• genes
  • Rearrangements in certain parts of their DNA called immunoglobulin genes are a normal part of their development. (labtestsonline.org)
  • More recently, expression of engineered immunoglobulin genes in tissue culture can be used to produce IgM with specific alternations and thus to identify the molecular requirements for features of interest. (wikipedia.org)
  • The immunoglobulin light chain genes in tetrapods can be classified into three distinct groups: kappa (κ), lambda (λ), and sigma (σ). (wikipedia.org)
  • Specific rearrangement of lambda light chain of immunoglobulins can lead to loss of some protein coding genes, which does not seem to be functionally relevant (while functionally relevant miR-650 can be overexpressed). (wikipedia.org)
  • While class switch recombination is mostly a deletional process, rearranging a chromosome in "cis", it can also occur (in 10 to 20% of cases, depending upon the Ig class) as an inter-chromosomal translocation mixing immunoglobulin heavy chain genes from both alleles. (wikipedia.org)
  • Structural
  • The V domains of normal immunoglobulin are highly heterogeneous, reflecting their role in protecting against the great variety of infectious microbes, and this heterogeneity impeded detailed structural analysis of IgM. (wikipedia.org)
  • pIgR
  • The extracellular portion of the protein contains 6 domains: 5 evolutionary conserved immunoglobulin-like domains, and 1 non-homologous domain, which is believed to be responsible for proteolytic cleavage of pIg-pIgR complex from the apical side of the IECs. (wikipedia.org)
  • Binding
  • Binding of the immunoglobulins to a microbe can have immediate effects such as blocking invasion and it can mobilize other components of the immune system to destroy or otherwise inactivate the microbes, thereby providing protection against infectious diseases. (wikipedia.org)
  • It, therefore, can mean: Binding immunoglobulin protein (BiP, or heat shock 70 kDa protein 5, with an official symbol HSPA5), a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum. (wikipedia.org)
  • Phosphocholine binding immunoglobulin Fab McPC603. (wikipedia.org)
  • Chain
  • Immunoglobulins are composed of two types of protein chain -- the heavy chain and the light chain. (wikipedia.org)
  • Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes). (wikipedia.org)
  • The variable domain of any heavy chain is composed of a single immunoglobulin domain. (wikipedia.org)
  • During class switching, the constant region of the immunoglobulin heavy chain changes but the variable regions, and therefore antigenic specificity, stay the same. (wikipedia.org)
  • In addition to the highly repetitive structure of the target S regions, the process of class switching needs S regions to be first transcribed and spliced out of the immunoglobulin heavy chain transcripts (where they lie within introns). (wikipedia.org)
  • symptoms
  • Immunoglobulin therapy is also used for a number of other conditions, including in many autoimmune disorders such as dermatomyositis in an attempt to decrease the severity of symptoms. (wikipedia.org)
  • infection
  • In these situations, immunoglobulin infusions confer passive resistance to infection on their recipients by increasing the quantity/quality of IgG they possess. (wikipedia.org)
  • Immunoglobulin therapy is especially useful in some acute infection cases such as pediatric HIV infection and is also considered the standard of treatment for some autoimmune disorders such as Guillain-Barré syndrome. (wikipedia.org)
  • Immunoglobulins are produced by vertebrate animals as part of the normal immune response to microbial, e.g., bacterial or viral, infection. (wikipedia.org)
  • microbes
  • The secretory component of sIgA protects the immunoglobulin from being degraded by proteolytic enzymes, thus sIgA can survive in the harsh gastrointestinal tract environment and provide protection against microbes that multiply in body secretions. (wikipedia.org)
  • human
  • Human Varicella-Zoster Immunoglobulin may be available in the countries listed below. (drugs.com)
  • Metabolism of human immunoglobulin D (IgD)" (PDF). (wikipedia.org)
  • Human immunoglobulin is made from human blood plasma. (wikipedia.org)
  • Human immunoglobulin therapy first occurred in the 1930s and a formulation for injection into a vein was approved for medical use in the United States in 1981. (wikipedia.org)
  • Immunoglobulin therapy is also used in some treatment protocols for secondary immunodeficiencies such as human immunodeficiency virus (HIV), some autoimmune disorders (such as immune thrombocytopenia and Kawasaki disease), some neurological diseases (multifocal motor neuropathy, stiff person syndrome, multiple sclerosis and myasthenia gravis) some acute infections and some complications of organ transplantation. (wikipedia.org)
  • found
  • The name Immunoglobulin Y was suggested in 1969 by G.A. Leslie and L.W. Clem, after they were able to show differences between the immunoglobulins found in chicken eggs, and immunoglobulin G. Other synonymous names are Chicken IgG, Egg Yolk IgG, and 7S-IgG. (wikipedia.org)
  • Of the immunoglobulins arising during the immune response, only IgY is found in chicken eggs. (wikipedia.org)
  • sIgA is the main immunoglobulin found in mucous secretions, including tears, saliva, sweat, colostrum and secretions from the genitourinary tract, gastrointestinal tract, prostate and respiratory epithelium. (wikipedia.org)
  • Therapy
  • The National Advisory Committee on Blood and Blood Products of Canada (NAC) and Canadian Blood Services have also developed their own separate set of guidelines for the appropriate use of immunoglobulin therapy, which strongly support the use of immunoglobulin therapy in primary immunodeficiencies and some complications of HIV, while remaining silent on the issues of sepsis, multiple sclerosis, and chronic fatigue syndrome. (wikipedia.org)