19107 Results for: "AP+physics"

Supplier: 3M

3M™ Disposable Protective Coverall Safety Work Wear 4520 helps protect against certain light liquid splashes and hazardous dusts. This coverall offers a collared option for situations where a hood is not required or may interfere with alternative head, face, or respiratory protection. Advanced, breathable and lightweight materials help reduce heat build-up and promote comfortable wear.

Supplier: Anaspec

Proinsulin C-peptide is the sequence of C peptide as it exists within proinsulin, the precursor to insulin which consists of insulin A chain, insulin B chain and C peptide (connecting peptide). In proinsulin, C peptide provides a means to ensure correct folding and assembly of the A and B chains. It is eventually cleaved away by proteases PC2, PC1/3 and CPE, at the flanking Arg-Arg and Lys-Arg basic residues (Arg-Arg-C peptide-Lys-Arg). Although C peptide is not present in mature insulin, it is stored in secretory granules, and eventually released into the bloodstream together with insulin in nearly equimolar amounts. Whereas insulin is metabolized quickly from circulation, C-peptide exhibits a slow turnover rate (>30 minutes). The measurement of the C-peptide is an important test for the β-cell function. In the red blood cells of type 2 diabetic patients, Na+,K+, ATPase activity is strongly related to blood C-peptide levels. C-peptide signal transduction in human renal tubular cells involves the activation of phospholipase C and PKC-δ and PKC-varepsilon, as well as RhoA, followed by phosphorylation of ERK1/2 and JNK and a parallel activation of Akt. C-peptide shows specific binding to a G-protein-coupled membrane binding site, resulting in Ca2+ influx, activation of mitogen-activated protein kinase signalling pathways and stimulation of Na+, K+ ATPase and endothelial nitric oxide synthase.
Sequence: RREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKR
MW: 3617 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. pNL2.1[Nluc/Hygro] and pNL2.2[NlucP/Hygro] Vectors are used for cloning putative promoters; select for stable cell lines using hygromycin.

Supplier: MP Biomedicals

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin. In the latter case, although histones restrict susceptibility to nuclease action, over a period of time nearly all chromatin DNA is acted upon. According to Mirsky and Silverman, this could result from the looseness of histone attachment to DNA. They found that lysine-rich histones more effectively block DNase access to DNA than arginine-rich histones. Billing and Bonner suggest that DNase attacks the histone-free strand of chromatin DNA. Schmidt, et. al.indicate that hydrolysis of the histone-free region of DNA strands accounts for the initial rapid action of the enzyme on chromatin. Bollum reports degradation of synthetic homopolymer complexes by DNase I. The intracellular functions of the enzyme are probably controlled by a DNase inhibitor, which according to Lazarides and Lindberg is actin.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. The pNL1.1[Nluc] and pNL1.2[NlucP] Vectors are used to clone putative promoter regions to express the bright NanoLuc(R) luciferase.

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. The pNL3.1[Nluc/minP] and pNL3.2[NlucP/minP] Vectors offer a minimal promoter for cloning response elements of interest.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Molecular Devices

Unparalleled performance on a personalized platform. The SpectraMax® iD3 Multi-Mode Microplate Reader is the cornerstone of a complete laboratory solution designed to expand the boundaries of research capabilities. With optimized reagents and the industry-leading data acquisition and analysis tool, SoftMax Pro® 7 Software, the SpectraMax® iD3 allows users to customize workflow to perfectly match their needs.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a 19.1kDa luminescent reporter enzyme that is about 100-fold brighter than either firefly or Renilla luciferase. Use the pNL3.2.NF-κB-RE[NlucP/NF-κB-RE/Hygro] Vector to measure changes in the levels of NF-kappaB in cells.

Supplier: DuPont

Tychem® 10000 exhibits excellent chemical barrier properties and offers an extremely durable fabric that is puncture- and tear-resistant.

Supplier: DuPont

Tychem® 10000 exhibits excellent chemical barrier properties and offers an extremely durable fabric that is puncture- and tear-resistant.

Supplier: Molecular Devices

The SpectraMax® iD5 Multi-Mode Microplate Reader is the complete laboratory solution to help you increase your research capabilities and comes with built-in absorbance, fluorescence, luminescence, time-resolved fluorescence (TRF), and tunable fluorescence polarization (FP) read modes

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. pNL2.1[Nluc/Hygro] and pNL2.2[NlucP/Hygro] Vectors are used for cloning putative promoters; select for stable cell lines using hygromycin.

Supplier: DuPont

Tychem® 10000 exhibits excellent chemical barrier properties and offers an extremely durable fabric that is puncture- and tear-resistant.

Supplier: DuPont

Tychem® 10000 exhibits excellent chemical barrier properties and offers an extremely durable fabric that is puncture- and tear-resistant.

Supplier: 3M Healthcare

3M™ Water Filtration Products High Flow Series (-S) model filter system provide Recipe Quality Water™ for commercial ice machines and commercial steam tables by reducing the effects of sediment*, chlorine taste and odor and scale* while helping you protect your equipment.

