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GENTAUR Europe BVBA Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45 Fax 0032 16 50 90 45 This email address is being protected from spambots. You need JavaScript enabled to view it.">This email address is being protected from spambots. You need JavaScript enabled to view it. |
GENTAUR BULGARIA
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GENTAUR France SARL
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Fax 01 43 25 01 60
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GmbH Marienbongard 20
52062 Aachen Deutschland
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531
Fax 020 8445 9411
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GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
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Fax 058 710 33 48
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GENTAUR SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6, 24122 Bergamo
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San Jose, CA 95123
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(408) 780-0908
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6017 Snell Ave, Suite 357
San Jose, CA. 96123
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Background Buster - peptide blocker for removal of background staining
Background staining or non-specific staining is an often-encountered problem in immunohistochemistry, in immunofluorescence and in situ stains. Background staining is caused by a number of factors such as cross reactivity of antibodies with the shared epitopes in the tissue, by the presence of natural and/or contaminating antibodies present in the primary antibody and/or the secondary antibody, by ionic interactions, by the presence of carbohydrates and by endogenous biotin present in the tissue. Eradicating background is most important for obtaining background-free specific staining for the ease of qualitative and quantitative evaluation.
PRODUCT DESCRIPTION
Background Buster is a peptide Blocker that eradicates all general background staining. Background Buster removes all background staining caused by primary antibodies, by the staining reagents, by the chromogens, by the fixatives and by endogeneouse biotin present in tissues such as liver and spleen and kidney. Background Buster is used in place of normal sera and other blocking solution for removing background staining in both human and animal tissues.
Background Buster is applicable IHC staining, to immunofluorescence staining and to in situ probe staining in both human and animal tissues. It is also applicable to flow cytometric assays.
Background Buster is a must for animal tissue staining, it is especially essential when staining identical species tissue and antibodies such as mouse antibodies on mouse tissues (Mouse-on-Mouse) and Rabbit-on- Rabbit. A 30-minute incubation with Background Buster is recommended prior to the application of the primary antibody for staining of identical species primary antibodies and tissues. The use of Background Buster is highly recommended for staining of indirect species (non-identical species tissue/ antibody) such as Rat –On-Mouse, Mouse-on- Rat, Mouse-on-Rabbit, etc. A 20-minute incubation with Innovex Background Buster is recommended prior to the application of the primary antibody for staining of Indirect (non-identical species primary antibodies and tissues).
In immunoperoxidase-IHC staining, another type of background and non-specific staining is caused by red blood cell staining; this is due to endogenous peroxidase enzyme present in red blood cells. This type of background requires a pre-treatment step with 3% freshly made hydrogen peroxide (H2O2) in water, this blocking step should precede the blocking step with Innovex Background Buster.
NB306 Background Buster 125 ml qty 419 EUR
NB306-50 Background Buster 50 ml qty 325 EUR
For more information Download PDF file
Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBCI and kNBCI in the rat eye
IMMNLINOLOCALIZATION OF SODIUM.BICARBONATE COTRANSPORTERS
More: Background Buster
The Secret Lives (and Deaths) of Neurons
As the human body fine-tunes its neurological wiring, nerve cells often must fix a faulty connection by amputating an axon -- the "business end" of the neuron that sends electrical impulses to tissues or other neurons. It is a dance with death, however, because the molecular poison the neuron deploys to sever an axon could, if uncontained, kill the entire cell.
Researchers from the University of North Carolina School of Medicine have uncovered some surprising insights about the process of axon amputation, or "pruning," in a study published May 21 in the journal Nature Communications. Axon pruning has mystified scientists curious to know how a neuron can unleash a self -destruct mechanism within its axon, but keep it from spreading to the rest of the cell. The researchers' findings could offer clues about the processes underlying some neurological disorders.
