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Fournisseur:  Biotium
Description:   Recognizes a protein of 80 kDa-90 kDa, identified as CD36 (Workshop IV; Code P-26). Its epitope maps between aa155-183. It is expressed on platelets, monocytes and macrophages, microvascular endothelial cells, erythrocyte precursors, mammary epithelial cells, and some macrophage derived dendritic cells. CD36 acts as a receptor for thrombospondin (TSP), collagen types I, IV and V, P. falciparum malaria-infected erythrocytes, and sickle erythrocytes. It also functions as a scavenger receptor, mediating macrophage uptake of oxidized low-density lipoprotein (LDL) and recognition of apoptotic polymorphonuclear leukocytes (PMN). CD36 plays a role in platelet aggregation, macrophage foam cell development, inflammation, and the tissue ischemia observed in sickle cell disease and cerebral malaria. Note that 1-4% of Japanese and East Asia population lack CD36. This MAb blocks adhesion of P. falciparum parasitized red blood cells to CD36 and strongly inhibits collagen-induced platelet aggregation.
Fournisseur:  Biotium
Description:   Recognizes a protein of 80 kDa-90 kDa, identified as CD36 (Workshop IV; Code P-26). Its epitope maps between aa155-183. It is expressed on platelets, monocytes and macrophages, microvascular endothelial cells, erythrocyte precursors, mammary epithelial cells, and some macrophage derived dendritic cells. CD36 acts as a receptor for thrombospondin (TSP), collagen types I, IV and V, P. falciparum malaria-infected erythrocytes, and sickle erythrocytes. It also functions as a scavenger receptor, mediating macrophage uptake of oxidized low-density lipoprotein (LDL) and recognition of apoptotic polymorphonuclear leukocytes (PMN). CD36 plays a role in platelet aggregation, macrophage foam cell development, inflammation, and the tissue ischemia observed in sickle cell disease and cerebral malaria. Note that 1-4% of Japanese and East Asia population lack CD36. This MAb blocks adhesion of P. falciparum parasitized red blood cells to CD36 and strongly inhibits collagen-induced platelet aggregation.
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:   Recognizes a protein of 80 kDa-90 kDa, identified as CD36 (Workshop IV; Code P-26). Its epitope maps between aa155-183. It is expressed on platelets, monocytes and macrophages, microvascular endothelial cells, erythrocyte precursors, mammary epithelial cells, and some macrophage derived dendritic cells. CD36 acts as a receptor for thrombospondin (TSP), collagen types I, IV and V, P. falciparum malaria-infected erythrocytes, and sickle erythrocytes. It also functions as a scavenger receptor, mediating macrophage uptake of oxidized low-density lipoprotein (LDL) and recognition of apoptotic polymorphonuclear leukocytes (PMN). CD36 plays a role in platelet aggregation, macrophage foam cell development, inflammation, and the tissue ischemia observed in sickle cell disease and cerebral malaria. Note that 1-4% of Japanese and East Asia population lack CD36. This MAb blocks adhesion of P. falciparum parasitized red blood cells to CD36 and strongly inhibits collagen-induced platelet aggregation.
Numéro de catalogue: (BOSSBS-12578R-A680)

Fournisseur:  Bioss
Description:   BCL2 is an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants (alpha and beta) produced by alternate splicing, differ in their C-terminal ends. BCL2 suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. It regulates cell death by controlling the mitochondrial membrane permeability. It appears to function in a feedback loop system with caspases. BCL2 inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF1). It can form homodimers, and heterodimers with BAX, BAD, BAK and BclX(L). Heterodimerization with BAX requires intact BH1 and BH2 domains, and is necessary for anti-apoptotic activity. Also interacts with APAF1, RAF1, TP53BP2, BBC3, BCL2L1 and BNIPL.
UOM:  1 * 100 µl

Fournisseur:  Biotium
Description:   This antibody recognizes a protein of 30 kDa, identified as CD70. It is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This cytokine is a ligand for TNFRSF27/CD27. It is a surface antigen on activated, but not on resting, T- and B-lymphocytes. It induces proliferation of co-stimulated T cells, enhances the generation of cytolytic T cells, and contributes to T cell activation. This cytokine is also reported to play a role in regulating B-cell activation, cytotoxic function of natural killer cells, and immunoglobulin synthesis. This MAb blocks the interaction between CD27 and CD70, and has been shown toinhibit T cell proliferation induced by dendritic cells.
UOM:  1 * 50 µl

