You Searched For: (2,4-Dinitrophenyl)acetic acid

Catalog Number: (CA95046-454)

Supplier: Enzo Life Sciences

Description: N-ethylmaleimide-sensitive factor (NSF) is involved in a variety of membrane fusion events and plays a prominent role in synaptic vesicle fusion. In order to interact with target membranes, NSF requires another set of soluble proteins called Soluble NSF attachment proteins (SNAPs). Together with synaptotagmin and alpha-SNAP, NSF modulates the interaction of SNAP25, VAMP, and syntaxin in an ATP-dependent manner to form a 20S complex involved in synaptic vesicle docking and fusion.

Catalog Number: (CA200062-418)

Supplier: Enzo Life Sciences

Description: Cleavage of heme b (Fe-protoporphyrin IX) at the a-methene carbon bridge to form the open tetrapyrrole, biliverdin IXa and carbon monoxide (CO) is catalyzed by heme oxygenase (HO) isozymes HO-1 and HO-2 (heme hydrogen-donor: oxygen oxidoreductase; EC 1.14.99.3). In mammalian species, biliverdin reductase (BVR; bilirubin: NAD(P)+ oxidoreductase; EC 1.3.1.24) converts the open tetrapyrrole to bilirubin. This pathway represents the only efficient way of making bilirubin and thereby deterring activation of oxygen by the heme molecule. HO-1 belongs to the heat shock protein family (Hsp32), while HO-2 takes a constitutive form expressed at exceedingly high levels in the brain and testes. The end products of the heme degradation process carry out important physiological activities. CO may act as a messenger in the brain and systemic organs stimulating cGMP-production through interactions with the heme-dependent form of guanylate cyclase. Bile pigments display potent antioxidant activity as well as effective antiviral activity against HIV and herpes virus. BVR is unique among all enzymes characterized to date in having two pH optima (6.8 and 8.7), using a different cofactor at each pH range (NADH at pH 7.0 and NADPH at pH 8.7). The enzyme displays pI and molecular mass microheterogeneity, apparently a result of post translational modifications. In rat, the enzyme also shows a tissue specific developmental pattern. BVR is not inactivated by heat shock, and its preexisting message is not sequestered from translation subsequent to thermal stress. Furthermore, reductase preserves microheterogeneity under thermal stress. BVR expression occurs not only in cells and brain regions that already display HO-1 and HO-2, but also in regions and cell types with potential to induce stress proteins. Rat cDNA for BVR has been isolated and characterized. The deduced protein contains 3 cysteine residues (Cys73, Cys281, and Cys290) involved in cofactor and substrate binding. Human BVR consists of a substantially longer polypeptide than the rat enzyme (41-42 kDa vs. 33 kDa), but also is dual cofactor and dual pH dependent, requires free SH groups for activity, and displays pI and molecular mass microheterogeneity. The human and rat BVR share some antigenic epitopes and show immunochemical cross reactivity.

Catalog Number: (CA200062-334)

Supplier: Enzo Life Sciences

Description: TAK1 (TGF-beta-activated kinase-1) is a 65 kDa serine/threonine kinase that is a member of the MAPKKK family. TAK1 is involved in the regulation of transcription by the TGF-beta super family, as its kinase activity is stimulated by TGF-beta and bone morphogenetic protein (BMP).

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.

Supplier: Enzo Life Sciences

Description: Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Supplier: Enzo Life Sciences

Description: Ubiquitin (Ub) plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to Ub and the ubiquinated protein is then selectively degraded by the 26S complex, a multicatalytic cytosolic and nuclear protease. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.

Catalog Number: (CA200063-102)

Supplier: Enzo Life Sciences

Description: In mammals, cyclin B associates with inactive p34cdc2 which facilitates phosphorylation of p34cdc2 at aa 14-Thr and 15-Tyr. This maintains the inactive state until the end of G2-phase. The inactive cyclin B-p34cdc2 complex continues to accumulate in the cytoplasm until the completion of DNA synthesis, when Cdc25, a specific protein phosphatase, dephosphorylates aa 14-Thr and 15-Tyr of p34cdc2 rendering the complex active at the G2/Mboundary. This mitotic kinase complex remains active until the metaphase/anaphase transition when cyclin B is degraded. This degradation process is ubiquitin-dependent and is necessary for the cell to exit mitosis. Therefore cyclin B-p34cdc2 plays a critical role in G2 to M transition.

Catalog Number: (CA200063-244)

Supplier: Enzo Life Sciences

Description: The 104 kDa yeast heat shock protein (Hsp104) is a cytosolic member of the Hsp100 family of proteins. Hsp104 cooperates with Hsp40 and Hsp70 co-chaperones in yeast in the reactivation of heat-damaged proteins. Hsp104 is also critical for the establishment and maintenance of the [PSI] prion phenotype in Saccharomyces cerevesiae.

Catalog Number: (CA101106-226)

Supplier: Enzo Life Sciences

Description: Progesterone is the major female sex hormone, and is responsible for reproductive-related activities such as breast glandular development, the endometrial aspects of the menstrual cycle, and the establishment and maintenance of pregnancy. In addition, progesterone also directs pregnancy support physiology including changes in carbohydrate, protein and lipid metabolism, thermoregulation, sodium reabsorption in renal tubules and the reduction of alveolar and atrial carbon dioxide partial pressures (PCO2). Progesterone is secreted in large amounts by the corpus luteum and by the extracellular conversion of cholesterol, cholestryl esters, adrenal steroids, prenenolone and pregnenolone sulfate. Small quantities are also secreted directly from the adrenal glands.

Supplier: Enzo Life Sciences

Description: 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

Description: p23 is a ubiquitous, highly conserved co-chaperone for Hsp90 that participates in the folding of a number of cell regulatory proteins including progesterone and glucocorticoid receptors, HSF1, and telomerase. p23 is thought to modulate Hsp90 activity in the last stages of the chaperoning pathway by binding and stabilizing Hsp90 in its ATP-bound state.

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: (CA95046-292)

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.

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.

SDS

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.

Catalog Number: (CA95045-858)

Supplier: Enzo Life Sciences

Description: The Akt (PKB) family of protein kinases are serine/threonine kinases, with three mammalian family members identified to date (Akt1, Akt2, Akt3). Akt is a well-characterized member of PI3 kinase-mediated signaling pathways, regulating cell growth, apoptosis, glycogen synthesis, and other cellular responses through its phosphorylation of downstream substrates. Akt activation is triggered by binding of phospholipid and phosphorylation at two key residues: Thr308 by PDK1, and Ser473 by PDK2, now identified as mTOR. Deregulation of Akt signaling has been associated with cancer, diabetes, and schizophrenia. Akt1 is the cellular homologue of the murine thymoma retroviral oncogene v-akt, and its role in anti-apoptotic and pro-mitotic pathways have made Akt a molecular target for anti-cancer therapeutic intervention. Akt activation inhibits apoptosis by phosphorylating the Bcl-2 related protein Bad, and increases p53 degradation by phosphorylating mdm2. Mitotic substrates of Akt include GSK-3β, p21CIP1, and p27KIP1, cell cycle inhibitors negatively regulated by Akt phosphorylation. Akt has been shown to mediate angiogenesis through regulation of thrombospondins, which may cooperate with pro-mitotic and anti-apoptotic functions of Akt to promote tumorigenesis.