NTHRYS BIOTECH LABS introduces our specialized 2D Gel Electrophoresis service, designed for the sophisticated analysis of proteins. This powerful technique is pivotal for separating proteins in complex mixtures based on their isoelectric points and molecular weights, enabling detailed protein identification, quantification, and post-translational modification analysis.
Scientific Principle
Our 2D Gel Electrophoresis service combines two-dimensional polyacrylamide gel electrophoresis for a comprehensive protein analysis. The principle involves two sequential steps:
First Dimension - Isoelectric Focusing (IEF): Proteins are separated based on their isoelectric points (pI). Each protein migrates until it reaches a region in the gel where the pH equals its pI, stopping its migration.
Second Dimension - SDS-PAGE: Following IEF, the proteins are subjected to SDS-PAGE, where they are separated based on their molecular weight. This step involves running the proteins perpendicular to the first dimension, resulting in a highly resolved 2D protein map.
This approach allows for the separation of thousands of proteins simultaneously, making it an invaluable tool for proteomics research.
Applications in Research
The 2D Gel Electrophoresis service is essential for various research methodologies, including:
Proteome analysis in disease states for biomarker discovery.
Comparative proteomics to understand differential protein expression.
Identification of post-translational modifications.
Drug target identification and validation.
Quality control in biopharmaceuticals.
Fields of Science Benefiting from Our Service
Our 2D Gel Electrophoresis service is beneficial across a variety of scientific fields, including:
Proteomics and Genomics
Pharmacology and Drug Development
Cancer Research
Molecular Biology
Environmental Science
Major Advantages
Choosing NTHRYS BIOTECH LABS for your 2D Gel Electrophoresis needs offers numerous advantages:
High Resolution: Achieve unparalleled clarity and detail in protein separation and identification.
Comprehensive Analysis: Capable of analyzing complex protein mixtures to reveal minute differences between samples.
Expert Interpretation: Our team provides in-depth analysis and interpretation of gel results, offering valuable insights into your research.
Customizable Protocols: Adapted to meet specific research needs and project goals.
Protein is a macromolecule which are have a long sting of amino acids that complete the important functions in the body. They are arranged in three dimensional structures. Proteins are classified according to their number of chains of amino acids. The side chains create pockets for these structures as they fold into tertiary structures according to their chemical interactions. The extraction process includes, the first step for disrupting the cells by homogenisation, cutting smashing shearing tissue into small pieces, freezing and thawing and Sonication. Cell lysis is also done with the help of detergents that break apart the cellular proteins. The next step involves centrifugation for removing cell debris. Protein inhibitors are used for the prevention of loss of proteins. Centrifugation yields cytoplasmic proteins, and buffers can be used further for nuclear proteins.
SDS PAGE - (Sodium dodecyl Sulfate - ployacrylamide gel electrophoresis) is a method for protein separation based on mass is an electrophoretic technique. The polyacrilamide is poured onto the gel slabs for the medium of electric field, and that is discontinuous and sandwiched between two glass plates. SDS is a surfactant changing the proteins charge that helps the migration of proteins to the anode based on the charge applied by the electric field across the gel slabs. SDS is amphipathic for folding of polar and no polar sections. Gradient gels of acrylamide have larger separation ranges of molecular masses. The denatured samples are loaded onto gel polyacrylamide which are placed along with suitable electrophoresis and electrolytes. Negatively charged molecules move toward the positive side, with larger molecules retained and smaller moving faster, thus, separating the molecules by their molecular sizes. The bromophenol blue in the sample makes their migration visible. Due to the relative smaller size, this chemical moves faster than the proteins. The individual molecular weights deter,Paine the protein bands in the separating gel. The relative distances over the size of the proteins as marker are plotted semi-logarithmically against their own molecular weights. It is easy to use, quick for analytical purposes. This method is used with the combination of western blot for the Presence of proteins and for the analysis of post translational modifications.
Iso Electric focusing (IEF) is a technique that utilises the isoelectric point (pI), for separating molecules.it is focused on a zone of isoelectric point that separates the molecules based on their isoelectric points. The molecules are from the ampholytic source that are added into immobilised pH gradient (IPG) gels. They are acrylamide gel matrix co-polymerised with the pH gradient. This immobilised pH is obtained by continuous change in immobiles ratio. A protein with pH below iso electric point, will be positive and migrates toward cathode through the gradient of increasing pH with changes in protein that ultimately reaches to the it’s corresponding pI. As a result the proteins are changed to sharp stationary bands with each protein positioned at its corresponding pI. After this point there is no net charge and the migration stops. The proteins are Sethu so positioned at their pI ranges that become sharp stationary bands.
₹ 4565 / kg
+ Tax (GST - 0 %): Rs 0.00/- Total with Tax: Rs 4,565.00/- Avail 85% Credit on PDC (Post Dated Cheque)
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Service Information
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