NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
Protein processing and production is often hampered by the formation of aggregates that restrict and complicate
the handling of proteins, antibodies and enzymes. NVoy is designed to minimise the sequential losses in consecutive
protein processing steps which would otherwise dramatically reduce the overall protein yield.
BLO: Transferring the macromolecule from gel to membrane followed by detection on the membrane using antibody is k/a blotting
molecular methods used to identify and measure specific DNA, RNA and protein in complex biological mixtures.
It is the technique för
transferring DNA, RNA and proteins onto a carrier so they can be separated, and often follows the use of a gel electrophoresis.
IMMUNO BLOTTING:
Immunoblotting techniques use antibodies to identify target proteins .
They involve identification of protein target via antigen-antibody (or protein-ligand) specific reactions.
The Southern blot is used for transferring DNA,.
The Northern blot for RNA
The western blot for PROTEIN.
The Eastern blot for PROTEIN, post-translational modifications (PTMS) .
WESTERN BLOTTING:
Principle:
Western blotting technique is used for identification of particular protein from the mixture of protein.
In this method labelled antibody against particular protein is used identify the desired protein, so it is a specific test.
Western blotting is also known as immunoblotting because it uses antibodies to detect the protein.
METHODOLOGY:
Extraction of protein
2. Gel electrophoresis: SDS PAGE
3. Blotting: electrical or capillary blotting
4. Blocking: BSA
5. Treatment with primary antibody
6. Treatment with secondary antibody( enzyme labelled anti Ab)
7. Treatment with specific substrate; if enzyme is alkaline phosphatase, substrate is p-nitro phenyl phosphate which give color.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
NVoy technology is a quantum leap in protein processing, production and analysis. It uses proprietary NV polymers to enhance protein solubility and stability through the formation of multi-point reversible complexes with proteins without altering their structure.
Protein processing and production is often hampered by the formation of aggregates that restrict and complicate
the handling of proteins, antibodies and enzymes. NVoy is designed to minimise the sequential losses in consecutive
protein processing steps which would otherwise dramatically reduce the overall protein yield.
BLO: Transferring the macromolecule from gel to membrane followed by detection on the membrane using antibody is k/a blotting
molecular methods used to identify and measure specific DNA, RNA and protein in complex biological mixtures.
It is the technique för
transferring DNA, RNA and proteins onto a carrier so they can be separated, and often follows the use of a gel electrophoresis.
IMMUNO BLOTTING:
Immunoblotting techniques use antibodies to identify target proteins .
They involve identification of protein target via antigen-antibody (or protein-ligand) specific reactions.
The Southern blot is used for transferring DNA,.
The Northern blot for RNA
The western blot for PROTEIN.
The Eastern blot for PROTEIN, post-translational modifications (PTMS) .
WESTERN BLOTTING:
Principle:
Western blotting technique is used for identification of particular protein from the mixture of protein.
In this method labelled antibody against particular protein is used identify the desired protein, so it is a specific test.
Western blotting is also known as immunoblotting because it uses antibodies to detect the protein.
METHODOLOGY:
Extraction of protein
2. Gel electrophoresis: SDS PAGE
3. Blotting: electrical or capillary blotting
4. Blocking: BSA
5. Treatment with primary antibody
6. Treatment with secondary antibody( enzyme labelled anti Ab)
7. Treatment with specific substrate; if enzyme is alkaline phosphatase, substrate is p-nitro phenyl phosphate which give color.
Following is my journal documentation during Master's in Biotechnology completed in 2015. I do understand many changes would've occurred in the curriculum since then, but the basics seldom change. Kindly absorb as per your need.
The first step in sample preparation is isolating proteins from their source. Usually, proteins are isolated from cells or tissues via lysis. Lysis breaks down the cell membrane to separate proteins from the non-soluble parts of the cell. A number of lysis buffers can be used to prepare samples for western blotting.
Biological Buffers & Reagents are critical tools for every life sciences laboratory to get accurate and trusted results. Our Time-saving solutions are free of toxicity and have great stability, a very precise pH, and showing minimal salt-driven effects.
Canvax™ offers a wide range of Molecular Biology Grade solutions ideal for a wide range of common applications, like PBS, TBS, Tris-Glycine, EDTA, TE, TAE, TBE or Tris, with a DNAse, RNase or protease-free guarantee.
