Rapid genomic and phenotypic change in response to climate warming
Predicting the distribution of plants under climate change constrained by our limited understanding of the potential for rapid adaptive evolution. In a study of experimental evolution with invasive common ragweed (Ambrosia artemisiifolia L.) we are subject to the population of the same genetic composition replicated beginning to climate warming simulations. Sequencing DNA collected from a population of parents and children showed that warming the population has genetic aberrations that are larger than their parents, rather than the control population.
In the general environment, the descendants of the population of warming shows more convergent phenotypes in seven of the nine properties of plants, with the later flowering and greater biomass of plants from a control population. For both properties, we also found significantly higher rates of genetic differentiation of phenotypic cross-generation for heating than the control population, showed a strong response to selection under heating conditions. As a measure for the rate of evolution, phenotypic and sequence differences between generations assessed using metrics Haldane.
Our approach combines the comparison between generations (allochronic) and between treatments (synchronous) in the field of study of experimental evolution and genomic data linking population with phenotypic analysis provided a strong test for the detection of rapid response to selection.
Our findings show that ragweed populations can rapidly evolve in response to climate change in a generation. Short-term evolutionary responses to climate change can exacerbate the effects of some plant invaders in the future and should be considered when making predictions about the distribution and impact of future plant invaders.
Rapid genomic and phenotypic change in response to climate warming in a widespread plant invader
Description: Small Intestine tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Small intestine tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Small intestine cancer, metastatic lymph nodes and normal tissue high density tissue microarray, 69 cases/208 core, with stage and grade data
Small intestine disease spectrum (small intestine cancer progression) tissue array
Description: Small Intestine tumor tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.
Description: Human small intestine tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human small intestine tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated small intestine tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated small intestine tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human small intestine tissue cytoplasmic protein lysate was prepared by isolating the cytoplasmic protein from whole tissue homogenates using a proprietary technique. The human small intestine tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The cytoplasmic protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, glycerol, and a cocktail of protease inhibitors. For quality control purposes, the isolated small intestine tissue cytoplasmic protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated small intestine tissue cytoplasmic protein is then Western analyzed by GAPDH antibody, and the expression level is consistent with each lot.
Description: Human small intestine tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human small intestine tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated small intestine tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated small intestine tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human small intestine tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human small intestine tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the small intestine tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The small intestine tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Small intestine carcinoma test tissue array, with normal small intestine tissues, including pathology grade, TNM and clinical stage, 6 cases/24 cores, replacing T421a
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Total Protein - Mouse Normal Tissue: Small Intestine
Description: The Multiple Species Tissue Array (MSTA) slides were designed to study protein expression patterns in different cells and tissues from multiple species. Tissue slices from three different species are mounted on each MSTA slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across different species. MSTA slides can also be used to quickly determine the species reactivity of a given antibody.
Total Protein - Liver Cirrhosis: Small Intestine: Jejunum
Genomic approaches to the synthesis of biomolecules vegetable for therapeutic applications to combat the SARS-CoV-2
COVID-19 caused by a coronavirus 2 acute respiratory syndrome (SARS-CoV-2) is a human eye with the army no vaccine or proper therapeutic molecules for the treatment identified. New drug discovery and repurposing existing drugs are being carried out; However, at the same time, research on plants to identify new therapeutic compounds or existing testing is progress at a slower pace.
In this context, genomics and biotechnology offers a variety of tools and strategies to manipulate the plant to produce products of complex biopharmaceuticals. This review mentions the scope for research on bio molecules for their potential application in treating a SARS-CoV infection-2. Strategies to edit genes and genomes, excess and silencing approaches, and molecular breeding to produce the target biomolecule in plant systems is discussed in detail. Overall, this review provides a roadmap to accelerate research using plants as a source of novel active biomolecules have therapeutic applications.
A high-throughput gene expression profiles using microarray plant biologists have provided powerful new technology to discover the function of genes and understand cellular processes. Bioinformatics has been growing rapidly to provide the necessary tools to interpret this gene expression data, but opportunities to exploit masses of data from hundreds of experiments to be dependent on the use of advanced database repository.
Data mining these resources will allow plant biologists to compare and expression profile relationships and experimental factors to uncover the functions and processes are not usually seen from analyzing a small set of microarray experiments. The in-silico analysis will be important when designing new experiments and interpret the new results.
Description: CFB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (260-764) and having a molecular mass of 59.4 kDa.;CFB is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Recombinant Human Complement Factor B/CFB (C-6His)
Description: CFB (26-259) Human Recombinant produced in E. Coli is. a single polypeptide chain containing 257 amino acids and having a molecular mass of 28.4kDa. CFB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CFB Human, Complement Factor B Human Recombinant Protein, Sf9
Description: CFB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 245 amino acids (26-259a.a.) and having a molecular mass of 27.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). CFB is expressed with a 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: Complement Factor B (CFB) belongs to the peptidase S1 family of enzymes. It is expressed by hepatocytes and macrophages and localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. CFB which is a component of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb. The active subunit Bb is a serine protease which associates with C3b to form the alternative pathway C3 convertase. Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
Description: Complement factor B is a protein that in humans is encoded by the CFB gene. This gene encodes complement factor B, a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Upon activation of the alternative pathway, it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which associates with C3b to form the alternative pathway C3 convertase. Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. This cluster includes several genes involved in regulation of the immune reaction. Polymorphisms in this gene are associated with a reduced risk of age-related macular degeneration. The polyadenylation site of this gene is 421 bp from the 5' end of the gene for complement component 2.
Description: A sandwich quantitative ELISA assay kit for detection of Rat Complement Factor B (CFB) in samples from serum, plasma or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Rat Complement Factor B (CFB) in samples from serum, plasma or other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Complement Factor B (CFB) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Complement Factor B (CFB) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Complement Factor B (CFB) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Complement Factor B (CFB) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Complement Factor B (CFB) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species.
