsible for the edema seen in the disease. It is thought to benefit the B. anthracis bacteria by inhibiting cells of the host immune system. The Anthrax toxin receptor (ATR) was initially discovered as the tumor endothelial marker 8 (TEM8). This protein, which exists in three isoforms (36, 40, and 60 kDa), is highly expressed in tumor vessels as well as in the vasculature of developing embryos, suggesting that it may normally play a role in angiogenesis in addition to its role as the anthrax toxin receptor.;;For images please see PDF data sheet

Description: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. In mammalian cells, APG7 is essential for autophagy conjugation systems, autophagosome formation, starvation-induced bulk degradation of proteins and organelles. Beclin-1, a coiled-coil Bcl-2-interacting protein homologous to the yeast autophagy gene apg6, is a mammalian autophagy gene that can inhibit tumorigenesis and is expressed at reduced levels in human breast carcinoma, suggesting that defects in autophagy proteins may contribute to the development or progression of tumors. PIST is a protein that interacts with Beclin-1 through its coiled-coil domain and can modulate Beclin-1 activity. LAMP1 and LAMP2 are homologous, highly glycosylated proteins associated with the lysosome and are thought to have overlapping functions. Mice lacking LAMP1 have very minor defects compared to those deficient in LAMP2 expression. However, the loss of both proteins results in embryonic lethality, suggesting that each protein possesses some unique and necessary functions.;;For images please see PDF data sheet