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Fournisseur:  Biotium
Description:   This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. In Western blotting of cell lysates from 7 human breast cancer cell lines (ZR75-1, ZR75-30, MCF-7, MDAMB453, T47D, CAL51, 734B), the antibody labels a single band corresponding to p27Kip1. It functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. Reportedly, low p27 expression has been associated with unfavorable prognosis in renal cell carcinoma, colon carcinoma, breast carcinomas, non-small-cell lung carcinoma, hepatocellular carcinoma, multiple myeloma, and lymph node metastases in papillary carcinoma of the thyroid, as well as a more aggressive phenotype in carcinoma of the cervix.
Numéro de catalogue: (BOSSBS-11468R-A350)

Fournisseur:  Bioss
Description:   Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo-A, -B and -C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilization. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11468R-CY5)

Fournisseur:  Bioss
Description:   Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo-A, -B and -C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilization. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   FGFRL1 is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11400R-CY3)

Fournisseur:  Bioss
Description:   May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo A, B and C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilisation. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13028R-CY3)

Fournisseur:  Bioss
Description:   Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP10 (dipeptidyl-peptidase 10), also known as DPRP3 (dipeptidyl peptidase IV-related protein 3), DPL2 or DPPY, is a non-functional dipeptidyl peptidase which can bind to the potassium channels KV4.1 and KV4.2. It is a single-pass type II membrane protein expressed in spinal cord, adrenal glands, pancreas and brain tissues and may act as a modulator for cell surface expression and activity of KV4.1 and KV4.2.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13028R)

Fournisseur:  Bioss
Description:   Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP10 (dipeptidyl-peptidase 10), also known as DPRP3 (dipeptidyl peptidase IV-related protein 3), DPL2 or DPPY, is a non-functional dipeptidyl peptidase which can bind to the potassium channels KV4.1 and KV4.2. It is a single-pass type II membrane protein expressed in spinal cord, adrenal glands, pancreas and brain tissues and may act as a modulator for cell surface expression and activity of KV4.1 and KV4.2.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13721R)

Fournisseur:  Bioss
Description:   The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including beta-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT4 (FAT tumor suppressor homolog 4), also known as FAT-J, CDHF14 or CDHR11, is a 4,981 amino acid single-pass type I membrane protein that belongs to the protocadherin subfamily of cadherins and localizes to the primary cilia of kidney. Widely expressed, FAT4 contains thirty-four cadherin domains, six EGF-like domains and two laminin G-like domains. FAT4 may function in the regulation of planar cell polarity.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11898R-CY7)

Fournisseur:  Bioss
Description:   NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-9507R-A555)

Fournisseur:  Bioss
Description:   Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-9507R-A488)

Fournisseur:  Bioss
Description:   Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM:  1 * 100 µl
Numéro de catalogue: (BWTEQT-PCB-K1)

Fournisseur:  BW TECHNOLOGIES GMBH
Description:   Accessoires pour systèmes de détection de gaz, Pour: Quattro, Replacement PCB with sensor set
UOM:  1 * 1 ST
Numéro de catalogue: (BOSSBS-11592R-A647)

Fournisseur:  Bioss
Description:   Acetyltransferases and deacetylases are protein groups most often associated with oncogenesis and cell cycle regulation. NAT-8B (N-acetyltransferase 8B), also known as CML2 (camello-like protein 2), is a 227 amino acid single-pass membrane protein that is implicated in gastrulation regulation. A member of the camello family, NAT-8B contains one N-acetyltransferase domain and is encoded by a gene that maps to human chromosome 2p13.2. The NAT-8B gene is susceptible to a nonsense mutation at Serine 16, which leads to a stop codon and subsequently, a non-functional protein that is truncated in length. Similarly, a nonsense mutation at Glutamine 168 is thought to lead to a non-functional protein, as it causes the N-acetyltransferase to become disrupted. Human chromosome 2 consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. A number of genetic diseases are linked to genes on chromosome 2 including Harlequin icthyosis, sitosterolemia and Alstré°‰ syndrome.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Acetyltransferases and deacetylases are protein groups most often associated with oncogenesis and cell cycle regulation. NAT-8B (N-acetyltransferase 8B), also known as CML2 (camello-like protein 2), is a 227 amino acid single-pass membrane protein that is implicated in gastrulation regulation. A member of the camello family, NAT-8B contains one N-acetyltransferase domain and is encoded by a gene that maps to human chromosome 2p13.2. The NAT-8B gene is susceptible to a nonsense mutation at Serine 16, which leads to a stop codon and subsequently, a non-functional protein that is truncated in length. Similarly, a nonsense mutation at Glutamine 168 is thought to lead to a non-functional protein, as it causes the N-acetyltransferase to become disrupted. Human chromosome 2 consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. A number of genetic diseases are linked to genes on chromosome 2 including Harlequin icthyosis, sitosterolemia and Alstré°‰ syndrome.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-3022R-A488)

Fournisseur:  Bioss
Description:   This gene encodes a receptor tyrosine kinase, which belongs to the insulin receptor superfamily. This protein comprises an extracellular domain, an hydrophobic stretch corresponding to a single pass transmembrane region, and an intracellular kinase domain. It plays an important role in the development of the brain and exerts its effects on specific neurons in the nervous system. This gene has been found to be rearranged, mutated, or amplified in a series of tumours including anaplastic large cell lymphomas, neuroblastoma, and non-small cell lung cancer. The chromosomal rearrangements are the most common genetic alterations in this gene, which result in creation of multiple fusion genes in tumourigenesis, including ALK (chromosome 2)/EML4 (chromosome 2), ALK/RANBP2 (chromosome 2), ALK/ATIC (chromosome 2), ALK/TFG (chromosome 3), ALK/NPM1 (chromosome 5), ALK/SQSTM1 (chromosome 5), LK/KIF5B (chromosome 10), ALK/CLTC (chromosome 17), ALK/TPM4 (chromosome 19), and ALK/MSN (chromosome X).[provided by RefSeq, Jan 2011].
UOM:  1 * 100 µl
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