Fournisseur:  Bioss
Description:   Troponin I (TnI), along with troponin T (TnT) and troponin C (TnC), is one of 3 subunits that form the troponin complex of the thin filaments of striated muscle. TnI is the inhibitory subunit; blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains three genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. This gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in this gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).
UOM:  1 * 100 µl

Fournisseur:  Biotium
Description:   Recognizes a protein of 180 kDa, identified as CD11a (Leucocyte Workshop IV; Code 1524). CD11a complex with the 2 subunit of the integrin family, CD18, to form the cell surface heterodimer, LFA-1 or CD11a /C18 (aLbL). LFA-1 is expressed on all leukocytes including lymphocytes, monocytes, and granulocytes. It is involved in leukocyte adhesion to its ligands including intercellular adhesion molecule-1 (ICAM-1 or CD54), ICAM-2 (CD102), ICAM-3 (CD50) and Telencephalin (TLN) and play a role in most immune/inflammatory responses. This MAb potently blocks LFA-1 dependent homotypic cell aggregation.
UOM:  1 * 50 µl
Fournisseur:  Tonbo Biosciences
Description:   The 2.4G2 antibody is specific for a common epitope found in the extracellular regions of mouse Fc-receptors Fc-gamma II (CD32) and Fc-gamma III (CD16). As these are receptors for the Fc portion of mouse IgG, they may also bind laboratory antibody preparations and products used in a variety of cell analysis protocols such as flow cytometry, immunohistochemistry and functional cell assays. The 2.4G2 antibody is therefore widely used as a pre-treatment reagent to block binding of specific antibodies of interest, e.g. fluorescently conjugated antibodies, to Fc receptors via their Fc domains and contributing to “non-specific” staining.
Numéro de catalogue: (BOSSBS-11477R-A555)

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
Numéro de catalogue: (BOSSBS-11477R-A350)

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
Numéro de catalogue: (BOSSBS-11477R-A647)

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
Numéro de catalogue: (BOSSBS-7336R-A680)

Fournisseur:  Bioss
Description:   The Zyxin family of proteins contains five members: Ajuba, Limd1, LPP, TRIP6 and Zyxin. Limd1 (LIM domain-containing protein 1) is a ubiquitously expressed tumor suppressor containing 3 LIM zinc-binding domains. LIM domains consist of a cysteine-rich consensus sequence containing two distinct zinc-binding subdomains, which mediate protein-protein interactions. Limd1 interacts with the proteins SQSTM1, Rb, p62 and TRAF6. Limd1 was first identified when the deletion of its gene was noted in some cervical cancers. Limd1 blocks <i>in vitro</i> and <i>in vivo</i> tumor growth and is down-regulated in lung cancer. Limd1 may regulate osteoclast development under stressful conditions via its interactions with TRAF6 and p62.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-7336R-A350)

Fournisseur:  Bioss
Description:   The Zyxin family of proteins contains five members: Ajuba, Limd1, LPP, TRIP6 and Zyxin. Limd1 (LIM domain-containing protein 1) is a ubiquitously expressed tumor suppressor containing 3 LIM zinc-binding domains. LIM domains consist of a cysteine-rich consensus sequence containing two distinct zinc-binding subdomains, which mediate protein-protein interactions. Limd1 interacts with the proteins SQSTM1, Rb, p62 and TRAF6. Limd1 was first identified when the deletion of its gene was noted in some cervical cancers. Limd1 blocks in vitro and in vivo tumor growth and is down-regulated in lung cancer. Limd1 may regulate osteoclast development under stressful conditions via its interactions with TRAF6 and p62.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11493R-CY3)

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. Additionally, UNC5H receptors induce apoptosis when cleaved by a caspase, producing an intracellular fragment containing a death domain. This activity is blocked by the binding of netrin-1. 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. The expression of UNC5H receptors is down-regulated in multiple cancers, including colorectal, breast, ovary, uterus, stomach, lung, and kidney cancers. UNC5H3, also known as UNC5C, plays an important role in the development of spinal accessory motor neurons. It is also involved in mediating the repulsive action for netrin-1 and it serves as a stop signal for migratory cells.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-3773R-CY5.5)

Fournisseur:  Bioss
Description:   Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.
UOM:  1 * 100 µl
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