Ra,Po and lead isotopes in a pit lake water profile in Sweden
A pit lake arises as a consequence of anthropogenic actions in opencast mining areas. These water our bodies could also be enriched in hazardous secure contaminants and/or innaturally occurring radionuclides relying on the native geological circumstances. Mining legacy in Sweden produced lots of of those pit lakes and most of them are used for leisure functions within the southern a part of the nation.
On this paper, one pit lake was chosen for having enhanced ranges of pure radionuclides. Physico-chemical parameters (temperature, pH, oxidation-reduction potential, dissolved oxygen and depth), elemental composition (through Inductive Coupled Plasma Mass Spectrometry) and radiometric characterization (through alpha spectrometry of 226Ra, 210Po and 210Pb) had been carried alongside the depth of a 60 m depth pit lake, with the principle purpose to explain how pure radionuclides and components behaves with depth in a non-uraniferous pit lake.
Primarily based on noticed adjustments in physico-chemical parameters, a thermocline and a chemocline area had been recognized at round 10 and 30 m depth respectively. Regarding radionuclides, 226Ra ranged from 75 ± Three as much as 360 ± 12 mBq/kg whereas 210Po ranged from 11 ± 1 as much as 71 ± Three mBq/kg. 210Pb distribution with depth was additionally decided through secular equilibrium with 210Po after 2 years and likewise secure Pb was measured. Disequilibrium 226Ra-210Pb was discovered and the residence time of 210Pb within the water column was assessed. Moreover, totally different vertical distributions between210Pb and Pb had been discovered which factors out totally different sources for various lead isotopes within the water physique.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation. It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1. The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation (2). It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1 (2). The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: LIF is a multifunctional secreted glycoprotein that exists in both soluble and matrix-bound forms. It displays biologic activities ranging from the differentiation of myeloid leukemic cells into macrophage lineage to effects on bone metabolism, inflammation, neural development, embryogenesis, and the maintenance of implantation (2). It is now clear that LIF is related in both structure and mechanism of action to the interleukin IL-6 family of cytokines, which also includes IL-11, ciliary neurotrophic factor, oncostatin M, and cardiotrophin 1 (2). The actions of these cytokines are mediated through specific cell-surface receptors that consist of a unique chain and the shared signal transducing subunit gp130.
Description: Based on its helical structure, LIF (Leukemia Inhibitory Factor) is considered a member of the Interleukin-6 family of cytokines. Functionally, it has been implicated in a many physiological processes including development, hematopoiesis, bone metabolism, and inflammation. Some cell types known to express LIF include activated T cells, monocytes, astrocytes, osteoblasts, keratinocytes, regenerating skeletal muscle, mast cells, and fibroblasts.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF.
Description: Leukemia inhibitory factor (LIF) is a member of Interleukin 6 family. This protein is mainly expressed in the trophectoderm of the developing embryo, with its receptor LIFR expressed throughout the inner cell mass. LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes. LIF is used in mouse embryonic stem cell culture, because that removal of LIF pushes stem cells toward differentiation, but they retain their proliferative potential or pluripotency. It is also used in phase II clinical trial, which can assist embryo implantation in women who have failed to become pregnant despite assisted reproductive technologies (ART). Mature mouse LIF shares 78 % a.a. sequence identity with Human LIF.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF. Recombinant mouse LIF produced in E. coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.86 kDa.
Description: Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence. Human LIF is as active on human cells as is it is on mouse cells, though mouse LIF is about 1000 fold less active on human cells, than human LIF. Recombinant mouse LIF produced in E. coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.86 kDa.
Description: Description of target: Leukemia inhibitory factor, or LIF, is an interleukin 6 class cytokine that affects cell growth by inhibiting differentiation. When LIF levels drop, the cells differentiate. The LIF was mapped gene to 22q11-q12.2 by Southern analysis of a series of mouse/human somatic cell hybrids and by in situ hybridization to the chromosomes of 2 normal males and some individuals with chromosomal rearrangements. The gene maps between the Philadelphia translocation BCR1 and the breakpoint of the translocation in cell line GM2324 at 22q12.2. LIF derives its name from its ability to induce the terminal differentiation of myeloid leukemic cells, thus preventing their continued growth. Other properties attributed to the cytokine include: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: <10pg/ml
Description: Description of target: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.;Species reactivity: Mouse;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.039 ng/mL
Growth of ‘on-site’ measurement strategies for assay of plutonium isotopes
Over the previous many years, radioanalytical strategies for environmental monitoring of plutonium (Pu) isotopes from contaminated soils had been developed to reply in case of a nuclear accident but in addition for routine analyses. On this paper we show the potential for on-site evaluation of plutonium utilizing alpha particle spectrometry.
Exams are carried out with two kinds of soils: a “brown” soil and a “sandy” soil, each spiked with 242Pu. The proposed methodology begins with leaching thesoil, then separating the radionuclides of curiosity by means of a TEVA column and at last getting ready counting planchets for alpha-spectrometry analyses. The purpose of this work was to acquire a quick and dependable process, from the pattern preparation to the evaluation, relevant straight within the subject and lasting not than a working day.
