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block+heaters+
Numéro de catalogue:
(BOSSBS-5220R-A488)
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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13018R-A350)
Fournisseur:
Bioss
Description:
DNA polymerase activity is essential for replication, repair, recombination and mutagenesis. DNA polymerases can often bypass DNA lesions that block DNA replication, thereby allowing the replication of damaged DNA. One such DNA polymerase is the distributive enzyme DNA Pol i, which is encoded by the POLI gene. POLI is located on human chromosome 18q21.2, a region often implicated in the etiology of many human cancers. At thymine templates, DNA Pol i is highly error-prone when replicating undamaged DNA in that it favors the misincorporation of guanine over the correct nucleotide, adenosine. DNA Pol i also promotes the replication of damaged DNA by misincorporating deoxynucleotides opposite DNA lesions. DNA Pol i acts sequentially with DNA Pol Ω, which is essential for damage-induced mutagenesis, to complete the DNA lesion bypass. Therefore, replication involving DNA Pol i is likely to be highly mutagenic.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13018R-CY3)
Fournisseur:
Bioss
Description:
DNA polymerase activity is essential for replication, repair, recombination and mutagenesis. DNA polymerases can often bypass DNA lesions that block DNA replication, thereby allowing the replication of damaged DNA. One such DNA polymerase is the distributive enzyme DNA Pol i, which is encoded by the POLI gene. POLI is located on human chromosome 18q21.2, a region often implicated in the etiology of many human cancers. At thymine templates, DNA Pol i is highly error-prone when replicating undamaged DNA in that it favors the misincorporation of guanine over the correct nucleotide, adenosine. DNA Pol i also promotes the replication of damaged DNA by misincorporating deoxynucleotides opposite DNA lesions. DNA Pol i acts sequentially with DNA Pol Ω, which is essential for damage-induced mutagenesis, to complete the DNA lesion bypass. Therefore, replication involving DNA Pol i is likely to be highly mutagenic.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13508R-A647)
Fournisseur:
Bioss
Description:
G2A (for G2 accumulation) is a seven transmembrane G protein-coupled receptor that is upregulated in response to DNA damage and stress (1). G2A is predominantly expressed in hematopoietic tissues and in hematopoietic stem cells, and it is more highly detected in pro-B cells, while lower expression is observed in immature B cells and pre-B cells (1,2). G2A is expressed throughout T cell maturation, and it is further increased in response to T-cell activation (3). Ectopic expression of a G2A fusion protein in NIH/3T3 fibroblasts induces a cell cycle arrest that is consistent with a block at the G2/M transition (1,4). G2A is also able to attenuate the proliferative effects of Bcr-Abl, a chimeric tyrosine kinase oncogene, suggesting that G2A possesses anti-oncogenic properties (5). The amino acid sequence of G2A contains a destruction box motif that is consistently observed in cyclins, where it is required for ubiquitination and proteolytic degradation (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13508R-A350)
Fournisseur:
Bioss
Description:
G2A (for G2 accumulation) is a seven transmembrane G protein-coupled receptor that is upregulated in response to DNA damage and stress (1). G2A is predominantly expressed in hematopoietic tissues and in hematopoietic stem cells, and it is more highly detected in pro-B cells, while lower expression is observed in immature B cells and pre-B cells (1,2). G2A is expressed throughout T cell maturation, and it is further increased in response to T-cell activation (3). Ectopic expression of a G2A fusion protein in NIH/3T3 fibroblasts induces a cell cycle arrest that is consistent with a block at the G2/M transition (1,4). G2A is also able to attenuate the proliferative effects of Bcr-Abl, a chimeric tyrosine kinase oncogene, suggesting that G2A possesses anti-oncogenic properties (5). The amino acid sequence of G2A contains a destruction box motif that is consistently observed in cyclins, where it is required for ubiquitination and proteolytic degradation (6).
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
MAb B-R18 specifically recognizes CD95, also known as Fas, a transmembrane glycoprotein with a MW of 40-45 kDa, containing 8 kDa of N-glycosidic-linked polysaccharide. It is a receptor for TNFSF6/FASLG, a member of the nerve growth factor receptor/tumor necrosis factor superfamily, mediating receptor-triggered apoptosis. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation, which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). CD95 antigen is expressed on the surface of various cell types, preferentially on the CD45RAlow CD45ROhigh subset of memory T lymphocytes.
Fournisseur:
Biotium
Description:
This MAb reacts with a CD32 (FcgRII) epitope (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.
