Gold nanoprism/Tollens’ reagent complicated as plasmonic sensor in headspace single-drop microextraction for colorimetric detection of formaldehyde in meals samples utilizing smartphone readout
On this work, an assay with excessive sensitivity and selectivity for the detection of formaldehyde (FA) is introduced. The assay utilized a gold nanoprism/Tollens’ reagent (Au-np/TR) complicated because the sensor utilized in headspace single-drop microextraction (HS-SDME). A floor plasmon resonance sign enhancement in addition to colour change was attributable to the formation of Au@Ag-np after a redox response between FA and TR through the HS-SDME course of.
With the utilization of smartphone nanocolorimetry (SNC), the FA may very well be detected and quantified. For HS-SDME-SNC, a linearity calibration curve ranging from 0.1 to 100 μM was obtained, and the restrict of detection was decided to be 30 nM. Profitable makes an attempt to find out FA have been demonstrated by evaluation of the analyte in (adulterated) uncooked meals samples (octopus and rooster flesh). Matrix results from actual samples have been prevented through the use of HS-SDME, and solely a 3-μL droplet of solvent was wanted within the assay.
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
Genetically Encoded Quinone Methides Enabling Fast, Web site-specific, and Photograph-controlled Protein Modification with Amine Reagents
-carbon, affording the shortest linkage to protein spine which is important for superior research involving orientation and distance. We put in numerous functionalities onto proteins, and connected a spin label as shut as doable to the protein spine, reaching excessive decision in double electron-electron paramagnetic resonance distance measurements.
bSite-specific modification of proteins with useful molecules gives highly effective instruments for researching and engineering proteins. Right here we report a brand new chemical conjugation technique which photocages extremely reactive however chemically selective moieties, enabling using protein-inert amines for selective protein modification. New amino acids FnbY and FmnbY, bearing photocaged quinone methides (QMs), have been genetically integrated into proteins.
Upon mild activation, they generated extremely reactive QM, which quickly reacted with amine derivatives. This technique incorporates a uncommon mixture of desired properties together with quick kinetics, small and steady linkage, compatibility with low temperature, photo-controllability, and broadly accessible reagents. Furthermore, labeling by way of FnbY happens on the
Impression of variation in reagent mixtures for one-stage clotting assay on assay discrepancy in nonsevere haemophilia A
Introduction: Issue VIII exercise (FVIII:C) is measured by one-stage clotting assay (OSA) or chromogenic substrate assay (CSA). Vital variations in FVIII:C between OSA (FVIII:C1st ) and CSA (FVIII:CChr ) are described as assay discrepancy in nonsevere haemophilia A (HA).
A lot of reagent mixtures (APTT reagent and FVIII-deficient plasma) are used for OSA, however the impression of variations in reagent mixtures on assay discrepancy has not been absolutely characterised.
Goal: To make clear the variations in FVIII:C1st /FVIII:CChr ratios based on OSA reagent mixture in HA topics with/with out assay discrepancy.
Strategies: Thirty-nine sufferers beforehand identified with nonsevere HA have been enrolled, and their FVIII genes have been investigated and FVIII:C ranges have been assessed by a single CSA reagent and 11 OSA reagent mixtures.
Receiver working attribute (ROC) curve evaluation was used to foretell doable cut-off values of the FVIII:C1st /FVIII:CChr ratio to outline FVIII assay discrepancy for every reagent mixture.
Outcomes: Sufferers have been categorized into nondiscrepant (n = 25), discrepant (n = 5) and unclassified (n = 9) teams based on their genotypes and data within the database.
The FVIII:C1st /FVIII:CChr ratio in nondiscrepant HA various broadly, relying on the APTT reagents and FVIII-deficient plasma used. The ratio in discrepant HA sufferers differed with respect to their genotype and the reagent mixture used.
ROC curve analyses revealed that cut-off values to tell apart the assay discrepancy differed relying on the reagents used, however revealed two novel genotype variants, p.Cys573Gly and p.Gly582Arg, related to FVIII assay discrepancy
Exploring the habits of the NFSI reagent as a nitrogen supply
The varied organic actions of nitrogen-containing compounds make the development of the C-N bond of nice significance. As N-fluorobenzenesulfonimide, one of the ample chemical feedstock, has a twin behaviour, i.e. as an electrophilic fluorination and amidation supply, it attracts the eye of artificial chemists for exploitation.
This assessment comprehensively summarizes the numerous progress of the environment friendly and gentle amidation reactions, with an emphasis on approaches for the era of nitrogen-centered intermediates, associated mechanisms and new artificial chemistry strategies that supply alternatives to beat obstacles in pharmaceutical purposes.
On this perspective, we focus on the developments within the amidation response utilizing NFSI prior to now decade. We focus on the latest progress, challenges and future outcomes within the space of amidation chemistry utilizing commercially accessible NFSI.
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.
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