105472 Results for: "electrophoresis+reagents+HyClone+products"

Supplier: VELP SCIENTIFIC INC.

Powerful digital magnetic hotplate stirrers, equipped with a 180 mm (7") square ceramic plate,  designed to deliver precise temperature control, improved safety features, maximum reliability and ease of use.

Supplier: Rockland Immunochemical

AKT2 Western Bloting kit allows for the detection of endogenous protein levels of human AKT2 present in cell lysates provided by the user. As a positive control, this kit includes a MDA-MB468 whole cell lysate proven to contain AKT2. After protein separation by SDS-PAGE and transfer, the membrane is probed with Rockland's optimized Anti-AKT2 antibody. Detection of the membrane bound antibody-antigen complex is achieved by the addition of a secondary antibody conjugated to the enzyme horseradish peroxidase. The enzyme reacts with a specialized formulation of luminol, an extremely sensitive, non-radioactive substrate that emits light and allows visualization using X-ray film or other imaging methods, including highly sensitive CCD cameras and imaging systems. AKT2 Western Bloting is ideal for investigators involved in Cell Signaling, Cancer, Neuroscience and Signal Transduction research.

Supplier: Nidec Shimpo America

FG-3000 Series Data logging, Compact Digital Force Gauge, Loaded with functionality to simplify compression and tension testing needs. Menu programming for easy selection and set-up of the instrument to desired requirements with three unique modes of operation.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Genetex

Myosin is the major component of thick muscle filaments, and is a long asymmetric molecule containing a globular head and a long tail. The molecule consists of two heavy chains each ~200,000 daltons, and four light chains each ~16,000 - 21,000 daltons. Activation of smooth and cardiac muscle primarily involves pathways that increase calcium levels and myosin phosphorylation, resulting in contraction. Myosin light chain phosphatase acts to regulate muscle contraction by dephosphorylating activated myosin light chain. This antibody is specific for the phosphorylated form of myosin light chain. The selected peptide sequence used to generate the polyclonal antibody is located near the amino terminal end of the polypeptide corresponding to the smooth/non-muscle form of myosin regulatory light chain found in cardiac myocytes in addition to smooth and non-muscle cells. This sequence differs from that of the sarcomeric/cardiac form of myosin regulatory light chain that has a different sequence around the phosphorylation site. Human and mouse have almost identical sequences. In human the phosphorylation site is pS19, while in mouse the site maps to pS20.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: 3M Healthcare

3M™ Series 500 High Performance Liquid Filter Bags incorporated with bypass and transport layer design that maximizes the amount of surface area in each bag. The result is a unique filter designed to improve performance and reduce operating costs. Filter contains up to 38 square feet of usable filter media.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C-terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. MMPs contain the motif His-Glu-X-X-His (X represents any amino acid) that binds zinc in the catalytic site, as well as another zinc molecule and two calcium molecules structurally. They fall within the matrixin subfamily and are EC designated 3.4.24.x. This group also contains astacin, reprolysin, and serralysin, as well as other more divergent metalloproteinases. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown.

Supplier: Upchurch Scientific

Wrenches are available in three standard sizes, to accommodate the hex headed fittings used throughout the analytical industry

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: MP Biomedicals

β-NADP is a coenzyme necessary for the alcoholic fermentation of glucose and the oxidative dehydrogenation of other substances. It occurs widely in living tissue, especially in the liver. Nicotinic acid can be converted to nicotinamide in the body and, in this form, is found as a component of two oxidation-reduction coenzymes: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The nicotinamide portion of the coenzyme transfers hydrogens by alternating between oxidized quaternary nitrogen and a reduced tertiary nitrogen. NADP is an essential coenzyme for glucose-6-phosphate dehydrogenase which catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconic acid. This reaction initiates metabolism of glucose by a pathway other than the citric acid cycle. This route is known as the hexose phosphate shunt or phosphogluconate pathway. Other enzymes which utilize NADP as a coenzyme are: Alcohol dehydrogenase:NADP dependent; Aromatic ADH:NADP dependent; Ferredoxin-NADP reductase; L-Fucose dehydrogenase; Gabase; Galactose-1-phosphate uridyl transferase; Glucose dehydrogenase; L-Glutamic dehydrogenase; Glycerol dehydrogenase:NADP specific; Isocitric dehydrogenase; Malic enzymes; 5,10-Methylenetetrahydrofolate dehydrogenase; 6-Phosphogluconate dehydrogenase and Succinic semialdehyde dehydrogenase.

Supplier: TCI America

CAS Number: 464-49-3 MDL Number: MFCD00064149 Molecular Formula: C10H16O Molecular Weight: 152.24 Purity/Analysis Method: 98.0% (GC) Form: Crystal Boiling point (°C): 204 Melting point (°C): 178 Flash Point (°C): 66 Specific rotation [a]20/D: 44.5 deg (C=20, EtOH)

Supplier: Prosci

The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR). The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s disease, epilepsy and ischemic neuronal cell death. Increased membrane surface expression of the NR1 subunit of the receptor has been associated with synaptic plasticity. There are a number of different splice variants of the NR1. Differential splicing of three exons in the NR1 subunit generates up to eight NR1 splice variants and 7 of these have been identified in cDNA libraries. These exons encode a 21 amino acid N-terminal domain (N1) and adjacent sequences in the C-terminus (C1 and C2). Splicing out the C2 cassette eliminates the first stop codon and produces a new reading frame that generates a new sequence of 22 amino acids (C2'). Considerable attention has been focused on the distribution and expression of these splice variants that may affect the functional properties and regulation of the NMDAR.

