You Searched For: Enzo Life Sciences

Catalog Number: (CA101106-236)

Supplier: Enzo Life Sciences

Description: Prostaglandin F2alpha (PGF2alpha) is formed in a variety of cells from PGH2, which itself is synthesized from arachidonic acid by the enzyme prostaglandin synthetase. PGF2alpha is often viewed as an antagonist to PGE2 due to their opposing effects on various tissues. PGF2alpha is a potent bronchoconstrictor and has been implicated in asthma attacks. PGF2alpha is also involved in reproductive functions including corpus luteum regulation, uterine contractions, and sperm motility. This has led to its use in terminating pregnancies and inducing labor at term. High levels of PGF2alpha have also been associated with preeclampsia.

Catalog Number: (CA101410-454)

Supplier: Enzo Life Sciences

Description: Smac/DIABLO is one of the pro-apoptotic proteins normally found in the intermembrane space of the mitochondria. In response to apoptotic stimuli, Smac/DIABLO is released into the cytosol resulting in permeabilization of the mitochondrial membrane. Cytosolic Smac/DIABLO activates caspase-9 by binding IAP proteins. Changes in the expression level of Smac/DIABLO have been demonstrated in a number of human cancers including melanoma, ovary, and prostate.

Catalog Number: (CA101410-458)

Supplier: Enzo Life Sciences

Description: The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.

Catalog Number: (CA95052-778)

Supplier: Enzo Life Sciences

Description: AP substrate.

Supplier: Enzo Life Sciences

Description: 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.

Supplier: Enzo Life Sciences

Description: Glycogen Synthase Kinase 3β (GSK-3β) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/AKT phosphorylates GSK-3β on serine 9, which prevents GSK-3β from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3β is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3β. The phosphorylated serine binds to the GSK-3β priming phosphate position and prevents binding of alternative substrates. In addition to insulin signaling, GSK-3β participates in the Wnt signaling pathway, where it forms a complex with axin, beta-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3β is unable to phosphorylate beta-catenin, which leads to stabilization of beta-catenin. The Wnt pathway inactivates GSK-3β via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3β with axin, beta-catenin, and APC. Clinically, there is considerable interest in GSK-3β inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.

Catalog Number: (CA200062-046)

Supplier: Enzo Life Sciences

Description: 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.

Catalog Number: (CA101410-450)

Supplier: Enzo Life Sciences

Description: 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.

Catalog Number: (CA200063-280)

Supplier: Enzo Life Sciences

Description: 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.

Supplier: Enzo Life Sciences

Description: 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.

Supplier: Enzo Life Sciences

Description: 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

Description: 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.

Supplier: Enzo Life Sciences

Description: 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.

Catalog Number: (CA95046-240)

Supplier: Enzo Life Sciences

Description: 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.

Catalog Number: (CA200061-472)

Supplier: Enzo Life Sciences

Description: 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.

Supplier: Enzo Life Sciences

Description: 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.