5268 Results for: "ENZO LIFE SCIENCES"

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Concentrated lysis buffer for preparation of cell and tissue extracts.

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For the quantitative determination of human leptin in culture supernatants, plasma, and serum.

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Most sensitive (0,088pmol/m) colorimetric kit for extracellular cGMP quantification.

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Fixation/Permeabilization, (buffer)

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For the quantitative determination of PGE2 in culture supernatants from any species.

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Ultrasensitive PGE2 ELISA kit for inflammation and eicosanoid research.

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Produced in E.coli.

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Chemiluminescent acridinium esters are commonly used to label antibodies, proteins, nucleic acids, and some peptides, and are frequently used as detection reagents in immunoassays.

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CD40 is a 45-50 kDa type I membrane protein and a member of the tumor necrosis factor (TNF) receptor superfamily. CD40 is also known as pb50 or CDW40.  CD40 is expressed primarily by professional antigen-presenting cells and it is also expressed on non-immune cell types. The CD40 expressed by professional antigen-presenting cells plays a critical role in co-stimulation and antigen-presenting cell activation in T cell-dependent immune responses. Signals generated through CD40 in B cells are anti-apoptotic. These signals are also required for T cell-dependent B cell activation and proliferation, isotype switching, up-regulation of costimulatory receptors, germinal center formation and memory generation. CD40 signal transduction is initiated by binding trimeric CD40 ligand (CD40L) which is found on the surface of activated T cells.  CD40 engages several signalling pathways in B cells and these include NF-kB, the mitogen-activated protein kinases p38 and c-Jun N-terminal kinase. The 62 amino acid cytoplasmic domain (CD40c) of CD40 contains two linear TNF-receptor associated factor (TRAF) binding domains. The membrane proximal site of CD40c binds TRAF6 and the membrane distal site binds TRAF1, 2 and 3. CD40c is thought to mediate the CD40-dependant signalling pathways by recruitment of TRAF to this multimerized domain. CD40 ligation has also been shown to stimulate iNOS expression, and therefore NO production, by activating NF-kB in IFN-g treated microglial cells. NO derived from microglia has been implicated in the damage of myelin-producing oligodendrocytes in demyelinating disorders like multiple sclerosis (MS) and neuronal death during Alzheimer’s disease and brain trauma. Increased CD40-CD40 ligation has been implicated in the pathogenesis of several autoimmune inflammatory diseases, such as MS, arthritis and insulin-dependant diabetes.

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Produced in E. coli. Human LC3-I is fused at the N-terminus to a His-tag.

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The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.

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Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins at the neuromuscular junction during development. Agrin, MuSK, and Rapsyn are all essential components for AChR aggregation, through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface and induces AChR aggregation.

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Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface, and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites, increasing the predicted MW from 200kDa to ~600kDa. The diagram shown indicates the domain structure and functional regions of agrin, as well as domains required for AChR aggregation and alpha-dystroglycan and heparin binding.  Various agrin isoforms are generated by alternative splicing at the X, Y and Z sites, and differ in the presence or absence of small inserts. The isoforms can determine the biological activity of agrin and their expression in specific tissues and stages of development. While no difference in functional activity has been detected between splicing variants at site X, insertion of a 4 aa peptide at site Y modestly increases agrins nAChR clustering activity. Insertion of an 8 aa peptide at splicing site Z increases the clustering activity of soluble rat agrin 10,000 fold.

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Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins at the neuromuscular junction during development.

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APRIL (A proliferation-inducing ligand) is a member of the TNF family. APRIL stimulates B- and T-cell proliferation, triggers humoral immune responses, activates NF-κB, and induces cell death.

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The PKA Kinase activity kit is an efficient assay that utilizes little sample volume. This kit gives you the ability to an end-point or kinetic assay read-out in a convenient 96-well plate based assay and offers easy sample handling protocols. The assay also offers a high signal to background ratio.