Pharmaceutical Biotechnology Research Presentation : Recombinant Streptokinase
Dr. Godfrey Mazhandu
Professor Peivand Pirouzi Inc. -
Copyright 2015 - Professor Peivand Pirouzi Inc., International Corporate Training, Canada
All rights reserved
Protecting Protein Stability with a Novel Grade of SucroseMerck Life Sciences
Sucrose is one of the most widely used stabilizers in marketed drug products, ensuring the chemical and physical stability of the therapeutic protein. A challenge with the use of sucrose as an excipient is that nanoparticle impurities (NPI) can originate from the raw materials or be introduced during production.
In this whitepaper, you can find information on NPIs found in commercially available sucrose, their origin and impact on protein stability; and on a novel sucrose purification process designed to minimize the presence of NPIs.
To find more information about this novel grade of sucrose, please visit our website: https://www.sigmaaldrich.com/product/mm/103789
And to learn more about protein stabilization of biomolecules in general, please follow this link: https://www.sigmaaldrich.com/products/pharma-and-biopharma-manufacturing/formulation/protein-stabilizers
IntroductionIn terms of total production tonnages used f.docxvrickens
Introduction
In terms of total production tonnages used for food, wheat is currently second to rice as the main human food crop and is the leading source of vegetable protein in human nutrition (Nutrient Data Laboratory). Aphids (Order Hemiptera) are major insect pests of world agriculture, damaging crops by removing photoassimilates and vectoring numerous plant viruses (Smith and Boyko, 2007). The grain aphid (Sitobion avenae) is considered a serious pest of commercial wheat in the UK. Many aphid species can develop resistance to insecticides (Devonshire and Field, 1991), and restrictions on the availability of active ingredients for insecticide production in Europe (European Directives 91/414/EEC) has prioritized research on crop varieties with resistance to aphid pests in UK agriculture (Painter, 1951; Panda and Kush, 1995; Smith, 2005). Most commercial wheat varieties have very little resistance to aphid pests (Lee, 1984; Dedryver and Di Pietro, 1984; Di Pietro and Dedryver, 1986; Migui, 2002; Migui and Lamb, 2003), with at best partial antibiosis, antixenosis and tolerancein some winter varieties (Lowe, 1984a; Lowe, 1984b; Havlícková, 1993). Wheat genetics are more complicated than that of most other crop species. Some wheat species are diploid, with two sets of chromosomes, but many are stable polyploids, with four sets of chromosomes (tetraploid) or six (hexaploid). Modern wheat varieties grown in the U.K. are hexaploid and have low genetic diversity for insect resistance traits (Ferry et al, 2011; Ogbonnaya et al, 2013; niab.com).
Diploid wheat (T. monococcum) lines have been observed to exhibit high levels of resistance against S. avenae (Migui and Lamb, 2003; 2004; Ferry et al, 2011). However, no previous studies have been carried out in these lines to investigate differentially expressed genes in response to aphid infestation. Therefore, differential proteomic analysis is being employed to identify putative defence responses in diploid wheat lines (Triticum monococcum L.) when subjected to grain aphid (S. avenae) feeding in order to better understand the basis of this observed resistance/tolerance.
In this lab you will conduct a 2D-electrophoresis separation of the wheat leaf proteome.
Methods
It is essential that you retrieve the full lab manual produced by GE healthcare for 2D electrophoresis:
Step 1 - Sample Solubilization
This has been done for you.
In this experiment 200mg of wheat leaf was ground in liquid nitrogen to a fine powder. The protein pellets available to you have been incubated in 10% (w/v) trichloroacetic acid/ acetone with 0.07% v/v 2-mercaptoethanol at -20 °C for 16 hours and then centrifuged at 35 000 x g for 20 mins.
> The pellets were washed with ice-cold acetone (0.07% 2-mercaptoethanol) 4-6 times and finally incubated at -20 °C for 1 h, and centrifuged at 12 000 x g for 15 min.
>>An acetone wash using 1 part sample: 3 parts acetone (w/v) was performed, the sample was vortexed to disperse pelle ...
NIZO Plant Protein Functionality Conference on October 21-22 gathered around 450 attendees to discuss the recent findings and innovations on plant proteins. Research team leader Emilia Nordlund gave a keynote presentation on bioprocessing technologies to improve the plant protein functionality.
Circular dichroism spectroscopy is an analytical technique used to estimate the secondary and tertiary structure of proteins. This technique can be used to confirm whether structure has been retained during protein processing, but is frequently adversely affected by additives such as solubility enhancers and detergents.
