5268 Results for: "ENZO LIFE SCIENCES"

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The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90α and Hsp90β, encoded by separate genes. The amino acid sequences of human and yeast Hsp90-alpha are 85% and 90% homologous to those of Hsp90β , respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1 to 2% of all cellular proteins in most cells. Hsp90 functions as part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control. In this context, researchers identified key regulatory proteins as substrates of Hsp90, including steroid receptors, cell cycle kinases involved in signal transduction, and p53. Hsp90 may act as a capacitor for morphological evolution by buffering widespread variation, potentially affecting morphogenic pathways. When temperature and other stress factors compromise Drosophila Hsp90 buffering, cryptic variant expression occurs, and selection can lead to the continued expression of these traits even after Hsp90 function is restored.

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Produced in E. coli.

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Isolated from bovine eye lens.

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HSFs (Heat Shock family of transcription factors), which consists of HSF 1-4, bind to highly conserved Heat shock elements (HSEs) in the promoter regions of heat shock genes, ultimately regulating the expression of Heat shock proteins (Hsps). On exposure to heat shock and other stresses, HSF1 localizes within seconds to discrete nuclear granules and on recovery from stress, HSF1 rapidly dissipates from the stress granules to a diffuse nucleoplasmic distribution.

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Anti-HMOX1 Rabbit Polyclonal Antibody

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GroEL and GroES are E.coli chaperonins, which are homologs of mitochondrial chaperonins Hsp60 and Hsp10. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding with an ATP-dependent mechanism.

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Bassoon is a 420 kDa protein that localizes at the presynaptic nerve terminals and is believed to play a role in the structural and functional organization of the synaptic vesicle cycle. Bassoon is concentrated at sites opposite to postsynaptic densities in synaptic terminals and in cultured neurons, it is found to colocalize with GABA (A) and glutamate (GluR1) receptors. These observations suggested that they serve specific functions at synaptic junctions and may be involved in organization of the cytoskeleton at the site of neurotransmitter release.

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Produced in E. coli.

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Produced in E. coli.

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Produced in E. coli.

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Dog;Human;Pig Endothelin 2

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Endogenous GHS-R ligand

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Produced in Sf21 cells. Mouse full-length PARP-2 is fused to a His-tag.

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Produced in E. coli.

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Produced in Drosophila Schneider 2 (S2) cells. Recombinant human hepsin (aa 45-417) is fused at the C-terminus to a V5-His-tag.

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Notch ligand

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Transferrin is a serum glycoprotein involved in iron transport. Transferrin exists in two forms, the iron-free Apotransferrin, which binds two Fe3+ ions to generate Ferrotransferrin. Apotransferrin remains tightly bound to its receptor until the complex is recycled to the cell surface, where Apotransferrin is released into the extracellular space to recruit more Fe3+ ions.

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Synthetic peptide corresponding to aa 345-369 of human, mouse or rat adiponectin receptor 1 (AdipoR1).

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beta-Amyloid (25-35)

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Angiotensin I

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Synapsin I, II and III belong to a family of neuron-specific phosphoproteins which maintain a reserve pool of vesicles in the vicinity of the active zone by tethering synaptic vesicles to each other and to an Actin-based cytoskeleton meshwork. They have been shown to regulate neurotransmitter release in mature synapses and to accelerate development of the nervous system.

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Syntaxins are type II integral membrane proteins localized to membranes that regulate vesicle transport, protein maturation, and exocytosis. Syntaxin 1A resides in the nerve terminals of sensory neurons and nerve fibers reaching small blood vessels. Syntaxin 2 localizes to the apical plasma membrane and regulates epithelial-mesenchymal interactions. Syntaxin 6 is primarily localized to the trans-Golgi network, and partially co-localizes with AP-1 on clathrin-coated membranes. Syntaxin 13 is ubiquitously expressed and localizes to the tubular early and recycling endosomes, as well as endosomal vacuoles.

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NOS inhibitor

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Produced in E. coli.

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Produced in E. coli. The extracellular domain of human TRAIL (aa 95-281) is fused at the N-terminus to a His-tag and a linker peptide. The active multimeric conformation is stabilized by an inserted mutation allowing an additional CC-bridge.

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Isolated from human rheumatoid synovial fibroblasts. Requires activation.

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Produced in E. coli.

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Control peptide for L-JNKI

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Produced in E. coli. Active human granzyme K.

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Negative control for Fc chimeric proteins