Numéro de catalogue:
(BOSSBS-15076R-A647)
Fournisseur:
Bioss
Description:
C1orf77, also known as Friend of PRMT1 protein, is a 248 amino acid protein that plays an essential role in the ligand-dependent activation of estrogen receptor target genes. C1orf77 is tightly associated with chromatin and is modified by both asymmetric and symmetric arginine methylation. Depletion of C1orf77 results in almost complete block of estradiol-induced promter occupancy by the estrogen receptor. Also, complete knockdown of C1orf77 mRNA in adult erythroid progenitors stongly induces fetal hemoglobin, suggesting that C1orf77 is a critical modulator of _-globin gene expression. There are two isoforms of C1orf77 that are produced as a result of alternative splicing events. The gene encoding C1orf77 maps to human chromosome 1, the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11480R-CY3)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins involved in neural development that are conserved from insects to humans. Members of this family 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. SEMA3E is a secreted semaphorin with 775 amino acids. Mutations in the SEMA3E gene are associated with CHARGE syndrome, a disorder characterized by cranial nerve dysfunction, coloboma of the eye, choanal atresia, inner and external ear abnormalities, cardiac anomalies, genitourinary abnormalities, and growth retardation.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a DQ antigen, which is a dimer of 60 kDa. The class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B Lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa. It is encoded by 5 exons; exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to four different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.This MAb strongly blocks cytotoxicity activity of T4-positive cytotoxic T cell clones.
Numéro de catalogue:
(BOSSBS-8413R)
Fournisseur:
Bioss
Description:
Galectin-12, also designated galectin-related inhibitor of proliferation 1 in mouse, is a 314 amino acid protein encoded by the human gene LGALS12. Galectin-12 is a member of the galectin family consisting of b-galactoside-binding proteins with conserved carbohydrate recognition domains. Galectin-12 binds lactose and may participate in the apoptosis of adipocytes. This protein is preferentially expressed in peripheral blood leukocytes and adipocytes. Galectin-12 is induced by cell cycle block at the G1 phase and causes G1 arrest when overexpressed. The galectin-12 gene is expressed in mouse preadipo-cytes and is upregulated when preadipocytes undergo cell cycle arrest, concomitant with acquisition of the competence to undergo differentiation in response to adipogenic hormone stimulation. Galectin-12 is an adipocyte-expressed protein which is downregulated by various insulin resistance-inducing hormones. As a result, galectin-12 may play a role in the pathogenesis of insulin resistance.
UOM:
1 * 100 µl
Fournisseur:
ENZO LIFE SCIENCES
Description:
Macrocyclic-triene antibiotic possessing potent immunosuppressant activity. It forms a complex with FKBP12 that binds to an effector, thus inhibiting IL-2 and other growth promoting lymphokines. The effectors were identified as FRAP (FKBP12 rapamycin-associated protein) and RAFT1 (rapamycin and KFBP12 target). Rapamycin/FKBP complex does not inhibit FRAP PI 4-kinase activity, but does inhibit FRAP autophosphorylation. Rapamycin induces inhibition of p70<sup>s6k</sup>, p33<sup>cdk2</sup> and p34<sup>cdc2</sup>. Selectively blocks signaling leading to the activation of p70/85 S6 kinase. Enhances apoptosis. Activator of autophagy both<i> in vitro</i> and <i>in vivo</i>.
Numéro de catalogue:
(BOSSBS-9022R-HRP)
Fournisseur:
Bioss
Description:
IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4700R-A647)
Fournisseur:
Bioss
Description:
Epstein Barr virus (EBV) is a member of the herpesvirus family and one of the most common human viruses. Most people become infected with EBV during their lives. Primary infections usually results in infectious mononucleosis (glandular fever) but the virus can also lay dormant in B lymphocytes and when reactivated become associated with more serious disease such as Burkitt's lymphoma, nasopharyngeal carcinoma and Hodgkin's disease. EBV latently infects B lymphocytes. Infected B cells express EBV nuclear antigens and latent proteins LMP1, LMP2A and LMP2B. LMP2A forms aggregates in the plasma membranes of B lymphocytes, where it functions as a negative regulator of the Src and Syk protein tyrosine kinases. Studies show that LMP2A blocks B-cell receptor (BCR) signal transduction in EBV immortalized B cells in vitro and may play an important role in maintaining a latent EBV infection within the peripheral blood B cells of infected individuals.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12577R-A555)
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
Numéro de catalogue:
(BOSSBS-3088R-A750)
Fournisseur:
Bioss
Description:
Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML.
UOM:
1 * 100 µl
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