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Artikel-Nr: (ABFRLF-PA0229)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0229
Beschreibung: Anti-G-CSF Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Artikel-Nr: (ABFRLF-PA0005)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0005
Beschreibung: Peroxiredoxin VI (Prx VI, 1-Cys Prx) is a member of Peroxiredoxin Family, an antioxidant enzyme that detoxifies reactive oxygen species and has a cysteine at their active site. Six isoforms (Prx I to VI) of Prx exist in all eukaryotic cells. These isoforms are classified into three subgroups (2-Cys, atypical 2-Cys, and 1-Cys). Prx VI modulates various receptor-signaling pathways and protects cells from cell death induced by oxidative stress. The active site cysteine(Cys47) is oxidized to cysteine sulfenic acid(Cys47-SOH) by H2O2. However, the resulting Cys47-SOH does not form a disulfide bond because of unavailability of another Cys-SH nearby. It can be reduced by nonphysiological thiols such as DDT but is not transformed by Thioredoxin/Thioredoxin Reductase or GSH. Occasionally, the sulfenic intermediate is hyperoxidized to sulfinic or sulfonic acid, resulting in inactivation of peroxidase activity.
UOM: 1 * 0,1 mL


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Artikel-Nr: (ABFRLF-PA0009)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0009
Beschreibung: Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-PA0059)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0059
Beschreibung: Check point kinase 1 (Chk1) is a serine / threonine protein kinase and a key mediator in the DNA damage-induced checkpoint network. Chk1 is an evolutionarily conserved protein kinase that functions to ensure genomic integrity upon genotoxic stress. When the G2 or S checkpoint is abrogated by the inhibition of Chk1, p53-deficient cancer cells undergo mitotic catastrophe and eventually apoptosis, whereas normal cells are still arrested in the G1 phase. Thus, Chk1 inhibitors can preferentially potentiate the efficacy of DNA damaging agents in cancer cells, and Chk1 is an attractive therapeutic target for cancer treatment, especially since approximately 50% of all human cancers are p53-deficient.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-PA0094)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0094
Beschreibung: Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGFAA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2– domaincontaining molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-PA0071)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-PA0071
Beschreibung: Signal transducer and activator of transcription (STAT), named after their dual role, are latent cytoplasmic transcription factors that mediate various biological responses. The activation of STAT proteins is largely mediated by phosphorylation of C-terminal transactivation domain through Janus kinases (JAKs) and mitogen-activated protein kinases (MAPKs), which allows the activated STATs to dimerize and to translocate into the nucleus. By modulating target gene expression, STAT proteins play an important role in mediating a broad range of biological processes such as cell proliferation, survival, apoptosis, and differentiation. Seven mammalian members of the STAT family are known (STAT1, 2, 3, 4, 5a, 5b, and 6) and they all share common features and structure. STAT3 is activated by growth factors and oncogenic kinases where it mediates transcriptional activation of genes encoding apoptosis inhibitors, cell-cycle regulators and inducers of angiogenesis.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0182)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0182
Beschreibung: Cytochrome c is a small heme protein consisting electron-transport chain in mitochondria and transfers electrons between complex III and IV. It is highly conserved through diverse species from unicellular microorganisms to animals and plants.
Cytochrome c is also an intermediate in apoptosis. Currently, it is widely accepted that mitochondria play a key role in the regulation of apoptosis. In mammalian cells, a major caspase activation pathway is the cytochrome c-initiated pathway. In this pathway, a variety of apoptotic stimuli cause cytochrome c release from mitochondria. In the cytosol, cytochrome c interacts with its adaptor molecule, Apaf-1, resulting in the recruitment, processing and activation of pro-caspase-9 in the presence of dATP or ATP. Caspase-9, in turn, cleaves and activates pro-caspase-3 and -7; these effector caspases are responsible for the cleavage of various proteins leading to biochemical and morphological features characteristic of apoptosis.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0114)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0114
Beschreibung: Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/ mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract. Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation. Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine. All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0087)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0087
Beschreibung: Ubiquitin+1 (Ub+1) is a novel mutant form of ubiquitin that can be produced through a process known as molecular frameshift. Ub+1 can be polyubiquitinated to produce aberrant polyubiquitin chains that inhibit the 26S proteasome. Especially ub+1 is accumulated in aggregates containing amyloid-β and phosphorylated-tau. Elevated expression of Ub+1 mRNA and protein has been observed in the brains of patients with Alzheimer's disease. Also ub +1 acts as an aggravating factor in polyglutamine-induced neuro-degeneration.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0263)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0263
Beschreibung: Vimentin is a member of the intermediate filament family of proteins found in various non-epithelial cells, especially mesenchymal cells. Vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Although most intermediate filaments are stable structures, vimentin also has a dynamic nature which is important when offering flexibility to the cell.