The western blot technique uses gel electrophoresis to separate proteins in a tissue homogenate or extract by molecular weight. The separated proteins on the gel are then transferred to a membrane (usually nitrocellulose or PVDF) which is then incubated with an antibody specific for a target protein. The protein of interest can be visualised using conjugated secondary antibodies and detection reagents.
Do you have a technical question? Get in touch: info@stjohnslabs.com
Protocol series - http://www.stjohnslabs.com/services/video-protocol-series
Potassium sorbate, sodium benzoate and citric acid together with vacuum packing have extended puree shelf life by 3-6 months in our trials at ambient conditions (T<25C).
However, the gap lies on the efficacy of the preservative combination in retarding or stopping the growth of harmful pathogens in the puree, and also their effects on β-carotene retention is unknown.
ELISA is a well know term that is an abbreviation of Enzyme Linked Immunosorbent Assay. This microplate based technique relies on the use of an antibody that has been linked to an enzyme. In the presence of an appropriate substrate, enzymatic activity produces a color change as the ELISA readout, which can be measured and provides information about the presence and quantity of the target antigen in the sample material.
Electrophoresis is a simple, rapid, and highly sensitive analytical technique to study the properties of proteins and nucleic acids, and has become a principle tool in analytical chemistry, biochemistry, and molecular biology. Polyacrylamide gel electrophoresis (PAGE) can be used to analyze the size, amount, purity, and isoelectric point of polypeptides and proteins. Sodium dodecyl sulfate polyacrylamide discontinuous gel electrophoresis (SDS PAGE) is the most commonly used system whereby proteins become separated strictly by their size, but there are different variations of this technique.
Antibody-oligonucleotide (Ab-Oligo) conjugates have been used in
numerous applications from diagnostics to therapeutics and were
developed through an unmet need for precise and efficient detection of low-abundance proteins. Ab-Oligo conjugates have since played a significant role in enhancing an extensive range of biological techniques that include immunological and proteomic research, biomarker discovery, clinical diagnostics – including point-of-care, as well as other novel techniques. Antibodies can be readily conjugated to oligonucleotides via their amino acid residues, making them suitable for most in vitro applications, as they possess several functional groups.
His Tag Protein Production and PurificationExpedeon
The study of protein regulation, structure, and function relies heavily on the expression and purification of recombinant proteins. Many recombinant proteins are expressed as fusion proteins, meaning that they contain an affinity / epitope tag. A tag is a short sequence of DNA that codes for a specific amino acid, which is frequently inserted into a target gene at the point of coding for expression at either the N or C terminal of the protein required.
Following is my journal documentation during Master's in Biotechnology completed in 2015. I do understand many changes would've occurred in the curriculum since then, but the basics seldom change. Kindly absorb as per your need.
The first step in sample preparation is isolating proteins from their source. Usually, proteins are isolated from cells or tissues via lysis. Lysis breaks down the cell membrane to separate proteins from the non-soluble parts of the cell. A number of lysis buffers can be used to prepare samples for western blotting.
Biological Buffers & Reagents are critical tools for every life sciences laboratory to get accurate and trusted results. Our Time-saving solutions are free of toxicity and have great stability, a very precise pH, and showing minimal salt-driven effects.
Canvax™ offers a wide range of Molecular Biology Grade solutions ideal for a wide range of common applications, like PBS, TBS, Tris-Glycine, EDTA, TE, TAE, TBE or Tris, with a DNAse, RNase or protease-free guarantee.
Pharmaceutical Biotechnology Research Presentation : Recombinant Streptokinase
Dr. Godfrey Mazhandu
Professor Peivand Pirouzi Inc. -
Copyright 2015 - Professor Peivand Pirouzi Inc., International Corporate Training, Canada
All rights reserved
Protecting Protein Stability with a Novel Grade of SucroseMerck Life Sciences
Sucrose is one of the most widely used stabilizers in marketed drug products, ensuring the chemical and physical stability of the therapeutic protein. A challenge with the use of sucrose as an excipient is that nanoparticle impurities (NPI) can originate from the raw materials or be introduced during production.
In this whitepaper, you can find information on NPIs found in commercially available sucrose, their origin and impact on protein stability; and on a novel sucrose purification process designed to minimize the presence of NPIs.
