Proteins are essential for all living organisms and contain 20 amino acids necessary for human survival. Antibodies are a special type of protein that act as part of the immune system, inhibiting the reproduction of viruses and bacteria. Antibodies are produced by B lymphocyte structures and can be monoclonal or polyclonal. Antibodies are used in medical research and there are many suppliers worldwide.
The main difference between an antibody and a protein is that while all antibodies are proteins, not all proteins are antibodies. Proteins are a general category of large molecules that serve as both structural and functional units for all living organisms on Earth. They are also the storehouse of 20 essential amino acid molecules in plants and animals that are necessary for human survival, but which the human body cannot produce on its own from other chemical precursors. Antibodies are a special type of Y-shaped protein that acts as part of the immune system, which contain special receptor binding sites for antigenic sites on viruses and bacteria, from which those organisms reproduce. When antibodies are present in significant numbers, they inhibit the reproduction of viruses and bacteria in the body by binding to antigens and trigger other immune responses to ensure health as well.
Another key feature of both an antibody and a protein that is instrumental in their function is how the molecules are folded or shaped, as this affects their ability to bind to other molecules and interact favorably in the cellular environment. While an antibody and a protein may have different chemical structures, their fold architecture may be similar in some cases, which has a direct impact on the role they play at any one time in the body. Current databases as of 2011 have identified only a small number of actual folding patterns that occur in nature, although, in theory, there could be millions of different combinations. Estimates are that there are between 1,233 and 1,393 fold patterns for an antibody and a protein. However, all antibodies take on a unique Y shape, with specific amino acid receptor sites at the top of the Y, where both branches of this region can bind to two separate antigens simultaneously to disable them.
A key difference between an antibody and a protein is also the region from which they are produced. While protein synthesis is a natural result of combining amino acid sequences in various cell types from deoxyribonucleic acid (DNA), antibodies have more restricted methods of production. Antibodies are often referred to as immunoglobulins due to their binding role in the immune system, and these molecules are usually only produced by B lymphocyte or B-cell structures, also known as white blood cells or plasma cells, located in the bone marrow.
The general classification of an antibody and a protein also varies. Although there are at least 100 different types of protein molecules and they perform numerous molecular functions, from facilitating motor activity to catalyzing DNA, antibodies are either monoclonal or polyclonal. Monoclonal antibodies are able to bind to only one specific antigen and are naturally produced in the body in response to foreign invaders. Polyclonal antibodies, on the other hand, are collected from the blood of immunized animals and can be engineered to bind to a wide range of antigens.
Organisms naturally stimulate the production of antibodies to protect themselves from infection, but medical science is also heavily involved in creating antibodies for research, and there are now large antibody catalog listings where laboratories can order the antibodies they need to particular research interests. The number of polyclonal antibody suppliers worldwide numbered at least 180 companies as of 2011, many of which have lists of over 20,000 different antibodies available for sale and shipment, including some monoclonal antibodies as well.
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