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Fournisseur:  Biotium
Description:   Recognizes a protein of14 kDa, identified as MRP-14 (also known as Calgranulin B or S100AA9). It comprises 60% of the cytoplasmic protein fraction of circulating polymorphonuclear granulocytes and is also found in monocytes, macrophages and ileal tissue eosinophils. Peripheral blood monocytes carry the antigen extra- and intracellularly, neutrophils only intracellularly. It is a potent chemotactic factor for neutrophils. Plasma concentrations are elevated in diseases associated with increased neutrophil activity, like inflammatory bowel disease. Granulocytes terminate their existence after transmigration through the intestinal wall. Therefore, it is also detectable in feces. Elevated levels have been observed in body fluids such as plasma, saliva, gingival crevicular fluid, stools, and synovial fluid during infection and inflammatory conditions. This MAb reacts with neutrophils, monocytes, and macrophages, and has been shown as an important marker for identifying macrophages in tissue sections.
UOM:  1 * 50 µl
Fournisseur:  Biotium
Description:   This MAb reacts with a protein of 22 kDa, identified as beta subunit of HCG. It does not cross react with the alpha subunit. HCG is a glycoprotein, which is secreted in large quantities by normal trophoblasts. It is present only in trace amounts in non-pregnant urine and sera but rises sharply during pregnancy. HCG is composed of two non-identical, non-covalently linked polypeptide chains designated as the alpha and beta subunits. The alpha subunit is identical to that of thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH), and luteinizing hormone (LH). hCG MAb detects cells and tumors of trophoblastic origin such as choriocarcinoma. Large cell carcinoma and adenocarcinoma of the lung demonstrate anti-hCG positivity in 90% and 60% of cases respectively. 20% of lung squamous cell carcinomas are positive. hCG expression by non-trophoblastic tumors may indicate aggressive behavior.

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-6560R-A647)

Fournisseur:  Bioss
Description:   The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6560R-A555)

Fournisseur:  Bioss
Description:   The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-8691R-CY3)

Fournisseur:  Bioss
Description:   Voltage-gated K+ channels in the plasma membrane control the repolarization and the frequency of action potentials in neurons, muscles and other excitable cells. The KV gene family encodes more than 30 proteins that comprise the subunits of the K+ channels, and they vary in their gating and permeation properties, subcellular distribution and expression patterns. Functional KV channels assemble as tetramers consisting of pore-forming å subunits (KV), which include the KV1, KV2, KV3 and KV4 proteins, and accessory or KV-subunits that modify the gating properties of the coexpressed KV subunits. KV∫, also known as KCNAB1 (potassium voltage-gated channel, shaker-related subfamily, beta member 1), is a 419 amino acid accessory K+ channel protein that exists as three alternatively spliced isoforms and regulates the activity of the pore-forming å subunit. It is expressed in brain, with highest levels detected in caudate nucleus, hippocampus and thalamus.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11646R-CY5)

Fournisseur:  Bioss
Description:   Humanin, an endogenous anti-apoptotic peptide against Alzheimer disease-related insults, consists of 24 amino acids. The secreted protein is a neuroprotective factor against death induced by several different types of Alzheimer's disease genes. Humanin protects neuronal cells from damage caused by Alzheimer's disease genes, specifically APP (amyloid precursor protein). Humanin acts as a ligand for formyl peptide receptor-like 1 (FPRL1) with APP and utilizes its neuroprotective effects by inhibiting FPRL1 access to APP. The peptide prevents Bax translocation from cytosol to mitochondria. Humanin expression levels may be dependent on defects in energy production in muscles with mitochondrial abnormalities. The peptide has been detected in muscles of patients with the mitochondrial disease chronic progressive external ophthalmoplegia (CPEO). Humanin is mainly expressed in the kidney, heart, liver, testis and skeletal muscles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13703R)

Fournisseur:  Bioss
Description:   The asymmetric unit membrane (AUM) forms numerous plaques, which cover the apical surface of the urothelium. These plaques are thought to strengthen the urothelium and reduce the risk of rupturing during ladder distention. They are composed of four major integral membrane proteins called uroplakins (UP). The uroplakin family comprises UPIa, UPIb, UPII, and UPIII. Family members are conserved among several species, including human, mouse, rat, rabbit, dog, pig and sheep. UPIa and UPIb form tightly packed structures with UPII and UPIII, respectively. This pairing is required for normal urothelial plaque formation and is regulated by proteolytic processing of the uroplakin proteins. Uroplakins are expressed in normal urothelium and are used as specific markers of urothelial differentiation. They are also expressed in a majority of transitional cell carcinomas of the bladder (TCCs), which make the uroplakins a useful marker for detecting bladder cancer metastasis and for staging and monitoring chemotherapeutic response.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11848R-CY5)