"Aberrant axon pruning is thought to underlie some of the causes for neurodevelopmental disorders, such as schizophrenia and autism," said Mohanish Deshmukh, PhD, professor of cell biology and physiology at UNC and the study's senior author. "This study sheds light on some of the mechanisms by which neurons are able to regulate axon pruning."
Axon pruning is part of normal development and plays a key role in learning and memory. Another important process, apoptosis -- the purposeful death of an entire cell -- is also crucial because it allows the body to cull broken or incorrectly placed neurons. But both processes have been linked with disease when improperly regulated.
The research team placed mouse neurons in special devices called microfluidic chambers that allowed the researchers to independently manipulate the environments surrounding the axon and cell body to induce axon pruning or apoptosis.
They found that although the nerve cell uses the same poison -- a group of molecules known as Caspases -- whether it intends to kill the whole cell or just the axon, it deploys the Caspases in a different way depending on the context.
"People had assumed that the mechanism was the same regardless of whether the context was axon pruning or apoptosis, but we found that it's actually quite distinct," said Deshmukh. "The neuron essentially uses the same components for both cases, but tweaks them in a very elegant way so the neuron knows whether it needs to undergo apoptosis or axon pruning."
In apoptosis, the neuron deploys the deadly Caspases using an activator known as Apaf-1. In the case of axon pruning, Apaf-1 was simply not involved, despite the presence of Caspases. "This is really going to take the field by surprise," said Deshmukh. "There's very little precedent of Caspases being activated without Apaf-1. We just didn't know they could be activated through a different mechanism."
In addition, the team discovered that neurons employ other molecules as safety brakes to keep the "kill" signal contained to the axon alone. "Having this brake keeps that signal from spreading to the rest of the body," said Deshmukh. "Remarkably, just removing one brake makes the neurons more vulnerable."
Deshmukh said the findings offer a glimpse into how nerve cells reconfigure themselves during development and beyond. Enhancing our understanding of these basic processes could help illuminate what has gone wrong in the case of some neurological disorders.
DNA Damage: The Dark Side of Respiration
Adventitious changes in cellular DNA can endanger the whole organism, as they may lead to life-threatening illnesses like cancer. Researchers at Ludwig-Maximilians-Universitaet (LMU) in Munich now report how byproducts of respiration cause mispairing of subunits in the double helix.
The DNA in our cells controls the form and function of every cell type in our bodies. The instructions for this are encoded in the linear sequence of the four subunits found in DNA, the bases adenine (A), cytosine (C), guanine (G) and thymine (T). Random changes in the sequence can lead to cell dysfunction, and may result in unrestricted cell proliferation and malignancies. Mutations can be induced by a variety of agents. For example, cellular respiration, i.e. the reduction of inspired oxygen to water, which powers cell function, also generates highly reactive oxygen species that can damage DNA, with the purine bases G and A being particularly susceptible to this kind of attack.
"Reactive oxygen species are responsible for two different sorts of DNA damage, as they induce formation of both 8-oxo-G and FaPy-G," says Professor Thomas Carell of the Department of Chemistry at LMU. In 2004, work done by Carell and his team defined how 8-oxo-G generates mutations. However, the basis for the mutagenic effect of FaPy-G has remained obscure -- until now. In their latest publication, Carell and his colleagues describe how FaPY-G leads to mispairing of bases in the double helix.
Pernicious partner swapping One G in one strand of the double helix normally matches up with a C on the other, forming a G:C pair. But as a consequence of damage by reactive oxygen species, the guanine base may be transformed into FaPy-G, so that we get a FaPy-G:C base pair. "We have now shown that, in the course of DNA replication prior to cell division, FaPy-G interacts with adenine, leading to the formation of FaPy-G:A base pairs. This partner swap is unusual, since unmodified guanine normally does not team up with adenine," Carell notes.
FaPy-G is subsequently recognized as abnormal and is removed by DNA repair enzymes. The missing base is replaced by a T -- which is the usual partner for A. The net result is that the original G:C base pair has been converted into an A:T pair, and the base sequence has undergone a potentially dangerous mutation.