The testing concerned a number of parameters, such because the soil-to-liquid ratio, the acid molarity, the affect of a purification step, the supply preparation. For every process outlined, the time and the restoration charges of 242Pu had been recorded and in contrast. Outcomes have confirmed that the restoration charges improve with the solid-to-liquid ratio, with the acid molarity, with the purification step however lower with the blending time. The 2 strategies used for supply preparation confirmed related outcomes and the sources had been measured by alpha spectrometry, utilizing two totally different counting units. The ultimate chosen pattern preparation process has a throughput of three h, with restoration charges of 33.8 ± 3.1% for the “brown” soil and 77.3 ± 9.2% for the “sandy” soil and is appropriate for a subject utility.
Steady C isotope information of southern mixed-grass prairie vegetation from Oklahoma, United States
Steady carbon isotopic information (δ13C) of 41 particular person plant species was collected from long-term grazed and ungrazed pastures in Oklahoma, USA. These information can function a library of secure carbon isotope values for Southern mixed-grass prairie species. Seventeen warm-season (C4) and twenty-four cool-season (C3) crops had been recognized and picked up from the US Division of Agriculture (USDA) Southern Plains Experimental Vary (SPER). Plant samples had been dried at 55°C, and floor finely.
The δ13C isotopic compositions had been decided utilizing a Europa Scientific automated nitrogen carbon analyzer (ANCA/NT) with a Stable/Liquid Preparation Module (Dumas combustion pattern preparation system) coupled to a Europa 20-20 Steady isotope analyzer steady circulate isotope ratio mass spectrometer (Sercon Ltd, previously Europa Scientific Ltd., Crewe, England). These information can be utilized as finish members in isotopic mixing fashions or in paleoecology to correlate soil ages with plant species composition. Information from plant species supplies details about soil natural carbon sequestration and potential long-term local weather change.
Description: Human IL-17 RA/IL-17 R Recombinant Protein expressed in Baculovirus with hIgG-His-tag. Sequence domain: 33-320aa. Application(s): SDS-PAGE. Endotoxin: < 1 EU per 1ug of protein (determined by LAL method).
Description: Cytokines are small, soluble proteins with pleiotropic effects on a variety of cell types. Cytokines have a regulatory function over the immune system and mediate aspects of inflammatory response. They exert their biological effects through the binding of membrane-bound receptors which, in turn, initiate signal transduction cascades and elicit physiological changes in their target cell. Interleukin-17 (IL-17) and its cognate receptor, IL-17R, are an example of such a cytokine receptor pair. Originally identified as a rodent cDNA termed CTLA8, IL-17 is capable of inducing the secretion of IL-6 and IL-8 and augmenting the expression of ICAM-1 in human fibroblast cultures. The IL-17 protein exhibits a striking degree of homology with the HSV13 protein which mimics its function. The IL-17 receptor is a type I transmembrane protein 864 amino acids in length, that is highly expressed in spleen and kidney.
Description: IL-17 binds to IL-17 receptors (IL-17 R), which share no homology with any known family of receptors. While the expression of IL-17 is restricted to activated T cells, IL-17 R mRNA exhibits a broad tissue distribution, and has been detected in virtually all cells and tissues tested. The amino acid sequence of human IL-17 R is 69% identical to mouse IL-17 R.
Description: Interleukin-17A Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 264 amino acids (2 chains of 132 aa) and having a molecular mass of 31kDa. ;The IL-17 is purified by proprietary chromatographic techniques.
Description: The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 136 amino acid chains, secreted by activated T-cells that act on stromal cells to induce production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 represents a family of structurally-related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17A exhibits cross-species bioactivity between human and murine cells. Recombinant human IL-17A is a 31.3 kDa disulfide-linked homodimer of two 137 amino acid polypeptide chains.
Description: Human Interleukin-17A (IL-17A) is encoded by the IL17A gene located on the chromosome 6 and belongs to the IL-17 family that contains IL-17A, IL-17B, IL-17C, IL-17D, IL-17E and IL-17F. They have a similar protein structure, with four highly conserved cysteine residues critical to their 3-dimensional shape, but no sequence similarity to any other known cytokines. Interleukin 17 is a T cell-expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpesvirus Saimiri. Mature IL-17 containing one potential N-linked glycosylation site. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers. At the amino acid level, IL-17 exhibits 63 % amino acid identity with mouse IL-17. High levels of human IL-17 were induced from primary peripheral blood CD4+ T cells upon stimulation and they can induce stromal cells to produce proinflammatory and hematopoietic cytokines.
Description: The IL-17 family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL-17 is induced by IL-15 and IL-23, mainly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17F is the most homologous to IL-17, but is induced only by IL-23 in activated monocytes. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL-17E is mainly produced by Th2 cells and recruits eosinophils to lung tissue. IL-17C has a very restricted expression pattern but has been detected in adult prostate and fetal kidney libraries.
Description: The IL-17 family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL-17 is induced by IL-15 and IL-23, mainly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17F is the most homologous to IL-17, but is induced only by IL-23 in activated monocytes. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL-17E is mainly produced by Th2 cells and recruits eosinophils to lung tissue. IL-17C has a very restricted expression pattern but has been detected in adult prostate and fetal kidney libraries.
Description: Quantitative sandwich ELISA for measuring Human IL-17 in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Human IL-17 in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Human IL-17 in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Interleukin-17A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 132 amino acids fragment (24-155) having a molecular weight of 19.62kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. ;The IL-17A His is purified by proprietary chromatographic techniques.
Human Interleukin 17 (IL-17) quantitative detection ELISA Kit
