Intercellular adhesion molecule-4 and CD36 are implicated in the abnormal adhesiveness of sickle cell SAD mouse erythrocytes to endothelium.
BACKGROUND adhesiveness abnormal red blood cells to the endothelium has been involved in vaso-occlusive crisis of sickle cell disease. This study examines whether the SAD mouse model showed the same abnormality adhesion of red blood cells found in human sickle cell disease.
METHOD The repertoire of adhesion molecules in murine erythrocytes and bEnd.3 microvascular endothelial cells was determined by flow cytometry using monoclonal antibodies or by Western blotting. Adhesion investigated under dynamic conditions and are measured at different shear stresses.
RESULTS CD36, CD47 and adhesion molecules between blood type-4, but not Lutheran antigen / basal cell adhesion molecules, which are present in the adult mouse erythrocytes. alpha (4) beta (1) is expressed on the SAD and the wild types of reticulocytes. bEnd.3 endothelial cells express alpha (v) beta (3), alpha (4) beta (1), CD47, vascular cell adhesion molecule-1, and the Lutheran blood group antigen molecules / basal cell adhesion, but not CD36.
Red blood cell adhesion SAD are: (i) 2 to 3 times higher than the wild-type red blood cells; (Ii) a further increase in platelet activating factor-activated endothelium; (Iii) are not stimulated by epinephrine; (Iv) inhibited after treating endothelial peptides bind to reproduce one of the sequences between mouse adhesion molecule-4, or with a mon-oclonal antibodies against murine alpha (v) integrin; and (v) inhibited after pretreatment red blood cells with monoclonal antibody anti-mouse CD36. Combination treatment with an adhesion molecule-4 peptides and anti-CD36 monoclonal antibody remove excess red blood cell adhesion SAD. Phosphorylation state of adhesion between the molecules-4 and CD36 may not engage in over-the adhesiveness of erythrocytes SAD.
CONCLUSION inter adhesion molecule-4 / alpha (v) beta (3) and CD36 / thrombospondin interaction may contribute to an abnormally high adhesion of red blood cells SAD. Mouse SAD is a valuable animal model to investigate the process of adhesion of sickle cell disease.
Intercellular adhesion molecule-4 and CD36 are implicated in the abnormal adhesiveness of sickle cell SAD mouse erythrocytes to endothelium.
The globoside receptor triggers structural changes in the viral capsid B19 that facilitates virus internalization.
Globoside (Gb4Cer), Ku80 auto anti gene, and α 5 β1 integrin has been identified as a cell receptors / coreceptors for human parvovirus B19 (B19V), but their role and mechanisms of interaction with the virus largely unknown. In UT7 / Epo cells, expression Gb4Cer and CD49e ( integrin alpha – 5 ) is high, but not significant Ku80 expression. B19V colocalized with Gb4Cer and, to a lesser extent, with CD49e. However, only anti -Gb4Cer anti the body can interfere with the attachment of the virus. Only a small portion of the cell-bound viruses are internalized, while the majority became detached from the receptor. When added to cells that are not infected, the virus receptor-detached shows superior binding capacity of cells and infectivity.
B19V attachment to the cell triggers a conformational change in the capsid leads to the accessibility of the N terminus of VP1 (VP1u) to anti body, which is maintained in a separate virus-receptor. VP1u be equally accessible to anti the following entities B19V particle incubation with increasing concentrations of purified Gb4Cer. Exposure VP1u receptor-mediated internalization is crucial for the virus, because less VP1 capsids can bind cells but not internalized.
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: LIF Antibody: LIF is a pleiotropic cytokine with roles in several different systems. It is involved in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and may also have a role in immune tolerance at the maternal-fetal interface. LIF was initially recognized by its ability to induce terminal differentiation of myeloid leukemic cells. It is a member of the IL-6 cytokine superfamily and can be highly glycosylated. LIF signaling is transduced through the LIF-R/gp130 receptor complex, leading to the phosphorylation and activation of the JAK/STAT pathway. Recent evidence shows that LIF inhibits cardiomyogenesis in embryonic stem cells via STAT3 activation.
Description: LIF Antibody: LIF is a pleiotropic cytokine with roles in several different systems. It is involved in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and may also have a role in immune tolerance at the maternal-fetal interface. LIF was initially recognized by its ability to induce terminal differentiation of myeloid leukemic cells. It is a member of the IL-6 cytokine superfamily and can be highly glycosylated. LIF signaling is transduced through the LIF-R/gp130 receptor complex, leading to the phosphorylation and activation of the JAK/STAT pathway. Recent evidence shows that LIF inhibits cardiomyogenesis in embryonic stem cells via STAT3 activation.
Description: A polyclonal antibody against LIF. Recognizes LIF from Human. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/20000
Description: A polyclonal antibody against LIF. Recognizes LIF from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:10000, IHC:1:25-1:100
Description: LIF is a pleiotropic cytokine with roles in several different systems. It is involved in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and may also have a role in immune tolerance at the maternal-fetal interface.
