The complete sequence of a heterochromatic island from a higher eukaryote. The Cold Spring Harbor Laboratory, Washington University Genome Sequencing Center, and PE Biosystems Arabidopsis Sequencing Consortium.
Heterochromatin, constitutively condensed chromosomal material, is widespread among eukaryotes but incompletely characterized at the nucleotide level. We have sequenced and analyzed 2.1 megabases (Mb) of Arabidopsis thaliana chromosome 4 that includes 0.5-0.7 Mb of isolated heterochromatin that resembles the chromosomal knobs described by Barbara McClintock in maize.
This isolated region has a low density of expressed genes, low levels of recombination and a low incidence of genetrap insertion. Satellite repeats were absent, but tandem arrays of long repeats and many transposons were found. Methylation of these sequences was dependent on chromatin remodeling. Clustered repeats were associated with condensed chromosomal domains elsewhere. The complete sequence of a heterochromatic island provides an opportunity to study sequence determinants of chromosome condensation.
Description: Galectin-1, also known as L14, BHL and galaptin, is a monomeric or homodimeric prototype galectin that is expressed in a variety of cells and tissues including muscle, heart, liver, prostate, lymph nodes, spleen, thymus, placenta, testis, retina, macrophages, B cells, T cells, dendritic cells, and tumor cells. It preferentially binds laminin, fibronectin, 90K/Mac2BP, CD45, CD43, CD7, CD2, CD3, and ganglioside GM1. Galectin-1 modulates cell growth and proliferation, either positively or negatively, depending on the cell type and activation status. It controls cell survival by inducing apoptosis of activated T cells and immature thymocytes. It modulates cytokine secretion by inducing Th2 type cytokines and inhibiting proinflammatory cytokine production. Galectin1 can also modulate cel-lcell as well as cell-lmatrix interactions and depending on the cell type and developmental stage, promote cell attachment or detachment. Galectin-1 has immunosuppressive and anti-inflammatory properties and has been shown to suppress acute and chronic inflammation and autoimmunity. Human and mouse galectin1 share about 88% amino acid sequence similarity.
Description: Galectin-1, also known as L14, BHL and galaptin, is a monomeric or homodimeric prototype galectin that is expressed in a variety of cells and tissues including muscle, heart, liver, prostate, lymph nodes, spleen, thymus, placenta, testis, retina, macrophages, B cells, T cells, dendritic cells, and tumor cells. It preferentially binds laminin, fibronectin, 90K/Mac2BP, CD45, CD43, CD7, CD2, CD3, and ganglioside GM1. Galectin-1 modulates cell growth and proliferation, either positively or negatively, depending on the cell type and activation status. It controls cell survival by inducing apoptosis of activated T cells and immature thymocytes. It modulates cytokine secretion by inducing Th2 type cytokines and inhibiting proinflammatory cytokine production. Galectin1 can also modulate cel-lcell as well as cell-lmatrix interactions and depending on the cell type and developmental stage, promote cell attachment or detachment. Galectin-1 has immunosuppressive and antiinflammatory properties and has been shown to suppress acute and chronic inflammation and autoimmunity. Human and mouse galectin1 share about 88% amino acid sequence similarity.
Description: Galectin-1, also known as L14, BHL and galaptin, is a monomeric or homodimeric prototype galectin that is expressed in a variety of cells and tissues including muscle, heart, liver, prostate, lymph nodes, spleen, thymus, placenta, testis, retina, macrophages, B cells, T cells, dendritic cells, and tumor cells. It preferentially binds laminin, fibronectin, 90K/Mac2BP, CD45, CD43, CD7, CD2, CD3, and ganglioside GM1. Galectin-1 modulates cell growth and proliferation, either positively or negatively, depending on the cell type and activation status. It controls cell survival by inducing apoptosis of activated T cells and immature thymocytes. It modulates cytokine secretion by inducing Th2 type cytokines and inhibiting proinflammatory cytokine production. Galectin1 can also modulate cel-lcell as well as cell-lmatrix interactions and depending on the cell type and developmental stage, promote cell attachment or detachment. Galectin-1 has immunosuppressive and antiinflammatory properties and has been shown to suppress acute and chronic inflammation and autoimmunity. Human and mouse galectin1 share about 88% amino acid sequence similarity.
