12523 Ergebnisse für: "ENZO LIFE SCIENCES"

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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.

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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.

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Rat lipocalin-2 is also called rat NGAL, as it is the ortholog of human neutrophil gelatinase-associated lipocalin (NGAL). Rat NGAL is a 25-kDa alpha 2-microglobulin-related protein or neu-related lipocalin. It is expressed by neutrophils and various epithelial cells, including cells of the renal proximal tubules. It is involved in physiological processes such as the binding of siderophore iron and tissue growth and regeneration. It is upregulated in a variety of pathological situations including infection, inflammation, ischemia-reperfusion and in certain adenocarcinomas.

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Anti-GHRL Mouse Monoclonal Antibody [clone: 45]

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Anti-HSP90A Mouse Monoclonal Antibody [clone: K41009]

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Anti-HSP90B1 Rabbit Polyclonal Antibody

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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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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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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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Cysteine string protein (CSP) is a 34 kDa rat brain protein localized to the cytoplasmic surface of the synaptic vesicle. CSP is believed to perform similar functions in the assembly of synaptic vesicle proteins which are essential to membrane trafficking.

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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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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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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.

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VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif
b) a more divergent proline-rich central domain (which is responsible for profilin binding)
c) a conserved C-terminal EVH2 domain.

VASP is expressed in a variety of mammalian cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.

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Host: Goat

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Host: Rabbit

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Anti-VDAC Rabbit Polyclonal Antibody

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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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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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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.

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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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Host: Mouse, Isotype: IgG

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Fas/APO-1/CD95 is a 36 kDa cell surface type I-membrane glycoprotein with an apparent molecular weight of 44 kDa on SDS-PAGE.  Fas belongs to the tumor necrosis factor receptor (TNFR) family, which includes TNFR1, TNFR2, CD27, CD30 and CD40.  Binding of Fas-ligand (FasL) to Fas or crosslinking of Fas by anti-Fas monoclonal antibodies leads to apoptosis of Fas expressing cells.  Both Fas and TNFR contain a 70 amino acid cytoplasmic “death domain” responsible for transmitting signals for apoptosis.  Apoptosis induced by Fas-Fas ligand interaction is inhibited by a number of cytosolic factors such as the ICE/CED3 family inhibitor CrmA, and the short and long forms of FLIP. Insertion of an early transposable element in intron 2 of the Fas gene, as in the mouse lpr mutations, causes lymphoproliferation and autoimmunity in mutant mice, suggesting the involvement of Fas in clonal deletion of autoreactive T cells.

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TAP1 and TAP2 are two structurally related subunits of the Transporter associated with antigen processing (TAP). The TAP complex is a member of the ATP binding cassette (ABC) family of transmembrane transporters. The TAP transporter is an essential component of the MHC class I antigen presentation pathway by binding peptides in its cytosolic part and subsequently translocating the peptides into the lumen of the endoplasmic reticulum where assembly of MHC class I and pepide takes place.

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ASC (Apoptosis-associated speck-like protein containing a CARD domain) is a bipartite protein comprising two protein-protein interaction domains, a Pyrin domain (PYD) and a caspase recruitment domain (CARD). Proteins containing these domains play pivotal roles in regulating apoptosis and immune response pathways. Reported functions of ASC include apoptosis, activation of inflammatory caspases and regulation of NFκB.

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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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HGF/SF (Hepatocyte growth factor/Scatter factor) is a multifunctional heterodimeric polypeptide. It mediates the growth and scattering of various cell types, epithelial mesenchymal transition, the formation of tubules and lumens, and promotes angiogenesis. The ligand-receptor pair has also shown to be uniquely involved in most human solid tumors and to participate in tumor development, invasion, and metastasis.