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Alpha-crystallins composed of alpha A (~20 kDa) and alpha B (~20 kDa) subunits, are major water-soluble proteins accounting for almost 50% of total protein in the mammalian transparent eye lens and they are also found in a variety of other tissues. The two other crystallin families, beta and gamma, are homologous to each other but not to the alpha family or the sHsp's. Alpha-crystallins are also referred to as small heat shock proteins, since they are induced by increased temperature in a variety of organisms. The alpha-crystallins have sequence homology as well as structural and functional similarities with the small Hsp's such as Hsp25/27. Most small heat shock proteins have four common structural and functional features: (i) molecular weight between 12 and 43kDa; (ii) the formation of large oligomeric complexes composed of alphaA-crystallin, alphaB-crystallin and Hsp25/27; (iii) the moderately conserved alpha-crystallin domain in the central region of the protein; and (iv) molecular chaperone activity. The alpha-crystallin domain comprises approximately 90 residues, is bounded by variable N-terminal and C-terminal extensions and is involved in oligomer assembly. Oligomers can reach 800kDa or more and are dynamic, exhibiting subunit exchanges and organizational plasticity, possibly leading to functional diversity. Phosphorylation of serine residues occurs during development and in response to stress, and usually decreases oligomer size. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation, although productive release and refolding of denatured proteins requires close cooperation with other chaperones. Other proposed functions include a role in membrane stabilization and modulation of intermediate filament organization during physiological stress and neurodegenerative disease.

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Glutathione, a major intracellular non-protein thiol, protects against free radical damage by providing reducing equivalents for several key antioxidant enzymes. In addition, glutathione acts as a scavenger of hydroxyl radicals and nascent oxygen. Elevated glutathione levels are associated with a reduced rate of illness, higher levels of self-rated health, lower cholesterol, lower body mass index, and lower blood pressure among the elderly. Glutathione provides a primary defense system for the removal of oxidants in the brain. Studies have revealed a correlation between low glutathione levels and damage to neurons that manufacture dopamine, suggesting a link to Parkinson's disease.

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GrpE (Glucose Regulated Protein E. coli) is encoded by a monocistronic E. coli gene, which is under the control of both s32 and s70 transcription factors. The GrpE protein is a so-called co-chaperone because it is known to assist the DnaK (Hsp70) protein to effectively carry out DnaK-dependent chaperone activity (i.e. protein folding, protein transport, disaggregation of heat inactivated proteins, activation of mutant protein).

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Hsp60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. Hsp60 is the eukaryotic homolog of the E. coli GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of Hsp60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.

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Produced in E. coli.

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Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

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Produced in E. coli.

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FKBP59, also known as Hsp56/p59 is an immunophilin that is a component of Hsp70/Hsp90/steroid receptor complexes. Expression of FKBP59 is increased in response to heat shock and ischemic stress, and is thought to play a role in the folding and cytoplasmic/nuclear distribution of steroid receptors.

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Synaptotagmins (Syt) are membrane-trafficking proteins characterized by an N-terminal transmembrane region, a variable linker, and two C-terminal C2-domains, C2A and C2B. At least twelve Synaptotagamins are expressed in vertebrates and can be found in both vesicular and plasma membranes.

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Membrin, also known as GS27 (Golgi SNARE of 27K), is an integral membrane protein present on the surface of the Golgi apparatus. GS27 is a member of a protein complex that consists of cis-Golgi vesicle receptor syntaxin 5 and GS28, v-SNARE rbet1 and Rsec22, and Rsly1. These complexes are postulated to direct the fusion of ER-derived vesicles with vesicular tubular cluster (VTC), and the fusion of VTCs to form cis-Golgi compartment.

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Produced in E. coli.

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rSec6 and rSec8 are rat homologs of the yeast Sec6 and Sec8 proteins that are essential for protein transport between the Golgi apparatus and the plasma membrane. In yeast, Sec8 is part of a 19.5S complex that includes Sec6 and Sec15, that also associate with the ras-like GTP binding protein Sec4. An analogous 17S complex in rat brain was found to contain rSec6 and rSec8, along with eight proteins with a combined molecular weight of 743 kDa. The membrane-associated rSec6/8 complex co-immunoprecipitates with syntaxin, providing evidence that this complex is involved in synaptic vesicle docking and fusion at the presynaptic terminal.

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Postsynaptic density protein 95 kDa (PSD-95), also known as Synapse associated protein 90 kDa (SAP90), is a brain specific protein that is highly similar to the Drosophila dlg tumor suppressor protein. PSD-95 is a member of membrane associated proteins that are localized beneath the postsynaptic membrane of synapses in the CNS. PSD-95 interacts with NMDA receptor and Shaker-type K+ channels and contributes to their clustering and localization at the synaptic spines in hippocampal neurons and the pinceau terminal of cerebellar basket cells, respectively.

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Produced in E. coli.