To find more information about this novel grade of sucrose, please visit our website: https://www.sigmaaldrich.com/product/mm/103789
And to learn more about protein stabilization of biomolecules in general, please follow this link: https://www.sigmaaldrich.com/products/pharma-and-biopharma-manufacturing/formulation/protein-stabilizers
IntroductionIn terms of total production tonnages used f.docxvrickens
Introduction
In terms of total production tonnages used for food, wheat is currently second to rice as the main human food crop and is the leading source of vegetable protein in human nutrition (Nutrient Data Laboratory). Aphids (Order Hemiptera) are major insect pests of world agriculture, damaging crops by removing photoassimilates and vectoring numerous plant viruses (Smith and Boyko, 2007). The grain aphid (Sitobion avenae) is considered a serious pest of commercial wheat in the UK. Many aphid species can develop resistance to insecticides (Devonshire and Field, 1991), and restrictions on the availability of active ingredients for insecticide production in Europe (European Directives 91/414/EEC) has prioritized research on crop varieties with resistance to aphid pests in UK agriculture (Painter, 1951; Panda and Kush, 1995; Smith, 2005). Most commercial wheat varieties have very little resistance to aphid pests (Lee, 1984; Dedryver and Di Pietro, 1984; Di Pietro and Dedryver, 1986; Migui, 2002; Migui and Lamb, 2003), with at best partial antibiosis, antixenosis and tolerancein some winter varieties (Lowe, 1984a; Lowe, 1984b; Havlícková, 1993). Wheat genetics are more complicated than that of most other crop species. Some wheat species are diploid, with two sets of chromosomes, but many are stable polyploids, with four sets of chromosomes (tetraploid) or six (hexaploid). Modern wheat varieties grown in the U.K. are hexaploid and have low genetic diversity for insect resistance traits (Ferry et al, 2011; Ogbonnaya et al, 2013; niab.com).
Diploid wheat (T. monococcum) lines have been observed to exhibit high levels of resistance against S. avenae (Migui and Lamb, 2003; 2004; Ferry et al, 2011). However, no previous studies have been carried out in these lines to investigate differentially expressed genes in response to aphid infestation. Therefore, differential proteomic analysis is being employed to identify putative defence responses in diploid wheat lines (Triticum monococcum L.) when subjected to grain aphid (S. avenae) feeding in order to better understand the basis of this observed resistance/tolerance.
In this lab you will conduct a 2D-electrophoresis separation of the wheat leaf proteome.
Methods
It is essential that you retrieve the full lab manual produced by GE healthcare for 2D electrophoresis:
Step 1 - Sample Solubilization
This has been done for you.
In this experiment 200mg of wheat leaf was ground in liquid nitrogen to a fine powder. The protein pellets available to you have been incubated in 10% (w/v) trichloroacetic acid/ acetone with 0.07% v/v 2-mercaptoethanol at -20 °C for 16 hours and then centrifuged at 35 000 x g for 20 mins.
> The pellets were washed with ice-cold acetone (0.07% 2-mercaptoethanol) 4-6 times and finally incubated at -20 °C for 1 h, and centrifuged at 12 000 x g for 15 min.
>>An acetone wash using 1 part sample: 3 parts acetone (w/v) was performed, the sample was vortexed to disperse pelle ...
NIZO Plant Protein Functionality Conference on October 21-22 gathered around 450 attendees to discuss the recent findings and innovations on plant proteins. Research team leader Emilia Nordlund gave a keynote presentation on bioprocessing technologies to improve the plant protein functionality.
Circular dichroism spectroscopy is an analytical technique used to estimate the secondary and tertiary structure of proteins. This technique can be used to confirm whether structure has been retained during protein processing, but is frequently adversely affected by additives such as solubility enhancers and detergents.
The western blot technique uses gel electrophoresis to separate proteins in a tissue homogenate or extract by molecular weight. The separated proteins on the gel are then transferred to a membrane (usually nitrocellulose or PVDF) which is then incubated with an antibody specific for a target protein. The protein of interest can be visualised using conjugated secondary antibodies and detection reagents.
Do you have a technical question? Get in touch: info@stjohnslabs.com
Protocol series - http://www.stjohnslabs.com/services/video-protocol-series
Potassium sorbate, sodium benzoate and citric acid together with vacuum packing have extended puree shelf life by 3-6 months in our trials at ambient conditions (T<25C).
However, the gap lies on the efficacy of the preservative combination in retarding or stopping the growth of harmful pathogens in the puree, and also their effects on β-carotene retention is unknown.
