5269 resultater for: "Enzo Life Sciences"

Supplier: Enzo Life Sciences

The p70 S6K activity kit is an efficient assay that utilizes little sample volume. This kit gives you the ability to an end-point or kinetic assay read-out in a convenient 96-well plate based assay and offers easy sample handling protocols. The assay also offers a high signal to background ratio.

Supplier: Enzo Life Sciences

Rap1, which is a member of the Ras family of GTP-binding proteins, cycles between an active GTP-bound and an unactive GDP-bound form that is mediated by GTPase activating protein (GAP). Rap1 is proposed to regulate Ras-mediated signaling and may also be involved in the regulation of Integrin-mediated cell adhesion although the mechanism of regulation is not known.

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SHPS-1 is a member of the gene family called the signal regulatory proteins of which there are at least fifteen members. SHPS-1 is a substrate of many activated tyrosine kinases such as Insulin receptor and EGFR, amongst others. SHPS-1 has regulatory effects on cellular responses induced by serum, growth factors, insulin, oncogenes, growth hormones and cell adhesion and plays a general role in different physiological and pathological processes.

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Cyclic GMP-dependent protein kinases (PKGs or cGKs) are classified into two types, PKGI and PKGII. Studies have shown that PKGs are highly homologous to PKAs; phosphorylation of cellular proteins by both families of kinases leads to alterations in calcium mobilization, protein phosphatase activity, ion channel function, gene transcription, smooth muscle contractility, and platelet aggregation.

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The Akt (PKB) family of protein kinases are serine/threonine kinases, with three mammalian family members identified (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.

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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.

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Acetylation and methylation of lysine are important post-translational modifications that regulate numerous protein-protein and protein-DNA interactions. Lysine acetylation and methylation involves the transfer of acetylCoA, or one or more methyl groups, to the e-amino group of lysine by modifying enzymes and cofactors. Histones and transcription factors are the primary targets of lysine acetylation and methylation, with either modification capable of inducing gene silencing or expression due to differential regulation of cofactors. For example, varying degrees of mono-, di-, and tri-methylation or acetylation of histone H3 at lysine residue 9 are known to demark distinct chromatin regions during various states of gene activation (methylation) or repression (acetylation).

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Protein phosphorylation is a complex biochemical process that is regulated by protein kinases that catalyze the transfer of the gamma-P of ATP to a recipient protein that acts as a substrate. This post-translational modification is primarily directed onto serine, threonine, and tyrosine amino acid residues within a protein. Changes in the phosphorylation status of phosphoproteins can alter their biological function, and aberrations in signal transduction cascades have been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders.

Supplier: Enzo Life Sciences

Produced in E. coli. Mouse Dkk-1 is fused at the N-terminus to a His-tag.

Supplier: Enzo Life Sciences

The Jurkat T lymphocyte cell line was established from the peripheral blood of a 14-year old boy with T cell leukaemia.

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.

Supplier: Enzo Life Sciences

The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

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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.

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Anti-KDEL Mouse Monoclonal Antibody [clone: 10C3]

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.

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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.

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Anti-GRP78 Rabbit Polyclonal Antibody

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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

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

Thioredoxin (Trx) is a redox protein of approximately 12 kDa. Its primary domain is conserved across a number of Trx family members and contains a conserved catalytic site Cys-Gly-Pro-Cys. It is ubiquitous and found in many organisms from bacteria to mammals. Trx has been shown to function in cell proliferation, redox signaling and inhibition of apoptosis.

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Synapse-associated proteins SAP97 and SAP102 display extensive sequence homology to the PSD 95 family of proteins that facilitate ion channel clustering at synaptic terminals. In addition to the CNS, SAP97 is also detected at the basal lateral membrane between a variety of epithelial cells. SAP102 associates with NMDA receptors through the C-terminal NR2B subunit of the receptor. The N-terminal SAP97 PDZ domain mediates its interaction with the synaptic ras-GTPase activating protein SynGAP.

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The tetrapeptide KDEL, located at the carboxy-terminal sequences of luminal proteins, is a retrieval motif essential for the precise sorting of these proteins along the secretory pathway. KDEL proteins perform essential functions in the endoplasmic reticulum (ER) related to protein folding as well as assembly. The localization of chaperones and other soluble proteins to the ER is achieved by their continuous retrieval from post-ER compartments by the KDEL receptor (Erd2p), which is a membrane protein localized in the Golgi apparatus.

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

Supplier: Enzo Life Sciences

Produced in E. coli.

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Produced in E. coli.

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Produced in E. coli.

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Negative control probe for in situ hybridization.

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The PATHO-GENE® HPV type 6/11 probe is a mixture of biotin-labeled HPV 6 and HPV 11-specific probes in buffered formamide and hybridisation enhancers.

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In Situ Hybridization Buffer provides a high quality hybridization medium for in situ hybridization analyses using either DNA or oligonucleotide probes labeled with biotin-, digoxigenin- or fluorescein-modified nucleotides.

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Host: Mouse, Isotype: IgG1