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Numéro de catalogue: (BOSSBS-1975R-CY3)

Fournisseur:  Bioss
Description:   Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-1975R-A555)

Fournisseur:  Bioss
Description:   Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.
UOM:  1 * 100 µl
Numéro de catalogue: (LEIH3808550E)

Fournisseur:  LEICA HISTOLOGY
Description:   These block banks are ideal for the long-term storage of paraffin blocks. These rigid steel cabinets will stack together or with the slide safe.
UOM:  1 * 1 ST
Numéro de catalogue: (BOSSBS-12260R-A350)

Fournisseur:  Bioss
Description:   The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity; or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven ?subunits each, and the inner two rings each consist of seven beta subunits.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   The UNC5H family of proteins act as transmembrane receptors for netrin-1 and play a crucial role in axon guidance and migration of neural cells. In fact, UNC5H receptors express widely in cells that migrate, where they bind the G protein G Alpha 1-2 to inhibit G protein signaling. Additionally, UNC5H receptors induce apoptosis when cleaved by a caspase, producing an intracellular fragment containing a death domain, but this activity is blocked by the binding of netrin-1. The expression of UNC5H receptors is down-regulated in multiple cancers, including colorectal, breast, ovary, uterus, stomach, lung, and kidney cancers. Hence, in the absence of netrin-1, UNC5H receptors act as tumor suppressors by inhibiting anchorage-independent growth and invasion, but mutation of these receptors provides a potential mechanism for tumorigenicity. UNC5H2, also designated unc-5 homolog B or p53-regulated receptor for death and life protein 1 (p53RDL1) is highly expressed in brain with lower levels of expression observed in developing lung, cartilage, kidney and hematopoietic and immune tissues.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12260R-A750)

Fournisseur:  Bioss
Description:   The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism. All of the subunits fall into one of two types: alpha subunits, which are structural, serve as docking domains for the regulatory particles and exterior gates blocking unregulated access to the interior cavity; or beta subunits, which are predominantly catalytic. The outer two rings in the proteasome consist of seven subunits each, and the inner two rings each consist of seven beta subunits.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   The UNC5H family of proteins act as transmembrane receptors for netrin-1 and play a crucial role in axon guidance and migration of neural cells. In fact, UNC5H receptors express widely in cells that migrate, where they bind the G protein G Alpha 1-2 to inhibit G protein Signalling. Additionally, UNC5H receptors induce apoptosis when cleaved by a caspase, producing an intracellular fragment containing a death domain, but this activity is blocked by the binding of netrin-1. The expression of UNC5H receptors is down-regulated in multiple cancers, including colorectal, breast, ovary, uterus, stomach, lung, and kidney cancers. Hence, in the absence of netrin-1, UNC5H receptors act as tumour suppressors by inhibiting anchorage-independent growth and invasion, but mutation of these receptors provides a potential mechanism for tumourigenicity. UNC5H2, also designated unc-5 homolog B or p53-regulated receptor for death and life protein 1 (p53RDL1) is highly expressed in brain with lower levels of expression observed in developing lung, cartilage, kidney and hematopoietic and immune tissues.
UOM:  1 * 100 µl
Fournisseur:  Tonbo Biosciences
Description:   The SK3 antibody reacts with human CD4, a 59 kDa protein which acts as a co-receptor for the T cell receptor (TCR) in its interaction with MHC Class II molecules on antigen-presenting cells. The extracellular domain of CD4 binds to the beta-2 domain of MHC Class II, while its cytoplasmic tail provides a binding site for the tyrosine kinase lck, facilitating the signaling cascade that initiates T cell activation. CD4, and co-receptors CCR5 and CXCR4, may also be utilized by HIV-1 to enter T cells. Human CD4 is typically expressed on thymocytes, some mature T cell populations such as Th17 and T regulatory (Treg) cells, as well as on dendritic cells. The SK3 antibody is widely used as a phenotypic marker for human CD4 expression, and has been reported to be cross-reactive with Rhesus and Cynomolgus CD4. This antibody does not block binding of alternative clone RPA-T4, suggesting that they recognize different epitopes.
Fournisseur:  Biotium
Description:   This MAb reacts with a CD32 (FcgRII) epitope distinct from that defined by MAb 8.26 and the epitope overlaps with that of MAb 7.30 (cluster 4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.
Fournisseur:  Biotium
Description:   This MAb reacts with a CD32 (FcgRII) epitope distinct from that defined by MAb 8.26 and the epitope overlaps with that of MAb 7.30 (cluster 4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.
Fournisseur:  Biotium
Description:   This MAb reacts with a CD32 (FcgRII) epitope distinct from that defined by MAb 8.26 and the epitope overlaps with that of MAb 7.30 (cluster 4). It displays a stronger reaction with Daudi than with U937 cells. The epitope is located in domain 2 of FcgRIIa. Its Fab'2 fragments block immune complex binding. CD32 (FcgRII) is a type 1 transmembrane glycoprotein that mediates several functions including phagocytosis, cytotoxicity, and immunomodulation as well as platelet aggregation. Three genes (A, B, and C) encode CD32 and at least 6 isoforms are generated via alternative mRNA splicing, i.e., IIa1, IIa2, IIb1, IIb2, IIb3 and IIc. Monocytes/macrophages, placental trophoblasts and endothelial cells express all isoforms. In addition, the IIb isoform is expressed by B cells, and the IIa isoform by platelets, granulocytes and, weakly, by B cells. NK cells and neutrophils express Isoform IIc. CD32 binds weakly to the Fc region of monomeric IgG but more strongly to IgG aggregates and immune complexes.

