Related Experiment Video
Updated: Feb 11, 2026
12:15
Generation of Monoclonal Antibodies Against Natural Products
Published on: April 6, 2019
11.6K
Mouse monoclonal antibodies against rat estramustine binding protein
Journal of Steroid Biochemistry
|April 1, 1987
Summary
Researchers developed monoclonal antibodies against rat prostatic estramustine binding protein (rEMBP). These antibodies showed high specificity, enabling the study of rEMBP subunits in various rat tissues.
Area of Science:
- Immunology
- Biochemistry
- Molecular Biology
Background:
- Rat prostatic estramustine binding protein (rEMBP) is a key molecule in prostate cancer research.
- Understanding the distribution and function of rEMBP is crucial for developing targeted therapies.
Purpose of the Study:
- To generate and characterize monoclonal antibodies against rEMBP.
- To investigate the tissue distribution of rEMBP in rats using the developed antibodies.
Main Methods:
- Hybridoma technology for antibody production.
- Solid-phase ELISA and radioimmunoassay for antibody screening and quantification.
- Characterization of antibody interaction with rEMBP subunits.
Main Results:
- Successfully produced and identified hybridomas secreting specific anti-rEMBP IgG antibodies.
- Antibodies demonstrated high specificity for rEMBP (F and S subunits) but not human estramustine binding protein.
- Radioimmunoassay revealed high concentrations of rEMBP in the prostate and lower levels in other male reproductive tissues, adrenals, pancreas, and submaxillary gland.
Conclusions:
- Monoclonal antibodies against rEMBP were successfully generated and validated.
- These antibodies are valuable tools for studying rEMBP and its subunits.
- Similar macromolecules to rEMBP are present in various hormone-sensitive rat tissues.
Related Concept Videos
01:20Factors Affecting Protein-Drug Binding: Protein-Related Factors
576
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
576
02:18The Equilibrium Binding Constant and Binding Strength
15.2K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.2K
01:10Antibody Structure
65.7K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
65.7K
01:29Drug Distribution: Plasma Protein Binding
9.0K
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
9.0K
01:22Protein-Drug Binding: Determination Methods
674
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
674
01:03Single-Strand DNA Binding Proteins
16.7K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.7K