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Masterflex+Single-use
Numéro de catalogue:
(BOSSBS-9937R-A750)
Fournisseur:
Bioss
Description:
C11orf24, also known as DM4E3, is a 449 amino acid single-pass type I membrane protein that is expressed in brain, lung, skeletal muscle, kidney, spleen, prostate, testis, ovary and small intestine, with highest expression in heart, placenta, liver, pancreas and colon, and low expression in thymus and leukocytes. C11orf24 is encoded by a gene located on human chromosome 11, which consists of approximately 135 million base pairs and 1400 genes. Chromosome 11 makes up around 4% of human genomic DNA and is considered a gene and disease association dense chromosome. The chromosome 11 encoded Atm gene is important for regulation of cell cycle arrest and apoptosis following double strand DNA breaks. Atm mutation leads to the disorder known as ataxia-telangiectasia. The blood disorders Sickle cell anemia and _ thalassemia are caused by HBB gene mutations. Wilms' tumours, WAGR syndrome and Denys-Drash syndrome are associated with mutations of the WT1 gene. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are also associated with defects in chromosome 11.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5039R-FITC)
Fournisseur:
Bioss
Description:
Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells and is essential for the normal catabolism of triglyceride-rich lipoprotein constituents.ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. Defects in ApoE are a cause of hyperlipoproteinemia type III due to increased plasma cholesterol and triglycerides levels which are the consequence of impaired clearance of chylomicron and VLDL remnants.Summary: Chylomicron remnants and very low density lipoprotein (VLDL) remnants are rapidly removed from the circulation by receptor-mediated endocytosis in the liver. Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells. ApoE is essential for the normal catabolism of triglyceride-rich lipoprotein constituents. The APOE gene is mapped to chromosome 19 in a cluster with APOC1 and APOC2. Defects in apolipoprotein E result in familial dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III), in which increased plasma cholesterol and triglycerides are the consequence of impaired clearance of chylomicron and VLDL remnants. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7100R-CY3)
Fournisseur:
Bioss
Description:
RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.
Numéro de catalogue:
(BNUM0148-50)
Fournisseur:
Biotium
Description:
This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-7100R)
Fournisseur:
Bioss
Description:
RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11959R-A647)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11959R-HRP)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11959R-A555)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5693R-A647)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4182R-A488)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4182R-A555)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BTIUBNUM0993-50)
Fournisseur:
Biotium
Description:
This antibody neutralizes TNF alpha biological activities. It prevents TNF alpha induced apoptosis in Jurkat cells. It also neutralizes HurTNFamediated cytotoxicity of L929 cells and inhibits tumor growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production.
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
This antibody neutralizes TNF alpha biological activities. It prevents TNF alpha induced apoptosis in Jurkat cells. It also neutralizes HurTNFamediated cytotoxicity of L929 cells and inhibits tumor growth in mice. It protects mice against toxicity of HurTNFa. Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production.
Numéro de catalogue:
(BOSSBS-1210R-A488)
Fournisseur:
Bioss
Description:
Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1210R-A555)
Fournisseur:
Bioss
Description:
Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180).
UOM:
1 * 100 µl
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