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Thermo Scientific Chemicals

MDL: MFCD00150035 Beilstein Registry No.: 6121732 Notes: Suitable for Karl Fischer reagent standardization. Soluble in water

Supplier: Thermo Scientific Chemicals

Baking powder, medicine (cathartic), component of Fehling's solution, silvering mirrors

Supplier: Thermo Scientific Chemicals

MDL: MFCD00150989 Beilstein Registry No.: 6113568 Notes: Loses water of crystallization at 140°C unstable above 225°C

Supplier: Thermo Scientific Chemicals

MDL: MFCD00148863

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Genetex

The RNAs that direct protein synthesis in animals and plant cells are synthesized in the nucleus as large precursors (pre-mRNAs). The protein coding sequences in pre-mRNA molecules are arranged in discontinuous segments - exons interspersed with noncoding sequences - introns. In a process termed splicing, these introns are efficiently removed before the pre-mRNA is transported from the nucleus to the cytoplasm, where it is translated into protein. Studies have shown that nuclear pre-mRNA splicing takes place in a multi-component structure termed a spliceosome. The polypyrimidine tract-binding (PTB) protein-associated splicing factor (PSF), which plays an essential role in mammalian spliceosomes, is a ubiquitous nuclear matrix protein. A complex between PTB and PSF is necessary for pre-mRNA splicing. PSF contains two consensus RNA-binding domains and an unusual amino terminus rich in proline and glutamine residues. The RNA-binding properties of PSF are apparently identical to those of PTB. Both proteins, together and independently, bind the polypyrimidine tract of mammalian introns. However, the nuclear localization of PSF and PTB and their distribution in subnuclear fractions differ markedly: isolated nuclear matrices contain a bulk of PSF, but only minor amounts of PTB. In confocal microscopy both proteins appear in speckles, the majority of which do not co-localize. These PTB/PSF complexes, as well as the observed PSF-PTB interaction, may reflect the presence of PTB and PSF in spliceosomal complexes during RNA processing, although other data point to different cellular distribution and nuclear matrix association of the majority of PSF and PTB. The cleavage of PSF during lysis of immature myeloid cells is accompanied by digestion of the PTB splicing regulator but not other proteins tested. In contrast, during apoptosis PTB is degraded while PSF remains intact. Proteolytic degradation of PSF specifically occurs in intact myeloid cells and this process is enhanced upon immature myeloid cell lysis; PSF is completely cleaved to a 47 kDa proteolytic cleavage product (p47), due to potent proteolytic activity found in these cells but rare in other cells and tissues. Furthermore, p47 is abundant in intact normal and tumor myeloid cells while in other cell types it is undetectable. The bone marrow 47 kDa protein is a fragment constituting the N-terminal, protease-resistant half of the splicing factor PSF. PSF is highly basic and migrates anomalously on SDS gels. The 47 kDa protein of mouse cells of immature myeloid origin (bone marrow and acute myeloid leukemia) exhibits a gel migration pattern corresponding to a 49 kDa molecule. In other cell types such as lymphoid cells and in peripheral blood cells, PSF appears as approx. 100 kDa or 75 kDa molecules. The sequence of a fragment of mouse PSF was found to be remarkably similar to that of human PSF ( > 98% homology). Also, the sequences of PSF and the human (h) 100 kDa DNA-pairing protein (hPOMp100) reveals identity. Homologous pairing is a fundamental biological reaction implicated in various cellular processes such as DNA recombination and repair, chromosome pairing, sister chromatid cohesion and chromosome condensation, gene inactivation and initiation of replication. The base pairing is also involved in spliceosome assembly resulting in formation of a dynamic Holliday-like structure within which splicing occurs. Indeed, PSF/hPOMp100 bind both singlestranded (ss) and double-stranded (ds) DNA and facilitates the renaturation of complementary ssDNA molecules. Importantly, PSF/hPOMp100 promotes the formation of D-loops in superhelical duplex DNA. PSF/hPOMp100 also serves as an efficient substrate for protein kinase C (PKC) in vitro. PKC phosphorylation of PSF/hPOMp100 stimulates its DNA binding and D-loop formation activity suggesting a possible regulatory mechanism. PSF has been demonstrated to interact with a variety of cellular targets including the human pro-oncoproteins EWS, hPOMp75/TLS and calmodulin, the RNA/DNAbinding nuclear protein p54nrb/NonO (the homolog of PSF) and DNA topoisomerase. A direct interaction has been observed, between PSF and topoisomerase I which has been implied in DNA recombination, DNA repair, and chromosome formation and may act as a transcription factor and a protein kinase. PSF is also expressed by differentiating neurons in developing mouse brain. Both the expression of PSF mRNA in cortex and cerebellum and PSF immunoreactivity in all brain areas has been found to be high during embryonic and early postnatal life. In adult tissue, only various neuronal populations in the hippocampus and olfactory bulb express PSF. PSF is expressed by differentiating neurons but not by astrocytic cells including radial glia; however oligodendrocytes differentiating in vitro were found to express it. The restricted expression of PSF suggests that it is involved in the control of neuronal-specific splicing events occurring at particular stages of neuronal differentiation and maturation. Monoclonal antibodies reacting specifically with PSF are useful tools for the molecular identification and characterization of the functional activity of PSF.

Supplier: Thermo Fisher Scientific

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