This outcome is made possible by the fact that the cell's damage-control systems find it surprisingly difficult to distinguish the normal guanine base from its aberrant derivative FaPy-G during DNA replication. "That this defect then leads to mispairing with adenine is one of the main reasons for the spontaneous development of tumors," says Carell. "So with every breath we take, our risk of getting cancer goes up by a teeny-weeny bit." Further insights into the reasons why FaPy-G often eludes the cell's detection and correction systems could help to improve the treatment of cancer, as the inhibition of DNA repair processes in tumor cells increases their sensitivity to chemotherapeutic drugs.
The study was supported by DFG grants awarded to Collaborative Research Centers 646 and 749 and the Center for Integrated Protein Science Munich (CIPSM), an Excellence Cluster.
Flu antibodies can make disease worse
Some antibodies to flu viruses may actually make patients sicker, a new study of pigs suggests.
The finding, published August 28 in Science Translational Medicine, may point to problems with catchall influenza vaccines.
Pigs vaccinated against a seasonal strain of influenza made antibodies to that strain. Some of the antibodies could also latch on to a different flu virus that caused a pandemic among humans in 2009, report scientists led by Hana Golding of the Food and Drug Administration’s Center for Biologics Evaluation and Research in Bethesda, Md., and Amy Vincent of the Department of Agriculture’s National Animal Disease Center in Ames, Iowa.
Instead of protecting the pigs against the 2009 pandemic flu, the broad-range antibodies actually helped the virus invade lung cells, causing pneumonia and lung damage.
Scientists hoping to create a universal flu vaccine need to learn how the pigs’ antibodies and viruses interacted to make the disease worse, James Crowe Jr. of Vanderbilt University writes in a commentary in the same issue of the journal.
And vaccines aren't the only problem, Crowe says. Natural infections may provoke similar disease-worsening problems.
Watching the production of new proteins in live cells
Researchers at Columbia University, in collaboration with biologists in Baylor College of Medicine, have made a significant step in understanding and imaging protein synthesis, pinpointing exactly where and when cells produce new proteins. Assistant Professor Wei Min's team developed a new technique to produce high-resolution imaging of newly synthesized proteins inside living cells. The findings were published in the July 9th issue of The Proceedings of the National Academy of Sciences (Volume 110; Issue 28).
Proteins carry out almost every crucial biological function. Synthesis of new proteins is a key step in gene expression and is a major process by which cells respond rapidly to environmental cues in physiological and pathological conditions, such as cancer, autism and oxidative stress. A cell's proteome (i.e., the sum of all the cell's proteins) is highly dynamic and tightly regulated by both protein synthesis and disposal to maintain homeostasis and ensure normal functioning of the body. Many intricate biological processes, such as cell growth, differentiation and diseases, involve new protein synthesis at a specific location and time. In particular, long-lasting neuronal plasticity (changes in neural pathways and synapses that come from alterations in behavior, environment and bodily injury), such as those underlying learning and long-term memory, require new protein synthesis in a site- and time- dependent manner inside neurons.
Min and colleagues' new technique harnesses deuterium (a heavier cousin of the normal hydrogen atom), which was first discovered by Harold Urey in 1932, also at Columbia University. When hydrogen is replaced by deuterium, the biochemical activities of amino acids change very little. When added to growth media for culturing cells, these deuterium-labeled amino acids are incorporated by the natural cell machineries as the necessary building blocks for new protein production. Hence, only newly synthesized proteins by living cells will carry the special deuterium atoms connected to carbon atoms. The carbon-deuterium bonds vibrate at a distinct frequency, different from almost all natural chemical bonds existing inside cells.
The Columbia team utilized an emerging technique called stimulated Raman scattering (SRS) microscopy to target the unique vibrational motion of carbon-deuterium bonds carried by the newly synthesized proteins. They found that by quickly scanning a focused laser spot across the sample, point-by-point, SRS microscopy is capable of delivering location-dependent concentration maps of carbon-deuterium bonds inside living cells.
