Detection Of Spike Protein

Description: True Blue

Description: True Blue

Description: True Blue

Description: True Blue

Description: True Blue

Description: The SARS-CoV-2 IgG detection kit is designed for qualitative detection of human IgG antibodies in serum collected from individuals suspected of prior infection with the virus that causes COVID-19. This fast and simple ELISA uses the trimeric form of the SARS-CoV-2 Spike protein (BPS Bioscience #100728) to identify IgG antibodies that indicate a previous infection with SARS-CoV-2. The Spike protein is expressed on the viral membrane as a trimer, which means this kit measures IgG antibodies in a more physiologically relevant context than many other commercially available ELISA kits. 

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

Description: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. This process is regulated by the interplay of pro- and anti-apoptotic members of the B-cell lymphoma 2 (Bcl-2) family. The BH3-only (Bcl-2-homology domain 3 only) proteins are a pro-apoptotic subgroup of the Bcl-2 family that are critical initiators of lymphocyte apoptosis and other processes. Unlike the other members of the Bcl-2 family which contain at least two Bcl-2 homology (BH) domains, these proteins contain just one, the BH3 domain. Some of the members of this family, such as Hrk, may show little sequence homology to the others, but all BH-only proteins can bind to at least some pro-survival Bcl-2-like proteins through this BH3 domain and trigger apoptosis when overexpressed. For example, the proteins Bad, Bim and Bmf regulate apoptosis by forming heterodimers with the anti-apoptotic proteins Bcl-2 and Bcl-xL. Bim, Noxa, and PUMA are activated by p53 following DNA damage although the exact mechanisms are not entirely clear. Noxa may also be involved with the activation of Bik, a BH3-only protein whose localization in the endoplasmic reticulum (ER) suggests that Bik may play a role in ER-stress-induced apoptosis. While full-length Bid also promotes apoptosis when expressed, its activity is enhanced following cleavage by enzymes such as capsase-8, suggesting that Bid may play a key role in death-receptor induced apoptosis.;;For images please see PDF data sheet

Description: The endoplasmic reticulum (ER) is an organelle composed of an interconnected network of tubules, vesicles and cisternae found in all eukaryotic cells. It is involved in several specialized processes such as protein translation, folding, and transport of proteins to be used in the cell membrane or secreted from the cell. Accumulation of malfolded proteins in the ER activates the unfolded protein response (UPR) and the upregulation of the ER molecular chaperones GRP78 and GRP 94. These proteins are normally bound to ER transmembrane proteins such as IRE1p and ATF6 but ER stress causes their dissociation. This allows IRE1p, a serine-threonine protein kinase, to transduce the unfolded protein signal from the ER to the nucleus. IRE1p also has an endoribonuclease activity that is required to splice X-box binding protein (XBP1) mRNA, converting it to a potent UPR transcriptional activator. ER stress also causes the cleavage of ATF6, yielding a cytosolic fragment which migrates to the nucleus and together with XBP-1, activates transcription of UPR-responsive genes. Depletion of IRE1p through the expression of a dominant negative form of IRE1p has no effect on transfected cells, but cell death via apoptosis occurs under stress conditions that cause unfolded proteins to accumulate in the ER.;;For images please see PDF data sheet