Two monomers which have central α-helical domains, capped on each end by non-helical domains twist around each other to form a coiled-coil dimer. Two dimers then form a tetramer, which, in turn, form a sheet by interacting with other tetramers.
There are some reports related to the biochemical function of intermediate filament network. The intracellular movement of LDL-derived cholesterol from the lysosome to the site of esterification is a vimentin-dependent process. A role for vimentin in mechanotransduction of shear stress has also been suggested. The mechanical stress of fluid shear on endothelial cells seems to trigger MAPK signaling pathways and stimulates proliferation.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0272)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0272
Beschreibung: The Smad family of proteins are functioning in the transmission of extracellular signals in the TGF-β signaling pathway. Binding of a TGF-β superfamily ligands to extracellular receptors triggers phosphorylation of Smad2 at a Serine-Serine-Methionine-Serine (SSMS) motif at its C-terminus. Phosphorylated Smad2 is then able to form a complex with Smad4. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.
In mammals, eight Smad proteins have been identified to date. The Smad family of proteins can be divided into three functional groups: the receptor-activated Smads (R-Smads), common mediator Smads (Co-Smads), and the inhibitory Smads (I-Smads). The R-Smads are directly phosphorylated by the activated type I receptors on their C-terminal Ser-Ser-X-Ser (SSXS) motif and include Smad1, Smad2, Smad3, Smad5, and Smad8. Smad2 and Smad3 are phosphorylated in response to TGF-β and activin, whereas Smad1, Smad5, and Smad8 are phosphorylated in response to BMP (Bone Morphogenetic Protein). This C-terminal phosphorylation allows R-Smad binding to Co-Smad, Smad4, and translocation to the nucleus where they regulate TGF-β target genes. Smad6 and Smad7 belong to the I-Smad which bind to the type I receptor or Smad4 and block their interaction with R-Smads.
The Smads share sequence similarities, most notably in the N-terminal and carboxy-terminal regions, referred to as the MH1 (Mad Homology 1) and MH2 domains respectively. Smad2 and Smad3 have 66% amino acid sequence identity between their MH1 domains and 96% amino acid sequence identity between their MH2 domains.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0317)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0317
Beschreibung: There are ten mitogen-activated protein kinase (MAPK) phosphatases
(MKPs) that act as negative regulators of MAPK activity in mammalian
cells.
MKP4(DUSP9) is a dual specificity phosphatase, which acts as a negative
regulator of insulin-stimulated pathways. MKP4 is expressed in kidney,
placenta and adipose tissue. MKP4, a cytosolic MKP with specificity to not
only Erk, but also, to a lesser extent, JNK and p38. MKP4 also reversed
the effect of TNF-a to inhibit insulin Signaling. MKP4 has a protective
effect against the development of insulin resistance through its ability to
dephosphorylate and inactivate crucial mediators of stress-induced insulin
resistance.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0248)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0248
Beschreibung: Cyclin-dependent kinase 7 (CDK7) has essential roles in the cell-division cycle as a CDK-activating kinase (CAK) and in the transcription as a component of the general transcription factor TFIIH.
This protein forms a trimeric complex with cyclin H and MAT1, which functions as a Cdk-activating kinase (CAK), phosphorylating cell-cycle CDKs. It is also an essential component of the transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of the largest subunit of Pol II. This protein is thought to serve as a direct link between the regulation of transcription and the cell cycle.
