Antibodies Stocks List

Related ETFs - A few ETFs which own one or more of the above listed Antibodies stocks.

Antibodies Stocks Recent News

Date Stock Title
Mar 18 REGN US appeals court revives Regeneron's antitrust lawsuit against Novartis
Mar 18 ADMA Cybin (CYBN) Begins Phase II Study on Anxiety Drug, Stock Up
Mar 18 ADMA Immuneering (IMRX) Plummets 71% in One Week: Here's Why
Mar 18 ADMA Wall Street Analysts Think Adma Biologics (ADMA) Could Surge 33.56%: Read This Before Placing a Bet
Mar 18 ADMA Wall Street Analysts See Adma Biologics (ADMA) as a Buy: Should You Invest?
Mar 18 ADMA J&J (JNJ) Gets FDA Panel Vote for Carvykti's Expanded Use
Mar 17 REGN 11 Oversold Biotech Stocks To Buy Right Now
Mar 17 REGN Regeneron Pharmaceuticals Insiders Sold US$26m Of Shares Suggesting Hesitancy
Mar 15 ADMA Adma Biologics (ADMA) Stock Moves -0.5%: What You Should Know
Mar 15 MOR MorphoSys AG (NASDAQ:MOR) Q4 2023 Earnings Call Transcript
Mar 15 ADMA Are Medical Stocks Lagging Adicet Bio (ACET) This Year?
Mar 15 ADMA Allogene's (ALLO) Q4 Loss Narrower Than Expected, Sales Miss
Mar 14 MOR MorphoSys AG (MOR) Q4 2023 Earnings Call Transcript
Mar 14 REGN Cardiff Oncology (CRDF) Moves 20.5% Higher: Will This Strength Last?
Mar 13 MOR MorphoSys GAAP EPS of €1.22, revenue of €59M
Mar 13 MOR MorphoSys AG Reports Fourth Quarter and Full Year 2023 Financial Results and Provides Corporate Update
Mar 13 REGN Regeneron Pharmaceuticals, Inc. (REGN) Leerink Partners Global Biopharma Conference (Transcript)
Mar 13 ADMA Regulus (RGLS) Up 71% on Topline Data from Kidney Disease Study
Mar 13 ADMA Pfizer's (PFE) Adcetris Meets Survival Goal in Lymphoma Study
Mar 13 MOR Earnings Scheduled For March 13, 2024
Antibodies

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the Fab's variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (similarly, analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essential for its invasion and survival). Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions. The production of antibodies is the main function of the humoral immune system.Antibodies are secreted by B cells of the adaptive immune system, mostly by differentiated B cells called plasma cells. Antibodies can occur in two physical forms, a soluble form that is secreted from the cell to be free in the blood plasma, and a membrane-bound form that is attached to the surface of a B cell and is referred to as the B-cell receptor (BCR). The BCR is found only on the surface of B cells and facilitates the activation of these cells and their subsequent differentiation into either antibody factories called plasma cells or memory B cells that will survive in the body and remember that same antigen so the B cells can respond faster upon future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions to continue to survey for invading microorganisms.
Antibodies are glycoproteins belonging to the immunoglobulin superfamily. They constitute most of the gamma globulin fraction of the blood proteins. They are typically made of basic structural units—each with two large heavy chains and two small light chains. There are several different types of antibody heavy chains that define the five different types of crystallisable fragments (Fc) that may be attached to the antigen-binding fragments. The five different types of Fc regions allow antibodies to be grouped into five isotypes. Each Fc region of a particular antibody isotype is able to bind to its specific Fc Receptor (except for IgD, which is essentially the BCR), thus allowing the antigen-antibody complex to mediate different roles depending on which FcR it binds. The ability of an antibody to bind to its corresponding FcR is further modulated by the structure of the glycan(s) present at conserved sites within its Fc region. The ability of antibodies to bind to FcRs helps to direct the appropriate immune response for each different type of foreign object they encounter. For example, IgE is responsible for an allergic response consisting of mast cell degranulation and histamine release. IgE's Fab paratope binds to allergic antigen, for example house dust mite particles, while its Fc region binds to Fc receptor ε. The allergen-IgE-FcRε interaction mediates allergic signal transduction to induce conditions such as asthma.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen-binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different antigen. This enormous diversity of antibody paratopes on the antigen-binding fragments allows the immune system to recognize an equally wide variety of antigens. The large and diverse population of antibody paratope is generated by random recombination events of a set of gene segments that encode different antigen-binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. This recombinational process that produces clonal antibody paratope diversity is called V(D)J or VJ recombination. Basically, the antibody paratope is polygenic, made up of three genes, V, D, and J. Each paratope locus is also polymorphic, such that during antibody production, one allele of V, one of D, and one of J is chosen. These gene segments are then joined together using random genetic recombination to produce the paratope. The regions where the genes are randomly recombined together is the hyper variable region used to recognise different antigens on a clonal basis.
Antibody genes also re-organize in a process called class switching that changes the one type of heavy chain Fc fragment to another, creating a different isotype of the antibody that retains the antigen-specific variable region. This allows a single antibody to be used by different types of Fc receptors, expressed on different parts of the immune system.

Browse All Tags