"Incorporation of deuterium-labeled amino acids to new proteins is minimally disruptive, and their biochemical properties are almost identical to their natural counterparts," says Lu Wei, the lead author of the paper. "Our technique is highly sensitive, specific, and compatible with living systems under physiological conditions that don't require killing cells or staining."
Prior to this discovery, the ability to observe protein synthesis in living cells had eluded scientists, who devoted extensive efforts to achieving this goal. A classic strategy that involves labeling amino acids with radioisotopes to trace and quantify proteome dynamics requires the samples be killed and exposed to films. Fluorescence microscopy, another popular method, takes advantage of the inherent glowing of green fluorescent protein (GFP) to follow a protein. While this process does work on individual proteins, scientists can't observe the cell's entire proteome. A third technique, bioorthogonal noncanonical amino acid tagging (BONCAT) metabolically incorporates unnatural (biosynthetic) amino acids containing reactive chemical groups. However, the method generally requires killing cells and subsequent dye staining, a process that presents an issue for live tissues and animals. Therefore, it is extremely challenging and desirable to quantitatively image proteome synthesis in living cells, tissues and animals with high resolution. Min's research opens the door for a new method to study living cells, presenting opportunities to understand previously unanswered questions about the behavior of cells as they perform their functions.
The next step for Min's team is to capture where and when a new protein is produced inside brain tissues when an animal is subject to various lab exercises to form long-term memory. "Our new technique will greatly facilitate understanding the molecular mechanisms of many complex behaviors such as learning and diseases," he says.
New function for a molecule interleukin-7 (IL-7)
The molecule interleukin-7 (IL-7) is an important immune system messengers that a sufficient number of T cells guaranteed at present in the body's defenses. ETH Zurich researchers have now shown that IL-7 has another important function: it improves the function of the lymphatic drainage collect moisture that has leaked from the blood vessels into the body tissues and back into the bloodstream. In the future, these insights for lymphedema patients, the lymphatic system is not working properly useful, what tissue to become fluid retention and swelling.
The predisposition to the development of lymphedema can on the one hand, are hereditary. On the other hand, lymphedema often. During the period after a tumor operation Primary tumors are surgically excised tumor and lymph nodes are often removed because they can contain metastases. Tumor in the course of such a surgical procedure is the lymphatic tissue is damaged. This tissue fluid is often not properly arranged, so that the occurrence of lymphedema in 20 to 30 percent of patients.
No drug treatment yet
Currently wearing the only treatment options for patients with lymphedema compression stockings and undergoing a medical manual lymphatic drainage massage therapist. "In IL-7, we have a molecule and a mechanism for improving lymphatic drainage for lymphedema therapy, useful to be discovered," says study leader Cornelia Halin, Assistant Professor of Drug Discovery Technologies.
In their study, the researchers found that IL-7, which shape is formed by the so-called endothelial cells. The lymphatic vessel wall These cells also bear receptors, IL-7 in a certain way based on the lock-and-key principle. "Although we have not formally proven that so far, we assume that the lymphatic endothelial cells produce the neurotransmitter, may directly affect their own function," says Halin. To date, IL-7 is one of only a few molecules have been identified that support lymphatic drainage. A few years ago, researchers discovered that the other endogenous growth factor VEGF-C, a molecule of interest in this context is perhaps also.
Findings from an animal model
Halin and her colleagues showed the drainage support function of IL-7 by drainage experiments in mice, where blue, albumin-binding dye in the skin of the mouse injected ear. It is noteworthy that albumin, a naturally occurring protein that is transported from the tissues via the lymphatics. By quantifying the dye in the tissue remained one day after the injection, the researchers were able to determine how well worked the lymphatic these animals.
