You Searched For: Enzo Life Sciences

Catalog Number: (CA200061-476)

Supplier: Enzo Life Sciences

Description: Osteopontin (OPN) is an acidic extracellular matrix cell adhesion protein that is relatively abundant not only in bone matrix, plasma, urine, and milk, but is also found in malignant and atherogenic tissues. Phosphorylation, glycosylation and calcium modifications allow intact and fragmented Osteopontin to direct a variety of diverse responses including tissue remodeling, inflammation and cell survival. Plasma Osteopontin has been shown to provide prognostic information in breast, prostate, colon, and lung cancers as well as metastatic carcinomas. The notable presence of Osteopontin in a variety of tumors is strongly correlated to pathological stage, suggesting its critical role in tumor invasiveness, progression and metastasis. In addition, Osteopontin inhibits inducible nitric oxide synthase activity, thereby protecting tumor cells from NO-mediated macrophage cytotoxic attack. Osteopontin is found in atherosclerotic plaques and may drive a number of diabetic vascular pathologies.

Catalog Number: (CA200061-504)

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: (CA200061-512)

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.

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: (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: (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.

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.

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: (CA101410-456)

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.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock proteins 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: (CA200062-766)

Supplier: Enzo Life Sciences

Description: The 90kDa 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 1-2% 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.

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: Synaptotagmins (Syt) are membrane-trafficking proteins characterized by an N-terminal transmembrane region, a variable linker, and two C-terminal C2-domains, C2A and C2B. At least twelve Synaptotagamins are expressed in vertebrates and can be found in both vesicular and plasma membranes.

Supplier: Enzo Life Sciences

Description: Hsp70-Hsp90 Organizing Protein (HOP, p60) is an ~60kDa protein that is a critical intermediate component for the efficient maturation of steroid receptor complexes, serving to recruit Hsp90 to Hsp70-containing complexes. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a, and TPR2b.

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.