5268 výsledků pro: "ENZO LIFE SCIENCES"

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Potent and selective NMDA receptor glycine site antagonist.

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Tamoxifen metabolite

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Lidocaine hydrochloride

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Minor constituent of hot pepper (capsicum oleoresin).

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Cholesterol metabolite linked to breast cancer, neurodegenerative disease and metabolism.

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Host: Mouse, Isotype: IgG2b

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Hedgehog (Hh) pathway blocker.

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TLR4 activator.

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TRP channel agonist.

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TLR4 activator.

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mGluR5 antagonist.

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TLR4 activator.

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Inhibits the recruitment of the co-activators β-catenin and GRIP1

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ATP analog that can substitute ATP in various kinase reactions. Substrate and inhibitor of ATP-dependent enzyme systems. The resulting thiophosphorylated proteins are resistant to dephosphorylation by protein phosphatases. Increases the activity of Ca2 -activated K channels.

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Octyl-β-D-thioglucopyranoside

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Produced in E.coli. Mouse Mn SOD is fused at the N-terminus to a His-tag.

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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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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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DnaK possesses an autophosphorylation activity and a weak 5-nucleotidase activity, cleaving the 5 phosphate groups from both ribose and deoxyribose nucleotides. The role of DnaK in ATP-dependent protein-protein interactions has been extended to normal E. coli physiology, where, like eukaryotic Hsp70 homologs, it is thought to participate in the assembly/disassembly of protein complexes.

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Concentrated lysis buffer for preparation of cell and tissue extracts.

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Inhibitor of caspase-1, -4 and -5

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Caspase and granzyme inhibitor

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Substrate for caspase-1 and -4

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Caspase-8 substrate

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PTP inhibitor, PTEN Inhibitor

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3-Aminobenzamide

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Calmodulin antagonist. PDE inhibitor.

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p38 inhibitor