In carrying out this experiment, mice, in which a functional IL-7 receptor, it is noted that these mice to only remove half the dye out of the ear skin in order to compare with a functional mouse IL-7 receptor. However, they observed a significant increase in lymphatic drainage in mice with increased IL-7 production. Finally she IL-7 protein is in a third experiment, unchanged administered healthy mice and found that a therapeutic treatment done to improve lymphatic drainage function.
Been tested in patients
The researchers are now planning similar experiments in mice in which lymph vessels are surgically destroyed, similar to the situation in patients after cancer surgery. Here, the researchers want to test whether treatment with IL-7 or IL-7 could lymphedema would be prevented. Reduce the existing lymphedema administered
The long-term goal is to explore the potential of IL-7-based drugs for lymphedema. In particular, IL-7 has been tested in clinical trials, although for different indications: due to its immune-stimulatory activity on T cells, IL-7 is currently undergoing in patients with immunodeficiency diseases such as HIV or hepatitis infection or bone marrow tested transplants.
INFLUENZA B VIRUS (Texas/6/11) Infectious Culture Fluid
PRODUCT DESCRIPTION:
Influenza viruses are enveloped viruses with a diameter of 80-120 nm, and contain a singlestranded, segmented, negative-sense RNA within a nucleocapsid. Influenza virus is propagated in the MDCK cell line. Influenza Culture Fluid is sold in 1.0 mL aliquots, and is shipped on dry ice. Viral culture fluids consist of virus, cells, and media taken directly from the tissue culture flask. Each lot of viral culture fluid is assayed for its Tissue Culture Infective Dose (TCID50), and sold with titers >105 U/ml. Custom orders are available, including specific titers and package sizes.
INTENDED USE:
This product is intended for research, product development testing, or quality assurance testing. Viral culture fluids are sold as consumable testing materials, and are not for propagation or commercialization. Applications include:
- Nucleic Acid / Molecular Testing
- Limit of Detection (LOD) Studies
- Cross-reactivity Studies
- Other Viral-based Assays
TIOLOGIC STATUS/BIOHAZARD TESTING:
Influenza virus is a Biosafety Level 2 organism.
PRECAUTIONS:
USE UNIVERSAL PRECAUTIONS when handling this product! Viral Culture Fluid is live and infectious!! This material should be handled as if capable of transmitting infectious agents.
RECOMMENDED STORAGE:
Viral culture fluid is stable for at least one year when stored at -65ºC or below. To avoid repeat freeze-thaws, which could negatively impact product performance, culture fluid should be stored in aliquots upon receipt.
DO NOT USE IN HUMANS!
These products are NOT intended for use in the manufacture or processing of injectable products subject to licensure under section 351 of the Public Health Service Act, or for any other product intended for administration to humans.
INFLUENZA B VIRUS (Wisconsin/1/10) Infectious Culture Fluid
PRODUCT DESCRIPTION:
Influenza viruses are enveloped viruses with a diameter of 80-120 nm, and contain a singlestranded, segmented, negative-sense RNA within a nucleocapsid. Influenza virus is propagated in the MDCK cell line. Influenza Culture Fluid is sold in 1.0 mL aliquots, and is shipped on dry ice. Viral culture fluids consist of virus, cells, and media taken directly from the tissue culture flask. Each lot of viral culture fluid is assayed for its Tissue Culture Infective Dose (TCID50), and sold with titers >105 U/ml. Custom orders are available, including specific titers and package sizes.
INTENDED USE:
This product is intended for research, product development testing, or quality assurance testing. Viral culture fluids are sold as consumable testing materials, and are not for propagation or commercialization. Applications include:
- Nucleic Acid / Molecular Testing
- Limit of Detection (LOD) Studies
- Cross-reactivity Studies
- Other Viral-based Assays
TIOLOGIC STATUS/BIOHAZARD TESTING:
Influenza virus is a Biosafety Level 2 organism.
PRECAUTIONS:
USE UNIVERSAL PRECAUTIONS when handling this product! Viral Culture Fluid is live and infectious!! This material should be handled as if capable of transmitting infectious agents.
