15516 Results for: "Clinical,+Fixed"

Supplier: Promega Corporation

The MagaZorb DNA Kit provides an easy, fast and cost-effective technique for isolating PCR-quality DNA.

Supplier: IBI Scientific

Cost-effective and non-invasive method to capture saliva samples for DNA extraction.

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: MP Biomedicals

MPure Viral/Pathogen Nucleic Acids Extraction Kit B is used with the MPure 12 instrument for extraction of viral and bacterial DNA/RNA from Viral, bacterial and swab samples (cell-rich samples).

Supplier: Biosensis

The Biosensis Mouse and Rat proNGF Rapid enzyme-linked immunosorbent assay (ELISA) Kit is a sandwich ELISA that allows the quantification of rodent full-length proNGF protein in less than 4 hours in cell culture supernatants, cell lysates and tissue homogenates only if used as directed. This ELISA Kit has also successfully been used on mouse urine samples (Ryu JC et al., 2018). Please refer to the kit protocol for specific use instructions for each substrate application.

This ELISA kit contains a recombinant mouse proNGF standard expressed in E.coli and consists of a pre-coated anti-proNGF capture antibody, a biotinylated anti-proNGF detection antibody and horseradish peroxidase (HRP)-conjugated streptavidin. The addition of a substrate (3,3',5,5'-tetramethylbenzidine, TMB) yields a colored reaction product which is directly proportional to the concentration of proNGF present in samples and protein standards. A proNGF positive control (QC sample) is provided to assure consistent assay performance. This ELISA kit detects rat proNGF due to high degree of homology (96%) with mouse proNGF based on amino acid sequence, and the ability of this kit in detecting proNGF in rat PC12 cell lysates and rat brain tissue homogenate. In the absence of a true rat proNGF standard, results may be expressed as 'mouse proNGF equivalents'. This ELISA kit shows only 20% reactivity with the human form of proNGF and is therefore not suitable to quantify human proNGF. No cross-reactivity was observed with mature mouse NGF and full-length proBDNF when tested in assay buffer.

The antibodies used in this ELISA kit bind epitopes within the pro-domain (capture) and mature domain (detection) of the protein, thus this ELISA assay does not detect the pro-domain peptide. This kit has not been tested for other applications. Sufficient amount of proNGF standard is supplied to allow for spike- and recovery experiments in order to validate this ELISA assay for other sample matrices if required.

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.