5059 Résultats pour : « Enzo Life Sciences »

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The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

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Polyclonal antibody prepared against the Adda moiety binds to microcystins and nodularins, allowing the congener-independent determination of these toxins and many of its congeners, and does not cross-react with other non-related toxins or compounds

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MEK is a dual specificity kinase capable of phosphorylating both tyrosine and threonine residues. The MEK family, which is also known as MAP kinase kinase, phosphorylates MAP kinases on the conserved T-X-Y motif; phosphorylation of MAPK by MEK results in an increase in MAPK activity. MEK is involved in a diverse array of cellular processes such as stress-activated response, apoptosis, cytokine-induced cell proliferation, and DNA recombination during meiosis.

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Bax is an appromimately 22 kDa pro-apoptotic protein belonging to the Bcl-2 family of proteins, which are characterized by the presence of at least one Bcl-2 homology (BH) domains. Bax normally resides in the cytoplasm, but following an apoptotic stimuli, Bax undergoes a conformational change and translocates to mitochondrial membranes where it inserts and mediates the release of cytochrome c. This activates caspase-3 and perpetuates the apoptotic cascade.

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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 multifunctional, multi-compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the soluble paralog of the ER membrane protein Calnexin (Cnx). Crts three domains include a 180 residue N-terminal domain, a proline-rich P-domain (residues 189-288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P-domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N-glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

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Aurora A, B, and C have emerged as key mitotic regulators of mammalian centrosome function, chromosome segregation and cytokinesis. Aurora B is one of several chromosomal passenger proteins involved in chromosome alignment at the metaphase plate and cytokinesis. Phosphorylation of a threonine residue in the Aurora activation loop (Thr232 in human Aurora B) is believed to be an essential regulatory mechanism in Aurora kinase activation.

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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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SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

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ERp57 (also known as Grp58), a member of the Thioredoxin superfamily, is an ER protein with disulfide isomerase activity. It has been shown to increase after oncogenic transformation and to be a component of the MHC Class I peptide-loading complex.

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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.

Supplier: Enzo Life Sciences

Calreticulin (CRT) is a multifunctional, multi-compartmental protein most abundant in the ER lumen. CRT contains the ER-retrieval sequence, KDEL, and has been best characterized as a soluble molecular chaperone of new or misfolded proteins and a Ca2+- binding protein. Both CRT and its membrane bound homolog, Calnexin (CNX) interact with proteins and glycoproteins that have monoglucosylated N-glycans. The CRT/CNX cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligimerization, regulates ER degradation, and provides quality control by preventing incompletely folded glycoproteins from exiting to the Golgi complex.

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Isotype matched controls are useful in flow cytometry to determine a gross estimate of non-specific binding that may be observed with a specific antibody of interest. In general, an isotype control should be of the same species and isotype as the antibody of interest, used at the same concentration, and conjugated to the same fluorophore. This reagent is an IgG1 isotype mouse monoclonal antibody (Clone # MOPC-21) conjugated to phycoerythrin (PE). It is intended for use as an isotype control antibody for flow cytometry.

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Prostaglandin E2 (PGE2) is an extensively studied prostaglandin owing to its predominance in inflammation, cancer, atherosclerosis, autoimmune disease, and sepsis. Oxidation of arachidonic acid by prostaglandin synthases (COX-1 and COX-2) produces prostaglandin H2 (PGH2), which is further metabolized by PGE synthases into its major product, PGE2. PGE2 mediates autocrine and paracrine signaling by binding to G-protein coupled receptors (EP1, EP2, EP3, EP4) on the cell surface, functioning to modulate phospholipase C and adenylate cyclase activity. PGE2 has been of great interest as a therapeutic target, either by modulation of its synthesis by COX inhibitors (NSAIDS) or by modulation of its receptors by downregulation or binding antagonists. PGE2 production in a variety of tissues has been shown to modulate numerous physiological processes including natriuresis in the kidney, smooth muscle elasticity in the vasculature, and the inflammatory response to damaged tissues by monocytes and macrophages.

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Cyto-ID® Green long-term cell tracer kit is suitable for a variety of applications including long term cell viability, cytotoxicity, cell adhesion, cell migration and cell-cell fusion studies.

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Produced in E. coli.

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The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: Enzo Life Sciences

Mitogenic platelet derived growth factor (PDGF) signaling is mediated by the PDGF tyrosine kinase receptors PDGFRα and PDGFRβ, which exist as homo- or heterodimer isoforms (αα, ββ, αβ). Secretion of PDGFs and expression of PDGFRs in a broad distribution of cell types contributes to regulation of cellular processes including cell growth, actin reorganization, prevention of apoptosis, and chemotaxis. Structurally, the transmembrane PDGFRs are composed of an N-terminal extracellular domain with five immunoglobulin repeats, and an intracellular domain containing two spaced tyrosine kinase domains. PDGF ligands display preferential affinity to PDGFRα and PDGFRβ, with PDGFRβ activation restricted to binding by PDGF BB and PDGF DD. Growth factor binding initiates receptor dimerization and activates the cytosolic tyrosine kinase domains.

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The Cyto-ID® Autophagy detection kit provides a rapid, specific and quantitative approach for monitoring autophagy in live cells by fluorescence microscopy and flow cytometry.

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Sensitive (30 ng/ml) ELISA for the quantitative determination of host cell protein contamination in bulk products expressed in E

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Caspase and granzyme substrate

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FAAH substrate.

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GSK-3 inhibitor

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Ubiquinone-5 ≥95% (by HPLC)

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Potent and selective serotonin uptake inhibitor

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PARP inhibitor

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Blocks Hedgehog signaling

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SIN-1 is a metabolite of molsidomine which decomposes spontaneously in solution in the presence of oxygen, releasing NO and superoxide anion under physiological conditions. Since NO and superoxide react to form peroxynitrite, SIN-1 may actually produce peroxynitrite under physiological conditions. It is a potent vasodilator and inhibitor of platelet aggregation and produces significant protective effects in myocardial ischemia-reperfusion. The effects of SIN-1 are markedly attenuated by nitroglycerin-induced tolerance. Inhibits cysteine proteases.

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Protein kinase inhibitor

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This peptide, Biotin-Ahx-KEAPEDLYKDFLTL, is derived from the KDR sequence and is a substrate for FGFR. The biotin allows peptide to be used in kinase assays with streptavidin-bound membranes.