Fournisseur:  Bioss
Description:   Semaphorins are a family of cell surface and secreted proteins that are conserved from insects to humans. Members of this family of proteins are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin” domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. Secreted and cell-bound semaphorins chemically attract and repel the growth of neural axons, guiding the development of intricate networks of neural tissue. SEMA4B (semaphorin-4B), also known as SemC or SEMAC, is an 832 amino acid single-pass type I membrane protein that belongs to the semaphorin family and exists as two alternatively spliced isoforms. Containing one Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a single sema domain, SEMA4B is encoded by a gene located on human chromosome 15.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Plasmodium falciparum is a protozoan parasite that causes malaria. It exhibits considerable antigenic heterogeneity which may be a major problem in developing an effective vaccine against malaria. The S-antigen of Plasmodium falciparum is a highly diverse, heat stable protein that is located in the parasitophorous vacuole of the mature asexual intraerythrocytic parasite. The S-antigen gene consists of multiple alleles that originate from the same chromosome site. The amino acid sequence of each allele contains a large central section of tandemly arranged, nearly identical peptides that are specific to each allele. Thus, directed against the repeat region of a particular allele can be used to define the serotype of an S-antigen. Flanking the central repeat block are two short regions of non-repetitive sequence which occur in four different forms, each of which is utilized to define a single S-antigen family. Comparison of the four S-antigen families reveals t hat they differ considerably from each other with variation being most pronounced in the C-terminal-flanking region.
UOM:  1 * 100 µl
Fournisseur:  Biotium
Description:   Recognizes a 53 kDa protein, which is identified as p53 suppressor gene product. It reacts with the mutant as well as the wild form of p53. Its epitope maps within the N-terminus (aa 37-45) of p53. Monoclonal antibody PAb1801 does not block the binding of DO-7 MAb to p53 in an ELISA test. p53 is a tumor suppressor gene expressed in a wide variety of tissue types and is involved in regulating cell growth, replication, and apoptosis. It binds to MDM2, SV40 T antigen and human papilloma virus E6 protein. Positive nuclear staining with p53 antibody has been reported to be a negative prognostic factor in breast carcinoma, lung carcinoma, colorectal, and urothelial carcinoma. Anti-p53 positivity has also been used to differentiate uterine serous carcinoma from endometrioid carcinoma as well as to detect intratubular germ cell neoplasia. Mutations involving p53 are found in a wide variety of malignant tumors, including breast, ovarian, bladder, colon, lung, and melanoma.
Fournisseur:  Corning
Description:   Le système d'inserts de plaques 96 multi-puits Corning® FluoroBlok™ HTS est une plateforme de tests de culture cellulaire conçue pour l'automatisation. Le boîtier des inserts en une seule pièce et la membrane microporeuse de protection contre la fluorescence (disponible en taille de pore 3,0 et 8,0 µm) permettent d'augmenter l'efficacité, la productivité et le rendement dans le processus de détection de médicaments. La conception de la plaque réceptrice minimise la contamination entre les puits.
Numéro de catalogue: (BOSSBS-1730R)

Fournisseur:  Bioss
Description:   Src (also known as pp60src) is a non receptor Tyrosine Kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. There are two critical phosphorylation sites of tyrosine on Src, tyrosine 418 and tyrosine 529 (referring to human Src sequence). The tyrosine 418 is located in the catalytic domain and is one of the autophosphorylation sites. Full catalytic activity of Src requires phosphorylation of tyrosine 418. The tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of tyrosine 418 at the catalytic domain, thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylated and Src becomes active. Src is a proto oncogene that may play a role in the regulation of embryonic development and cell growth. Mutations in this gene could be involved in the malignant progression of colon cancer. Immunogen: Synthetic peptide (Human) derived from the region of Src that contains tyrosine 529, based on the human sequence. The sequence is conserved in mouse (tyrosine 534), chicken (tyrosine 527) and frog (tyrosine 525).
UOM:  1 * 100 µl
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