Antibody Stocks List

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

Antibody Stocks Recent News

Date Stock Title
May 18 TECH Rapper Kid Rock Drives Into Live Concert In Texas On Custom Cybertruck Resembling General Lee
May 18 TECH Tesla Bull Gary Black Says 'Likely' Approval Of Elon Musk's $56B Pay Package Is 'Next Major Catalyst' For The Company
May 18 TECH Tesla Cybertruck Seemingly Drives To Saudi Royal Family; Elon Musk Thinks It's 'Cool'
May 18 TECH Crisis At OpenAI? Top Executive Who Just Quit Says Focus Shifted Away From AI Safety To 'Shiny Products:' Here's Sam Altman's Reply
May 18 TECH Boeing's Outgoing CEO Dave Calhoun Reelected To Board Despite Safety Concerns At Company
May 18 TECH Amid 'Mass Exodus' From OpenAI's AI Safety Team, Insider Says 'Trust Collapsing Bit By Bit' In CEO Sam Altman: Report
May 18 TECH TikTok And US Justice Department Push For Speedy Court Action On Divestment Law: Report
May 18 TECH Tesla Makes Its 3 Millionth Car In California Despite Rising Inventory, Layoffs
May 18 TECH After Elon Musk, Argentina's President Milei To Meet Mark Zuckerberg And Other Tech Leaders In Silicon Valley: Report
May 17 TECH Microchip Boosts Aerospace Portfolio With New Launch
May 17 TECH Decoding The FFIE Surge: Inside Faraday Future's Nasdaq Rally
May 17 TECH Baidu Has An 'Increasing Gen-AI Centric Revenue Mix': Analysts Look Into Q1 Results, Outlook
May 17 MRVI Maravai (MRVI) Advances in RNA Research With New Collaboration
May 17 TECH EV Market Set For 20-23% Growth, Led By China-Based Companies Like Nio, XPeng, Li Auto: JPMorgan
May 17 TECH Nvidia's Jensen Huang Tells Stanford Graduates To Embrace 'Pain' For Success: '...Hope Suffering Happens To You'
May 17 TECH Druckenmiller Back In Palantir Game: Duquesne Rebuys Into AI Play After Year-Long Gap, Slashing Nvidia Stake
May 17 TECH Alibaba Boosts E-Commerce Edge with AI, Despite Shrinking Market Share
May 17 TECH Breakthrough For Tesla In China? Shanghai Reportedly Greenlights 'Ordinary' Data Flow Overseas For Intelligent Vehicles
May 17 TECH What's Going On With Applied Materials Stock Today?
May 17 TECH Microsoft Unveils AMD-Powered AI Chips To Rival Nvidia: Report

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.

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