Embryonic stem cells (ESCs) shows a very unusual cell cycle structure, characterized by a short G1 phase and a high proportion of cells in S-phase. This is associated with a unique mechanism of cell cycle regulation by the activity of cyclin dependent protein kinase (Cdk). The unique cell cycle structure and mechanism of cell cycle control indicates that the cell cycle machinery plays a role in establishment or maintenance of the stem cell state.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0266)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0266
Beschreibung: Both Chk1 and Chk2 are critically important checkpoint kinases. Chk1 is essential for normal development and cell growth and Chk1 deficiency in mouse or in embryonic stem (ES) cells is lethal. Loss of Chk2 is tolerated and has been found to be associated with a subset of Li-Fraumeni cases. Li-Fraumeni syndrome increases greatly the susceptibility to cancer, with particularly high occurrences of breast cancer, brain tumors, acute leukemia, soft tissue sarcomas, bone sarcomas, and adrenal cortical carcinoma.
Chk2 regulates cell cycle checkpoints and apoptosis in response to DNA damage, particularly to DNA double-strand breaks. The cell either stops the cell cycle and therefore its proliferation until the damage is repaired, or it destructs itself (apoptosis).
The ataxia telangiectasia mutated (ATM) and ATR (ATM and Rad3-related) protein kinases exert cell cycle delay, in part, by phosphorylating Chk1, Chk2, and p53. Phosphorylation on Chk1 and p53 requires ATR, whereas phosphorylation on Chk2 requires ATM.
Screening of novel substrates of Chk1 and Ckh2 followed by imunoprecipitation kinase assay and site-directed mutagenesis analysis suggests that HDAC5 and PGC-1 are specific targets for Chk1 and/or Chk2 at least in vitro.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0277)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0277
Beschreibung: Hemoglobin (haemoglobin, Hb) is the iron-containing oxygen-transport protein in the red blood cells of vertebrates. Its chief physiological function is to transport oxygen from the lungs or gills to the tissues where it releases the oxygen for the cellular respiration.
Hb A (most of adult hemoglobin) is a tetrameric protein with a molecular weight of 64,500 Da, consisting of two identical α-chains of 141 amino acids each, and two identical β-chains of 146 amino acids each. Each subunit or chain of Hb A adopts a three dimensional structure, called the globin fold, similar to that of the related, monomeric protein myoglobin (Mb). This fold is an arrangement of the helices which forms a pocket that encloses and binds a heme prosthetic group which consists of an iron (Fe) ion held in a heterocyclic ring, known as a porphyrin.
The binding of oxygen is a cooperative process. The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule. the oxygen binding curve of hemoglobin is sigmoidal, or S-shaped, as opposed to the normal hyperbolic curve associated with noncooperative binding. Hemoglobin's oxygen-binding capacity is decreased in the presence of carbon monoxide because both gases compete for the same binding sites on hemoglobin. Carbon dioxide occupies a different binding site on the hemoglobin.
Some mutations in the globin chain are associated with the hemoglobinopathies, such as sickle-cell disease and thalassemia. Hemoglobin (Hb)-based O2 carriers (HBOCs) such as hemoglobin vesicle (HbV) have been investigated as a transfusion alternative and other clinical applications.
UOM: 1 * 0,1 mL


Artikel-Nr: (ABFRLF-MA0256)
Lieferant: AbFrontier
Hersteller Artikel Nummer : LF-MA0256
Beschreibung: Cyclin-dependent kinases (cdk) belong to a group of protein kinases originally discovered as being involved in the regulation of the cell cycle. Cdks are also involved in the regulation of transcription and mRNA processing. A Cdk is activated by association with a cyclin, forming a cyclin-dependent kinase complex.
Cdk1, also known as cell division control protein 2 (cdc2), is one of the components of the maturation promoting factor (MPF) which is essential for G1/S and G2/M phase transitions of eukaryotic cell cycle. Cdk1, when bound to cyclin B, allows a dividing cell to enter into mitosis from G2 and permits the transition from G1 through S in conjunction with cyclin A and cyclin E. The Cdk1 protein is constantly present throughout the cell division cycle, but its activity is finely tuned by means of protein-protein interactions and reversible phosphorylation.
Cdk1 can also enhance cell migration. Increased levels of Cdk1 promote cell migration together with cyclin B2 and the actin-stabilizing protein caldesmon. Phosphorylation of caldesmon bound to actin results in the displacement of caldesmon from actin followed by the altered interaction of actin with myosin. These events contribute to increased cell migration.
UOM: 1 * 0,1 mL


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