Description: LIF is a pleiotropic cytokine with roles in several different systems. It is involved in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and may also have a role in immune tolerance at the maternal-fetal interface.
Description: LIF is a pleiotropic cytokine produced at the maternal-fetal interface which has been shown to play an essential role in implantation in mice. It is produced in high amounts by the human endometrium and the trophoblast itself, and its receptors are present on cytotrophoblast cells. LIF could thus play a role in modulating HLA-G production and immune tolerance at the maternal-fetal interface. The gene maps to 22q11-q12.2, between the Philadelphia translocation BCR gene and the breakpoint of the translocation in cell line GM2324 at 22q12.2.
Description: LIF is a pleiotropic cytokine produced at the maternal-fetal interface which has been shown to play an essential role in implantation in mice. This gene is mapped to 22q11-q12.2, between the Philadelphia translocation BCR gene and the breakpoint of the translocation in cell line GM2324 at 22q12.2. LIF is produced in high amounts by the human endometrium and the trophoblast itself, and LIF receptors are present on cytotrophoblast cells. It could, thus, play a role in modulating HLA-G production and immune tolerance at the maternal-fetal interface.
Description: Quantitativesandwich ELISA kit for measuring Mouse Leukemia inhibitory factor, LIF in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Mouse Leukemia inhibitory factor, LIF in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Leukemia Inhibitory Factor (LIF) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Leukemia Inhibitory Factor (LIF) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich CLIA kit for quantitative measurement of Mouse LIF (Leukemia Inhibitory Factor) in samples from Serum, Plasma, Cell supernatant
ELISA kit for Mouse LIF (Leukemia Inhibitory Factor)
Description: A sandwich ELISA kit for quantitative measurement of Mouse LIF (Leukemia Inhibitory Factor) in samples from Serum, Plasma, Cell supernatant
LIF Leukemia Inhibitory Factor Mouse Recombinant Protein
Description: Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. ;The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human LIF . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human LIF . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody for detection of LIF from Human. This LIF antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human LIF
Description: A polyclonal antibody for detection of LIF from Human. This LIF antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human LIF
Description: A polyclonal antibody for detection of LIF from Human. This LIF antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human LIF
Description: LIFR also known as CD118 (Cluster of Differentiation 118), is a subunit of a receptor for leukemia inhibitory factor. This gene encodes a protein that belongs to the type I cytokine receptor family. This protein combines with a high-affinity converter subunit, gp130, to form a receptor complex that mediates the action of the leukemia inhibitory factor, a polyfunctional cytokine that is involved in cellular differentiation, proliferation and survival in the adult and the embryo. Mutations in this gene cause Schwartz-Jampel syndrome type 2, a disease belonging to the group of the bent-bone dysplasias. A translocation that involves the promoter of this gene, t(5;8)(p13;q12) with the pleiomorphic adenoma gene 1, is associated with salivary gland pleiomorphic adenoma, a common type of benign epithelial tumor of the salivary gland. Multiple splice variants encoding the same protein have been found for this gene.
Description: The protein encoded by this gene is a pleiotropic cytokine with roles in several different systems. It is involved in the induction of hematopoietic differentiation in normal and myeloid leukemia cells, induction of neuronal cell differentiation, regulator of mesenchymal to epithelial conversion during kidney development, and may also have a role in immune tolerance at the maternal-fetal interface. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human LIF (Center). This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human LIF (Internal). This antibody is tested and proven to work in the following applications:
Lif sgRNA CRISPR/Cas9 All-in-One Lentivector set (Mouse)
Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Murine LIF is a 19.9 kDa protein containing 180 amino acids residues, including three disulfide bonds.
Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Human LIF is a 19.7 kDa protein containing 180 amino acid residues, including three disulfide bonds.
Description: Leukemia Inhibitory Factor (LIF) is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid level. Human LIF is equally active on human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells than human LIF.
Description: Mouse Leukemia inhibitory factor（lif）is a secreted protein which belongs to the LIF/OSM family.LIF has been implicated in a many physiological processes including development, hematopoiesis, bone metabolism, and inflammation. it 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.
Description: Leukemia inhibitory factor, or LIF, an interleukin 6 class cytokine, is a protein in cells that affects cell growth and development.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. Removal of LIF pushes stem cells toward differentiation, but they retain their proliferative potential or pluripotency. Therefore LIF is used in mouse embryonic stem cell culture. It is necessary to maintain the stem cells in an undifferentiated state, however genetic manipulation of embryonic stem cells allows for LIF independent growth, notably overexpression of the gene Nanog. LIF is not required for culture of human embryonic stem cells.
Description: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also 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 activates JAK & STAT signaling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signaling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signaling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF.
In addition, a anti the body of the N terminus of VP1u disrupted virus internalization, but only if it is present during and after the attachment of the virus, which indicates the involvement of these regions in the binding events required for internalization.