Description: A sandwich ELISA for quantitative measurement of Human Galectin 1 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A sandwich ELISA for quantitative measurement of Human Galectin 1 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A sandwich ELISA for quantitative measurement of Human Galectin 1 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: Galectin-1 is a member of the galectin family, and binds B-galactosidase moieties on glycoproteins or glycolipids. Galectins are primarily involved in modulation of cell-cell and cell-matrix interactions. Galectin-1 acts as a negative regulator of immunity, promoting immune suppression and lessening the inflammatory response. Galectin-1 binds CD45, CD3 and CD4, resulting in the inhibition of CD45 phosphatase dependant dephosphorylation of lyn kinase, as well as a number of other immune related receptors. Due to its function as a negative regulator of the immune response, and role inducing apoptosis in activated Th1 and Th17 cells, it is commonly found upregulated around malignant tumours. It has also been implicated as having a role in the development of immune tolerance during pregnancy, and is highly expressed at the maternal-fetal interface. As a dimer it down-regulates neutrophils by inducing exposure of phosphatidylserine, thereby marking the cell for apoptosis. It shares approximately 88% and 90% sequence similarity with mouse and rat galectin-1, respectively. Recombinant Human Galectin-1 is a 14.9kDa protein.
Description: Galectin-1 is a member of the galectin family, and binds B-galactosidase moieties on glycoproteins or glycolipids. Galectins are primarily involved in modulation of cell-cell and cell-matrix interactions. Galectin-1 acts as a negative regulator of immunity, promoting immune suppression and lessening the inflammatory response. Galectin-1 binds CD45, CD3 and CD4, resulting in the inhibition of CD45 phosphatase dependant dephosphorylation of lyn kinase, as well as a number of other immune related receptors. Due to its function as a negative regulator of the immune response, and role inducing apoptosis in activated Th1 and Th17 cells, it is commonly found upregulated around malignant tumours. It has also been implicated as having a role in the development of immune tolerance during pregnancy, and is highly expressed at the maternal-fetal interface. As a dimer it down-regulates neutrophils by inducing exposure of phosphatidylserine, thereby marking the cell for apoptosis. It shares approximately 88% and 90% sequence similarity with mouse and rat galectin-1, respectively. Recombinant Human Galectin-1 is a 14.9kDa protein.
Description: Galectin-1 is a member of the galectin family, and binds B-galactosidase moieties on glycoproteins or glycolipids. Galectins are primarily involved in modulation of cell-cell and cell-matrix interactions. Galectin-1 acts as a negative regulator of immunity, promoting immune suppression and lessening the inflammatory response. Galectin-1 binds CD45, CD3 and CD4, resulting in the inhibition of CD45 phosphatase dependant dephosphorylation of lyn kinase, as well as a number of other immune related receptors. Due to its function as a negative regulator of the immune response, and role inducing apoptosis in activated Th1 and Th17 cells, it is commonly found upregulated around malignant tumours. It has also been implicated as having a role in the development of immune tolerance during pregnancy, and is highly expressed at the maternal-fetal interface. As a dimer it down-regulates neutrophils by inducing exposure of phosphatidylserine, thereby marking the cell for apoptosis. It shares approximately 88% and 90% sequence similarity with mouse and rat galectin-1, respectively. Recombinant Human Galectin-1 is a 14.9kDa protein.
Supramolecular insight into the substitution of sulfur by selenium, based on crystal structures, quantum-chemical calculations and biosystem recognition
Statistical analysis of data from crystal structures extracted from the Cambridge Structural Database (CSD) has shown that S and Se atoms display a similar tendency towards specific types of interaction if they are part of a fragment that corresponds to the side chains of cysteine (Cys), methionine (Met) selenocysteine (Sec) and selenomethionine (Mse).
The most numerous are structures with C-H…Se and C-H…S interactions (∼80%), notably less numerous are structures with Se…Se and S…S interactions (∼5%), and Se…π and S…π interactions are the least numerous.