Fournisseur:  Bioss
Description:   G protein-coupled receptors (GPRs or GPCRs), also known as seven transmembrane receptors, heptahelical receptors, or 7TM receptors, are members of the largest protein family and play a role in many different stimulus-response pathways. G-protein coupled receptors mediate extracellular signals into intracellular signals (G-protein activation). They respond to a great variety of signaling molecules, including hormones, neurotransmitters and other proteins and peptides. GPR proteins are integral seven-pass membrane proteins with some conserved amino acid regions. G-protein coupled receptor 56 (GPR56), also designated TM7XN1 protein, contains one GPS domain. GPR56 plays an important role in cell-cell interactions and is widely expressed, with highest levels detected in brain, heart and thyroid gland. Defects in the gene encoding for GPR56 can cause bilateral frontoparietal polymicrogyria (BFPP) which is characterized by disorganized cortical lamination.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11848R-CY3)

Fournisseur:  Bioss
Description:   G protein-coupled receptors (GPRs or GPCRs), also known as seven transmembrane receptors, heptahelical receptors, or 7TM receptors, are members of the largest protein family and play a role in many different stimulus-response pathways. G-protein coupled receptors mediate extracellular signals into intracellular signals (G-protein activation). They respond to a great variety of signaling molecules, including hormones, neurotransmitters and other proteins and peptides. GPR proteins are integral seven-pass membrane proteins with some conserved amino acid regions. G-protein coupled receptor 56 (GPR56), also designated TM7XN1 protein, contains one GPS domain. GPR56 plays an important role in cell-cell interactions and is widely expressed, with highest levels detected in brain, heart and thyroid gland. Defects in the gene encoding for GPR56 can cause bilateral frontoparietal polymicrogyria (BFPP) which is characterized by disorganized cortical lamination.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6991R-A488)

Fournisseur:  Bioss
Description:   In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6991R-A350)

Fournisseur:  Bioss
Description:   In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13010R-A750)

Fournisseur:  Bioss
Description:   DNA repair proteins are necessary for the maintenance of chromosome integrity and are involved in the elimination of premutagenic lesions from DNA. The DNA repair proteins Rad51 and Rad52 are key components of the double-strand-break repair (DSBR) pathway. Rad51 is essential for mitotic and meiotic recombination, and its mutation in yeast and mammalian cells results in chromosome loss. Overexpression of Rad52 confers resistance to ionizing radiation and induces homologous intrachromosomal recombination. Rad52 is thought to be involved in an early stage of Rad51-mediated recombination. Additional proteins involved in the pathway include Nibrin and Dmc1. Nibrin, which complexes with Mre11 and Rad50, is absent in Nijemegen breakage syndrome (NBS) patients. Dmc1 is specifically involved in meiotic recombination. An alternative spliced form of Dmc1, designated Dmc1-D, is deleted for a region between the two motifs involved in nucleotide binding. The alternatively spliced Dmc1-D transcript is detected in both male and female germ cells, indicating that the encoded protein may have a role in mammalian genetic recombination in meiosis.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   DNA repair proteins are necessary for the maintenance of chromosome integrity and are involved in the elimination of premutagenic lesions from DNA. The DNA repair proteins Rad51 and Rad52 are key components of the double-strand-break repair (DSBR) pathway. Rad51 is essential for mitotic and meiotic recombination, and its mutation in yeast and mammalian cells results in chromosome loss. Overexpression of Rad52 confers resistance to ionizing radiation and induces homologous intrachromosomal recombination. Rad52 is thought to be involved in an early stage of Rad51-mediated recombination. Additional proteins involved in the pathway include Nibrin and Dmc1. Nibrin, which complexes with Mre11 and Rad50, is absent in Nijemegen breakage syndrome (NBS) patients. Dmc1 is specifically involved in meiotic recombination. An alternative spliced form of Dmc1, designated Dmc1-D, is deleted for a region between the two motifs involved in nucleotide binding. The alternatively spliced Dmc1-D transcript is detected in both male and female germ cells, indicating that the encoded protein may have a role in mammalian genetic recombination in meiosis.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-7116R-CY5)

Fournisseur:  Bioss
Description:   Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).
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.
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