ELISA is a well know term that is an abbreviation of Enzyme Linked Immunosorbent Assay. This microplate based technique relies on the use of an antibody that has been linked to an enzyme. In the presence of an appropriate substrate, enzymatic activity produces a color change as the ELISA readout, which can be measured and provides information about the presence and quantity of the target antigen in the sample material.
Electrophoresis is a simple, rapid, and highly sensitive analytical technique to study the properties of proteins and nucleic acids, and has become a principle tool in analytical chemistry, biochemistry, and molecular biology. Polyacrylamide gel electrophoresis (PAGE) can be used to analyze the size, amount, purity, and isoelectric point of polypeptides and proteins. Sodium dodecyl sulfate polyacrylamide discontinuous gel electrophoresis (SDS PAGE) is the most commonly used system whereby proteins become separated strictly by their size, but there are different variations of this technique.
Antibody-oligonucleotide (Ab-Oligo) conjugates have been used in
numerous applications from diagnostics to therapeutics and were
developed through an unmet need for precise and efficient detection of low-abundance proteins. Ab-Oligo conjugates have since played a significant role in enhancing an extensive range of biological techniques that include immunological and proteomic research, biomarker discovery, clinical diagnostics – including point-of-care, as well as other novel techniques. Antibodies can be readily conjugated to oligonucleotides via their amino acid residues, making them suitable for most in vitro applications, as they possess several functional groups.
His Tag Protein Production and PurificationExpedeon
The study of protein regulation, structure, and function relies heavily on the expression and purification of recombinant proteins. Many recombinant proteins are expressed as fusion proteins, meaning that they contain an affinity / epitope tag. A tag is a short sequence of DNA that codes for a specific amino acid, which is frequently inserted into a target gene at the point of coding for expression at either the N or C terminal of the protein required.
GELFrEE® 8100 Fractionation System Tech NoteExpedeon
Successful sample preparation is a key step during any analytical
procedure and begins with a defined experimental design. Important steps in sample preparation include proteolytic digestion of proteins into peptide fragments, and peptide fractionation. This is especially important prior to applications such as mass spectrometry (MS).
Antibody-oligonucleotide (Ab-Oligo) conjugates have been used in
numerous applications from diagnostics to therapeutics and were
developed through an unmet need for precise and efficient detection of low-abundance proteins.
Proteomics of small proteins from plant tissuesExpedeon
Small genes and the proteins that they encode can play important biological roles including signaling, development, and mediation of plant-microbe interactions in organisms ranging from bacteria to plants to mammals (Frith et al.; Basrai et al.; Galindo et al.; Hemm et al. 2008, 2010; Kastenmeyer et al.). However, genes that encode proteins containing <100 residues are difficult to identify reliably solely by DNA sequence analysis (Dinger et al.)
Proteomic profiling of fractionated post-myocardial infarctionExpedeon
Acute myocardial infarction remains a leading cause of morbidity and mortality worldwide.Heart failure is the result of adverse remodeling of the collagenous scar that replaces the
damaged myocardium after MI. Markers of LV remodeling can be either identified in the circulation (e.g. serum or plasma) or detected in the heart by imaging technologies or biopsy.
Top down proteomics of soluble and integral membrane proteinsExpedeon
Mitochondria provide important cellular functions including
oxidative phosphorylation, fatty acid biosynthesis, and acting as
gatekeepers to apoptosis.
GELFrEE1 affords rapid mass-based protein separation over a range 10-150 kDa. Here, we demonstrate a multiplexed design enabling increased loading capacity and throughput. We
demonstrate comprehensive analysis of the yeast proteome using GELFrEE coupled to LC-MS/MS analysis.
Identification and characterization of intact proteins in complex mixturesExpedeon
The ability to fully characterize proteins in their intact forms allows thorough biological investigation of the functional importance of changes such as post-translational modifications, protein isoforms/sequence variations, and protease cleavages.
Improved coverage of the proteome using gel eluted liquidExpedeon
It has long been understood that sample fractionation is critically important to generating quality, comprehensive proteomics data. In spite of the continual improvements in speed and sensitivity of mass spectrometers, these instruments are still unable to adequately overcome the enormous challenge
of most biological samples without multiple dimensions of separation prior to mass analysis.