The results of quantum-chemical calculations have indicated that C-H…Se (∼-0.8 kcal mol-1) and C-H...S interactions are weaker than the most stable parallel interaction (∼-3.3 kcal mol-1) and electrostatic interactions of σ/π type (∼-2.6 kcal mol-1).
Their significant presence can be explained by the abundance of CH groups compared with the numbers of Se and S atoms in the crystal structures, and also by the influence of substituents bonded to the Se or S atom that further reduce their possibilities for interacting with species from the environment.
This can also offer an explanation as to why O-H…Se (∼-4.4 kcal mol-1) and N-H…Se interactions (∼-2.2 kcal mol-1) are less numerous. Docking studies revealed that S and Se rarely participate in interactions with the amino acid residues of target enzymes, mostly because those residues preferentially interact with the substituents bonded to Se and S.
The differences between Se and S ligands in the number and positions of their binding sites are more pronounced if the substituents are polar and if there are more Se/S atoms in the ligand.
A simple biosystem for the high-yielding cascade conversion of racemic alcohols to enantiopure amines
The amination of racemic alcohols to produce enantiopure amines is an important green chemistry reaction for pharmaceutical manufacturing, requiring simple and efficient solutions. Here we developed a novel concept and the simplest system for ADH-TA-catalyzed cascade reaction to aminate racemic alcohols, which utilizes an ambidextrous ADH to oxidize a racemic alcohol, an enantioselective transaminase to convert the ketone intermediate to chiral amine, and isopropylamine to recycle PMP and NAD + cofactors via the reversed cascade reactions.
The concept was proven by using an ambidextrous CpSADH-W286A engineered from ( S )-enantioselective CpSADH as the first example of evolving ambidextrous ADHs, an enantioselective BmTA, and isopropylamine. A biosystem containing isopropylamine and the cells of E. coli (CpSADH-W286A/BmTA) expressing the two enzymes was developed for the amination of racemic alcohols to produce eight useful and high-value ( S )-amines in 72-99% yield and 98-99% ee , providing with a simple and practical solution to this type of reaction.
Evaluation of chromosomal insertion loci in the Pseudomonas putida KT2440 genome for predictable biosystems design
The development of Pseudomonas strains for industrial production of fuels and chemicals will require the integration of heterologous genes and pathways into the chromosome.
Finding the most appropriate integration site to maximize strain performance is an essential part of the strain design process. We characterized seven chromosomal loci in Pseudomonas putida KT2440 for integration of a fluorescent protein expression construct. Insertion in five of the loci did not affect growth rate, but fluorescence varied by up to 27-fold.
Three sites displaying a diversity of phenotypes with the fluorescent reporter were also chosen for the integration of a gene encoding a muconate importer. Depending on the integration locus, expression of the importer varied by approximately 3-fold and produced significant phenotypic differences. This work demonstrates the impact of the integration location on host viability, gene expression, and overall strain performance.
Description: All three isoforms of GRO or KC are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: All three isoforms of GRO or KC are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: Mouse CXCL1, also known as KC, is belonging to the CXC chemokine family. It is encoded by the GRO gene now designated CXCL1. The gene for CXCL1 was initially discovered in mouse fibroblasts by plateletderived growth factor. KC is member of the intercrine alpha (chemokine C-X-C) subfamily of chemokines. It is secreted by human melanoma cells, and also expressed by macrophages, neutrophils and epithelial cells. The functional receptor for CXCL1 has been identified as CXCR2. CXCL1 has chemotactic activity for neutrophils, and plays a role in inflammation and wound healing. Amino acid sequence of Mouse CXCL1 is approximately 60 % identical to the human CXCL1. KC was found to be involved in monocyte arrest on atherosclerotic endothelium and may also play a pathophysiological role in Alzheimer’s disease.
Description: KC Mouse Recombinant also known as N51 and GRO1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of approximately 8 kDa.;The GRO-1 is purified by proprietary chromatographic techniques.
GRO1/KC Mouse, GRO/KC (CXCL1) Mouse Recombinant Protein, His Tag
Description: GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.;GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant rat GRO/KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