Supplier: Genetex

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane-type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimers, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

Supplier: Genetex

Jun activation domain-binding protein 1 (JAB1) also designated COP9 subunit 5 (COPS5) or SGN5 is a coactivator of AP1 transcription factor that also promotes degradation of the cyclin-dependent kinase inhibitor p27Kip1. JAB1 interacts with c-Jun AP1 containing complexes, and enhances transactivation from AP1 dependent promoters. It also interacts with Jun D but not with Jun B or v-Jun. JAB1 is highly conserved in evolution and is widely expressed in mammalian tissues. It is localized both the nucleus and the cytoplasm. It interacts with the cytoplasmic domain of the alphaL/beta2 integrin LFA1. Following LFA1 engagement the nuclear pool of JAB1 increases and activation of an AP1 driven promoter is enhanced. Interaction of JAB1 with the nuclear progesterone receptor and the steroid receptor activator (SRC1) was reported. JAB1 is a stability and activity regulator of Hypoxia - inducible factor 1 (HIF1), a transcription factor that controls activation of several genes responsive to the cellular oxygen tension. The macrophage migration inhibitory factor (MIF) associates with JAB1 in the cytosol near the plasma membrane. Endogenous MIF inhibits JAB1-induced AP1 transcriptional activity. JAB1 is a subunit of the COP9 regulatory complex. COP9 cleaves the ubiquitin-like protein Nedd8 from the Cul1 subunit of SCF ubiquitin ligases. A metalloprotease motif in JAB1 plays a role in this isopeptidase activity. Breakdown of the cyclin dependent kinase inhibitor p27Kip1 is promoted by JAB1. The latter expression in several cancers inversely correlates with p27Kip1 and may reflect tumor aggressiveness. A possible involvement of JAB1 in atherosclerosis was also reported. Involvement of JAB1 in degradation of the suppressors p53 and smad4 was described recently.

Supplier: Prosci

The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR). The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s disease, epilepsy and ischemic neuronal cell death. Increased membrane surface expression of the NR1 subunit of the receptor has been associated with synaptic plasticity. There are a number of different splice variants of the NR1. Differential splicing of three exons in the NR1 subunit generates up to eight NR1 splice variants and 7 of these have been identified in cDNA libraries. These exons encode a 21 amino acid N-terminal domain (N1) and adjacent sequences in the C-terminus (C1 and C2). Splicing out the C2 cassette eliminates the first stop codon and produces a new reading frame that generates a new sequence of 22 amino acids (C2'). Considerable attention has been focused on the distribution and expression of these splice variants that may affect the functional properties and regulation of the NMDAR.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: VWR International

Designed for applications requiring exceptional accuracy, stability, and repeatability, these hotplate-stirrers are equipped with superior heating and mixing capabilities. With temperature ranges up to 500 °C and stirring speeds reaching 1600 rpm, the VWR® hotplate-stirrers are equipped to handle any research, academic and industrial application. Available in two sizes.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Beckman Coulter

The MET ONE HHPC+ Series Handheld Particle Counters are lightweight, comfortable, and allow single-handed operation within mini-environments and workstations.

Supplier: Labconco

These enclosures provide practical, economical protection of operator and environment for applications involving biohazardous material and toxic particulates

Supplier: IMPLEN U.S.A. INC

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: VWR International

The VWR® Dura-Shakers are designed for a wide range of applications including cell cultures that require CO₂ and humidity for optimal cell growth. The remote control module is designed to sit outside of the incubator. The thin ribbon cable is 5.5 feet (168 cm) long and easily passes underneath incubator door or through incubators utility port (minimum diameter 1.2” (3 cm). Controller magnetically attaches to most incubator doors or can sit on a lab bench.

Supplier: Miele

The PLW 8615 laboratory washer can accommodate 216 laboratory flasks, 588 vials, or 294 pipettes. The large glassware washer is flexible and simple to use, it has modular load carriers and SimpleLoad system. This efficient unit has a single door, 900 mm wide, a usable capacity of 351 litres. PLW 8615 provides reliable results, high pump performance with a variable-speed pump and features spray arm monitoring and a conductivity meter.

Supplier: Orflo

Moxi GO II™ combines two instruments to deliver amazingly affordable, easy to use, maintenance-free, gold standard cell count accuracy and precision through the Coulter Principle and integrating 2 channels of flow cytometry. This unique combination covers a large number of routine cell assays (cell count, cell volume, viability, cell proliferation, transfection checks, apoptosis, phenotyping, cellular response) with quantitative single cell data output.

Supplier: Miele

The PLW 8616 laboratory washer can accommodate 216 laboratory flasks, 588 vials, or 294 pipettes. The large glassware washer is flexible and simple to use, it has modular load carriers and SimpleLoad system. This efficient unit has a double door, 900 mm wide, a usable capacity of 351 litres. PLW 8616 provides reliable results, high pump performance with a variable-speed pump and features spray arm monitoring and a conductivity meter.