MBS154734-1Set

TOR Signaling Pathway Detection Set

1622.69 €

MBS154734-5x1Set

TOR Signaling Pathway Detection Set

6805.89 €

PSI-1805

TOR Signaling Pathway Detection Set

The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle progression through its ability to integrate signals from nutrient levels and growth factors. TOR regulation is accomplished through a network of various activators and repressors. It is phosphorylated by Akt, whose activity is indirectly inhibited by the lipid phosphatase PTEN. TOR is normally associated with the regulatory proteins RAPTOR, a scaffold protein whose binding by TOR substrates is necessary for effective TOR-catalyzed phosphorylation, and G&#914;L, which stimulates TOR’s kinase activity towards downstream proteins. It is further regulated by the proteins Rheb, TSC1 and TSC2, which act to modulate TOR activity. The downstream targets of TOR are thought to be the ribosomal protein S6 kinases and the eukaryotic initiation factor 4E binding proteins (4EBPs) whose activation leads to increased protein translation and cell growth.;;<b>For images please see PDF data sheet</b>

2082.01 €

PSI-1807

TLR Adaptor Detection Set

Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules to activate various kinases and transcription factors so the organism can respond to potential infection. These adaptor molecules include MyD88, TIRAP, TIRP, TOLLIP, and TRIF. These molecules interact with and activate the IL-1R-associated kinase (IRAK) family, which then activates TNF receptor associated factor (TRAF)-6, and ultimately leads to the activation of NF-&#954;B. While most TLRs utilize more than one adaptor, certain adaptor molecules are essential for individual TLR signaling, e.g., TLR4 signaling is dependent on TIRP expression.;;<b>For images please see PDF data sheet</b>

1471.17 €

PSI-1810

SARS Protein Detection Set

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.;;<b>For images please see PDF data sheet</b>

1471.17 €

PSI-1811

Anthrax Protein Detection Set

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.;;<b>For images please see PDF data sheet</b>

1471.17 €