RECOMMENDED STORAGE:
Viral culture fluid is stable for at least one year when stored at -65ºC or below. To avoid repeat freeze-thaws, which could negatively impact product performance, culture fluid should be stored in aliquots upon receipt.
DO NOT USE IN HUMANS!
These products are NOT intended for use in the manufacture or processing of injectable products subject to licensure under section 351 of the Public Health Service Act, or for any other product intended for administration to humans.
INFLUENZA A H3 VIRUS (Victoria/361/11) Infectious Culture Fluid
PRODUCT DESCRIPTION:
Influenza viruses are enveloped viruses with a diameter of 80-120 nm, and contain a singlestranded, segmented, negative-sense RNA within a nucleocapsid. Influenza virus is propagated in the MDCK cell line. Influenza Culture Fluid is sold in 1.0 mL aliquots, and is shipped on dry ice. Viral culture fluids consist of virus, cells, and media taken directly from the tissue culture flask. Each lot of viral culture fluid is assayed for its Tissue Culture Infective Dose (TCID50), and sold with titers >105 U/ml. Custom orders are available, including specific titers and package sizes.
INTENDED USE:
This product is intended for research, product development testing, or quality assurance testing. Viral culture fluids are sold as consumable testing materials, and are not for propagation or commercialization. Applications include:
- Nucleic Acid / Molecular Testing
- Limit of Detection (LOD) Studies
- Cross-reactivity Studies
- Other Viral-based Assays
TIOLOGIC STATUS/BIOHAZARD TESTING:
Influenza virus is a Biosafety Level 2 organism.
PRECAUTIONS:
USE UNIVERSAL PRECAUTIONS when handling this product! Viral Culture Fluid is live and infectious!! This material should be handled as if capable of transmitting infectious agents.
RECOMMENDED STORAGE:
Viral culture fluid is stable for at least one year when stored at -65ºC or below. To avoid repeat freeze-thaws, which could negatively impact product performance, culture fluid should be stored in aliquots upon receipt.
DO NOT USE IN HUMANS!
These products are NOT intended for use in the manufacture or processing of injectable products subject to licensure under section 351 of the Public Health Service Act, or for any other product intended for administration to humans.
INFLUENZA B VIRUS (Massachusetts/2/12) Infectious Culture Fluid
PRODUCT DESCRIPTION:
Influenza viruses are enveloped viruses with a diameter of 80-120 nm, and contain a singlestranded, segmented, negative-sense RNA within a nucleocapsid. Influenza virus is propagated in the MDCK cell line. Influenza Culture Fluid is sold in 1.0 mL aliquots, and is shipped on dry ice. Viral culture fluids consist of virus, cells, and media taken directly from the tissue culture flask. Each lot of viral culture fluid is assayed for its Tissue Culture Infective Dose (TCID50), and sold with titers >105 U/ml. Custom orders are available, including specific titers and package sizes.
INTENDED USE:
This product is intended for research, product development testing, or quality assurance testing. Viral culture fluids are sold as consumable testing materials, and are not for propagation or commercialization. Applications include:
- Nucleic Acid / Molecular Testing
- Limit of Detection (LOD) Studies
- Cross-reactivity Studies
- Other Viral-based Assays
TIOLOGIC STATUS/BIOHAZARD TESTING:
Influenza virus is a Biosafety Level 2 organism.
PRECAUTIONS:
USE UNIVERSAL PRECAUTIONS when handling this product! Viral Culture Fluid is live and infectious!! This material should be handled as if capable of transmitting infectious agents.
RECOMMENDED STORAGE:
Viral culture fluid is stable for at least one year when stored at -65ºC or below. To avoid repeat freeze-thaws, which could negatively impact product performance, culture fluid should be stored in aliquots upon receipt.
DO NOT USE IN HUMANS!
These products are NOT intended for use in the manufacture or processing of injectable products subject to licensure under section 351 of the Public Health Service Act, or for any other product intended for administration to humans.