Optimization of experimental protocols for cellular lysisExpedeon
In this project, we have compared existing sample preparation methods for proteomics studies against newly developed FASP method and our in-house developed SDS-TCA protocol. For our
preliminary studies, we have chosen a very well characterized soil microbe Pseudomonas putida.
Characterization of intact antibodies by pre-fractionation using gel electrop...Expedeon
Antibodies represent an important class of proteins due to their central role in the immune response. Moreover, there is an increasing interest in the use of recombinant antibodies as novel drug therapies.
Advances in Capillary Liquid Chromatography for High-Throughput Top Down Prot...Expedeon
Top Down proteomics has benefited greatly from advances in
mass spectrometry instrumentation and database searching,
yet it has been hindered by the lack of robust separation
platforms for intact proteins. Recently, the use of Gel-Eluted
Liquid Fraction Entrapment Electrophoresis (GELFrEE)1,2
followed by capillary liquid chromatography-MS/MS has
enabled hundreds of Top Down identifications from a single
proteome run.
Fast, simple and-cost-effective immunoassay developmet validation and sample ...Expedeon
SPARCL (Spatial Proximity Analyte Reagent Capture Luminescence) is a novel homogeneous proximity assay technology utilizing flash chemiluminescence detection without solid support or wash steps.
Lightning-Link® is an innovative technology that enables direct labeling of antibodies, proteins, peptides or other
biomolecules with only 30 seconds hands-on time.
The increased availability of biomedical data, particularly in the public domain, offers the opportunity to better understand human health and to develop effective therapeutics for a wide range of unmet medical needs. However, data scientists remain stymied by the fact that data remain hard to find and to productively reuse because data and their metadata i) are wholly inaccessible, ii) are in non-standard or incompatible representations, iii) do not conform to community standards, and iv) have unclear or highly restricted terms and conditions that preclude legitimate reuse. These limitations require a rethink on data can be made machine and AI-ready - the key motivation behind the FAIR Guiding Principles. Concurrently, while recent efforts have explored the use of deep learning to fuse disparate data into predictive models for a wide range of biomedical applications, these models often fail even when the correct answer is already known, and fail to explain individual predictions in terms that data scientists can appreciate. These limitations suggest that new methods to produce practical artificial intelligence are still needed.
In this talk, I will discuss our work in (1) building an integrative knowledge infrastructure to prepare FAIR and "AI-ready" data and services along with (2) neurosymbolic AI methods to improve the quality of predictions and to generate plausible explanations. Attention is given to standards, platforms, and methods to wrangle knowledge into simple, but effective semantic and latent representations, and to make these available into standards-compliant and discoverable interfaces that can be used in model building, validation, and explanation. Our work, and those of others in the field, creates a baseline for building trustworthy and easy to deploy AI models in biomedicine.
Bio
Dr. Michel Dumontier is the Distinguished Professor of Data Science at Maastricht University, founder and executive director of the Institute of Data Science, and co-founder of the FAIR (Findable, Accessible, Interoperable and Reusable) data principles. His research explores socio-technological approaches for responsible discovery science, which includes collaborative multi-modal knowledge graphs, privacy-preserving distributed data mining, and AI methods for drug discovery and personalized medicine. His work is supported through the Dutch National Research Agenda, the Netherlands Organisation for Scientific Research, Horizon Europe, the European Open Science Cloud, the US National Institutes of Health, and a Marie-Curie Innovative Training Network. He is the editor-in-chief for the journal Data Science and is internationally recognized for his contributions in bioinformatics, biomedical informatics, and semantic technologies including ontologies and linked data.
Nutraceutical market, scope and growth: Herbal drug technologyLokesh Patil
As consumer awareness of health and wellness rises, the nutraceutical market—which includes goods like functional meals, drinks, and dietary supplements that provide health advantages beyond basic nutrition—is growing significantly. As healthcare expenses rise, the population ages, and people want natural and preventative health solutions more and more, this industry is increasing quickly. Further driving market expansion are product formulation innovations and the use of cutting-edge technology for customized nutrition. With its worldwide reach, the nutraceutical industry is expected to keep growing and provide significant chances for research and investment in a number of categories, including vitamins, minerals, probiotics, and herbal supplements.
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
A brief information about the SCOP protein database used in bioinformatics.
The Structural Classification of Proteins (SCOP) database is a comprehensive and authoritative resource for the structural and evolutionary relationships of proteins. It provides a detailed and curated classification of protein structures, grouping them into families, superfamilies, and folds based on their structural and sequence similarities.