12531 Résultats pour : "Enzo Life Sciences"

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DNA-topoisomerase II, also known as Topo II or Top 2, is a multifunctional nuclear enzyme required during DNA replication, chromosome disjunction at mitosis, and other DNA-related activities because of its ability to alter DNA supercoiling. In mammalian cells, Topo II consists of two isozymes, Topo II-alpha (170kDa) and Topo II-beta (180kDa) and expression and localization of each isoform are distinct and stage specific during the cell cycle. Topo II-beta is expressed constitutively throughout the cell cycle, whereas the expression of Topo II-alpha is cell cycle-regulated, peaking in G2 to M phase and declining to a minimal level at the end of M phase. DNA-topoisomerase II is the target of some of the most active drugs used in chemotherapy and has been shown to have a critical role in neural development.

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The Rab family of GTP-binding proteins are members of the Ras superfamily of small G proteins, and participate in multiple steps of the membrane trafficking. Rab3A participates in the fusion of synaptic vesicles during neurotransmitter release, a process regulated by GDP/GDP exchange cofactors such as GAP, GDI, GRF, and rabphilin. Rab4 regulates recycling of proteins from the early endosome to the surface of many cell types, regulating glucose transporter and transferrin receptor cell surface localization. Rab5 regulates the fusion of plasma membrane-derived clathrin-coated vesicles with early endosomes and homotypic fusion among early endosomes.

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The lymphocyte activation gene-3 (LAG-3, CD223), a member of the immunoglobulin superfamily (IgSF) related to CD4, binds to the major histocompatibility complex (MHC) class II molecules but with higher affinity than CD4. Several alternative mRNA splice-variants of human LAG-3 have been described, two of them encoding potential secreted forms: LAG-3V1 (i.e. the D1-D2 domains of the protein, 36 kDa) and LAG-3V3 (D1-D3, 52 kDa). The longer form was detected by ELISA in the serum of healthy individuals as well as of tuberculosis patients with a favorable outcome. LAG-3 expression by T cell clones correlated with IFN-γ production, and hence soluble LAG-3 has been suggested as a serological marker of Th1 responses.

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A complete colorimetric assay kit for measuring cellular calcineurin (PP2B) phosphatase activity. It employs a convenient 96-well plate format with all reagents necessary for measuring calcineurin (PP2B) phosphatase activity in tissue/cellular extracts PLUS human recombinant calcineurin is included as a positive control.

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Adrenergic receptors mediate the hormone and neurotransmitter functions of adrenaline and noradrenaline. Adrenoreceptors function in peripheral tissues and the central nervous system to regulate numerous vascular, metabolic, and neurological functions, and are the target for many therapeutically relevant drugs including those for the treatment of hypertension, asthma, benign prostatic hypertrophy, and depression. Adrenoreceptors are classified by three types and multiple subclasses (alpha1A,1B,1D; alpha2A,2B,2C; and beta1,2,3) based on pharmacological and molecular characteristics.

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For the quantitative determination of LTB4 in culture supernatants, plasma, saliva, and urine from any species. Cited sample types include bronchioalveolar lavage fluid, cell lysate, crevicular fluid, tissue, serum and whole blood.

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Mitochondria dye

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DNA dye

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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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AP substrate.

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The GOLGI ID® Green assay kit contains a Golgi apparatus-selective dye suitable for live cell, or aldehyde-fixed cell staining. It is more faithfully localized to the target organelle, with minimal staining of the endoplasmic reticulum. Micromolar concentrations of GOLGI ID® Green dye are sufficient for staining mammalian cells, as validated with human cervical carcinoma cell line HeLa, human T-lymphocyte cell line, Jurkat, canine kidney cell line MDCK, and human bone osteosarcoma epithelial cell line U2OS.

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The Assay Designs Ras activation kit provides a simple, convenient and efficient tool for monitoring the activation of the small GTPase, Ras. This assay uses a GST-fusion protein containing the Ras-binding domain (RBD) of Raf1 to affinity precipitate active Ras (GTP-Ras) from cell lysates. The GST-Raf1-RBD fusion protein (~42kDa) is incubated with cell lysate and an Immobilized Glutathione Resin. The pulled-down active or GTP-Ras is detected by Western blot analysis using a specific Ras Antibody.

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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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Produced in E.coli.

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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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Produced in E. coli.

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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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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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The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

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Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex which regulates systemic, local and intracellular homeostatic responses elicited by hypoxia. HIF-1 is a heterodimer of HIF-1alpha and HIF-1beta.

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Potent and selective thromboxane A2 synthase inhibitor (IC50=11nM).

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Viperin has been identified as a human cytomegalovirus and IFN-γ inducible protein. Its expression is activated by both TLR3-dependent and RIG-I-dependent pathways. Viperin inhibits influenza A virus release of infected cells by altering plasma membrane fluidity and the formation of lipid rafts. It acts on the lipid rafts by decreasing the activity of the enzyme farnesyl diphosphate synthase (FPPS) which is essential for isoprenoid biosynthesis.

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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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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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EBI3 (Epstein-Barr virus-induced gene 3 protein; EBV-induced gene 3 protein; IL-27B; IL-27 subunit β) and IL-12A (IL-12 subunit p35; CLMF p35) form the heterodimeric cytokine IL-35 (interleukin-35) involved in T cell regulation.

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Produced in E. coli.

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Produced in E. coli.

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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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Produced in E. coli.

Supplier: Enzo Life Sciences

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.