Laimaphelenchus africanus n. sp. (Tylenchomorpha: Aphelenchoididae) from South Africa, a morphological and molecularphylogenetic examine, with an replace to the diagnostics of the genus
A newly recovered inhabitants of the genus Laimaphelenchus from a useless maritime pine wooden pattern in Potchefstroom, South Africa, representing a brand new species, named L. africanus n. sp., is herein described and illustrated primarily based on morphological and molecular information. The brand new species is especially characterised by the next: 750-987 µm lengthy females; a cephalic area with no disc and 6 cephalic lobs not divided by ribs; a 10.0-12.5 µm lengthy stylet; 4 incisures within the lateral subject; secretory-excretory pore (SE-pore) at barely posterior to the nerve ring; vulva with a well-developed anterior flap, vagina with two well-developed sclerotized items; post-vulval uterine sac (PUS) 63-125 µm lengthy; tail conical, 30-44 µm lengthy, ventrally curved with a subventral stalk in terminus, missing tubercles, with six to 9 small projections on the tip in scanning electron microscopy (SEM); and uncommon males with 17 μm lengthy spicules.
The brand new species was morphologically in comparison with these species of the genus with a stalk in tail terminus, missing tubercles, a vulval flap and 4 incisures within the lateral subject viz., L. liaoningensis, L. preissii, L. simlaensis, L. sinensis, L. spiflatus, and L. unituberculus. Phylogenetically, the brand new species was positioned into the foremost Laimaphelenchusclade utilizing partial massive subunit ribosomal DNA (LSU rDNA D2-D3) sequences. An total literature overview corroborated the presence of the stalk (at the moment with two most important teams) on the tail finish is the primary attribute trait delimiting the genus. A compendium primarily based on the characters of the stalk, presence/absence of a vulval flap in females and variety of the lateral traces was additionally established.
Cyperus prophyllatus: An endangered aquatic new species of Cyperus L. (Cyperaceae) with a distinctive spikelet disarticulation sample amongst about 950 species, together with molecularphylogenetic, anatomical and (micro)morphological information
Cyperus prophyllatus, an endangered new species of Cyperus (Cyperaceae) from an aquatic ecosystem of the Atlantic Forest, Espírito Santo State, southeastern Brazil, is described and illustrated. The spikelet morphology of Cyperus prophyllatus is exclusive among the many c. 950 species of Cyperus in having each a conspicuous spikelet prophyll and a corky rachilla articulation, which stay persistent on the base of the spikelet after disarticulation. Our molecular phylogenetic information assist the location of C. prophyllatus within the C3 Cyperus Grade and extra exactly within the clade representing Cyperus sect. Oxycaryum, which additionally consists of C. blepharoleptos and C. gardneri.
Anatomical and (micro)morphological analyses corroborate the phylogenetic outcomes, present a greater understanding of ecology and taxonomy, in addition to reveal compatibility of buildings with survival and dispersion in aquatic environments. A distribution map, desk with distinctive characters of allied species, and conservation standing are made obtainable.
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
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: 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: Mouse LIF Protein, Tag Free (LIF-M5219) is expressed from human 293 cells (HEK293). It contains AA Ser 24 - Phe 203 (Accession # P09056-1).
Full chloroplast genome of novel Adrinandra megaphylla Hu species: molecular construction, comparative and phylogenetic evaluation
Adrinandra megaphylla Hu is a medicinal plant belonging to the Adrinandra genus, which is well-known for its potential well being advantages resulting from its bioactive compounds. This examine aimed to assemble and annotate the chloroplast genome of A. megaphylla in addition to examine it with beforehand printed cp genomes throughout the Adrinandra genus. The chloroplast genome was reconstructed utilizing de novo and reference-based meeting of paired-end reads generated by long-read sequencing of complete genomic DNA. The dimensions of the chloroplast genome was 156,298 bp, comprised a big single-copy (LSC) area of 85,688 bp, a small single-copy (SSC) area of 18,424 bp, and a pair of inverted repeats (IRa and IRb) of 26,093 bp every; and a complete of 51 SSRs and 48 repeat buildings have been detected.
The chloroplast genome features a complete of 131 purposeful genes, containing 86 protein-coding genes, 37 switch RNA genes, and eight ribosomal RNA genes. The A. megaphylla chloroplast genome indicated that gene content material and construction are extremely conserved. The phylogenetic reconstruction utilizing full cp sequences, matK and trnL genes from Pentaphylacaceae species exhibited a genetic relationship. Amongst them, matK sequence is a greater candidate for phylogenetic decision. This examine is the primary report for the chloroplast genome of the A. megaphylla.
A brand new species of Pilarella (Copepoda, Calanoida, Arietellidae) from the hyperbenthic layer of Japan, with a molecularphylogenetic evaluation of some consultant genera of the Arietellidae
A brand new species of the continental shelf hyperbenthic genus Pilarella is described, the primary from the Indo-Pacific. That is the second species of Pilarella recognized, and the primary description of a male within the genus. The brand new species is definitely distinguished from different species of Pilarella (P. longicornis) primarily based on: (1) brief caudal rami, roughly 1.5 occasions longer than large; (2) 2 setae on the mandibular endopod; (3) 6 setae on the maxillular coxal epipodite; and (4) within the feminine, a brief left antennule reaching the posterior border of the genital double-somite. The brand new analysis of Pilarella differs from Metacalanus within the separation of ancestral segments IX-XII and XIV-XV of the antennule, and the presence of 5-6 setae on the maxillular praecoxal arthrite.
Pilarella can also be separated from Metacalanalis primarily based on the absence of a seta on the third ancestral phase of the antennary exopod, the symmetry of legs 1-3, the presence of a medial basal seta on the feminine leg 5, and a couple of lateral exopodal spines on the feminine leg 5. A molecular phylogenetic evaluation of some consultant genera of the household Arietellidae, together with the current new species, recovers two arietellid clades (Metacalanus– and Arietellus-clades) as in earlier research. Dichotomous keys for the genera of Arietellidae and the species of Pilarella are included.
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: 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.
