14670 Results for: "ENZO LIFE SCIENCES"

Supplier: Enzo Life Sciences

Substrate for the smooth muscle myosin light chain kinase.

Supplier: Enzo Life Sciences

Excellent PKC substrate

Supplier: Enzo Life Sciences

PKC substrate

Supplier: Enzo Life Sciences

Receptor tyrosine kinase inhibitor

Supplier: Enzo Life Sciences

Semisynthetic (from GM2).

Supplier: Enzo Life Sciences

PKC inhibitor

Supplier: Enzo Life Sciences

D-myo-Inositol-1,4,5-trisphosphate trilithium salt ≥98% (by HPLC)

Supplier: Enzo Life Sciences

Fas-associating death domain containing protein (FADD)/MORT1 serves as a signal transducer of Fas-induced apoptosis. Through its amino-terminal death effector domain (DED), FADD binds to cytosolic proteins such as TRADD, a cytosolic death domaincontaining protein that asssociates with the cytosolic portion of TNF receptor, or MACH/FLICE/caspase-8, a protease with sequence homology to ICE-CED-3 protease family, in order to transduce the death signal.

Supplier: Enzo Life Sciences

Bad is an important regulatory protein involved in the control of cell survival and apoptosis, and is a member of the BH3-only family of proteins such as Bim and Bid that share homology with Bcl-2 only in the BH3 domain. Phosphorylated Bad is sequestered in the cytosol by 14-3-3 proteins under normal conditions, but is dephosphorylated and activated following apoptotic signals. Apoptotic stimuli induce Bad dephosphorylation by a number of phosphatases (e.g., calcineurin) and recruitment to the mitochondria, where Bad heterodimerizes with and inhibits prosurvival proteins of the Bcl family. In contrast, survival signals lead to phosphorylation of Bad at multiple serine residues, including phosphorylation at Ser112 and Ser136 which induce association with 14-3-3 proteins. Phosphorylation at Ser112 and Ser136 is required for a third phosphorylation event at Ser155, which induces dissociation of Bad/Bcl heterodimers to promote cell survival. This antibody specifically binds the Bad protein, but does not recognize Bad/Bcl-2 heterodimers in immunoprecipitation assays.

Supplier: Enzo Life Sciences

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).

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.

Supplier: Enzo Life Sciences

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).

Supplier: Enzo Life Sciences

Tumor necrosis factor alpha (TNF-α), also known as cachectin, is a 17.5 kDa 157 amino acid member of the TNF superfamily of cytokines that is a potent lymphoid factor with effects on a wide range of target cells. Active TNFalpha is produced in both soluble and membrane-anchored trimers by macrophages, NK cells, and T- and B-lymphocytes. TNF exerts proinflammatory signals via binding and inducing trimerization of TNF-receptor1 (TNF-R1) expressed on most normal and transformed cells, or to TNF-receptor 2 (TNF-R2), expressed on endothelial and most immune cells. TNF signaling regulates hematopeiesis, differentation, endothelial cell activation, apoptosis, lipid metabolism, tumor progression, and immune suveillance, and dysregulation of TNF or its receptors is implicated in numerous disease states including cancer, osteoporosis, autoimmune disease, diabetes, and atherosclerosis.

Supplier: Enzo Life Sciences

Endoplasmic reticulum protein (ERp) 72, a 72 kDa protein localized to the endoplasmic reticulum, is a member of the Protein Disulfide Isomerase (PDI) family of proteins. Together with other ER resident proteins such as BiP, GRP94, and PDI, they serve as the molecular chaperones for proper folding of newly translocated and glycolsylated proteins such as Thyroglobulin (Tg) and Human chorionic gonadotropin (hCG)-beta.

Supplier: Enzo Life Sciences

Anti-ESR Mouse Monoclonal Antibody [clone: h-151]

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

Neuronal and autophagy detection in yeast detection.

Supplier: Enzo Life Sciences

This kit provides a rapid assay for nuclear condensation, a prominent hallmark of apoptosis.A highly permeable green-emitting dye for enhanced detection of apoptosis-induced chromatin condensation.

Supplier: Enzo Life Sciences

Zinc dye

Supplier: Enzo Life Sciences

Calcium dye

Supplier: Enzo Life Sciences

Calcium dye

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.

Supplier: Enzo Life Sciences

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

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

DnaJ is a basic 41 kDa E. coli Heat shock protein which belongs to the molecular chaperone class of proteins. Bacterial DnaJ protein acts synergistically with the bacterial chaperone DnaK (Hsp70 homologue) and the other co-chaperone GrpE in suppressing eukaryotic and prokaryotic polypeptide aggregation, facilitating protein translocation through intracellular compartments or protein secretion, reactivating some partially aggregated enzymes, and activating pre-priming complex during initiation of DNA replication.

Supplier: Enzo Life Sciences

Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

Supplier: Enzo Life Sciences

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

The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.