An immunoglobulin which accounts for less than 1% of plasma immunoglobulin. It is found on the membrane of many circulating B LYMPHOCYTES.
The class of heavy chains found in IMMUNOGLOBULIN D. They have a molecular weight of approximately 64 kDa and they contain about 500 amino acid residues arranged in four domains and an oligosaccharide component covalently bound to the Fc fragment constant region.
Autosomal recessive disorder caused by mutations in the mevalonate kinase gene. Because of the mutations cholesterol biosynthesis is disrupted and MEVALONIC ACID accumulates. It is characterized by a range of symptoms, including dysmorphic FACIES, psychomotor retardation, CATARACT, hepatosplenomegaly, CEREBELLAR ATAXIA, elevated IMMUNOGLOBULIN D, and recurrent febrile crises with FEVER; LYMPHADENOPATHY; ARTHRALGIA; EDEMA; and rash.
The domains of the immunoglobulin molecules that are invariable in their amino acid sequence within any class or subclass of immunoglobulin. They confer biological as well as structural functions to immunoglobulins. One each on both the light chains and the heavy chains comprises the C-terminus half of the IMMUNOGLOBULIN FAB FRAGMENT and two or three of them make up the rest of the heavy chains (all of the IMMUNOGLOBULIN FC FRAGMENT)
A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally being called a macroglobulin.
The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.
Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses.
Lymphoid cells concerned with humoral immunity. They are short-lived cells resembling bursa-derived lymphocytes of birds in their production of immunoglobulin upon appropriate stimulation.
The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.
Represents 15-20% of the human serum immunoglobulins, mostly as the 4-chain polymer in humans or dimer in other mammals. Secretory IgA (IMMUNOGLOBULIN A, SECRETORY) is the main immunoglobulin in secretions.
Immunoglobulin preparations used in intravenous infusion, containing primarily IMMUNOGLOBULIN G. They are used to treat a variety of diseases associated with decreased or abnormal immunoglobulin levels including pediatric AIDS; primary HYPERGAMMAGLOBULINEMIA; SCID; CYTOMEGALOVIRUS infections in transplant recipients, LYMPHOCYTIC LEUKEMIA, CHRONIC; Kawasaki syndrome, infection in neonates, and IDIOPATHIC THROMBOCYTOPENIC PURPURA.
Genes encoding the different subunits of the IMMUNOGLOBULINS, for example the IMMUNOGLOBULIN LIGHT CHAIN GENES and the IMMUNOGLOBULIN HEAVY CHAIN GENES. The heavy and light immunoglobulin genes are present as gene segments in the germline cells. The completed genes are created when the segments are shuffled and assembled (B-LYMPHOCYTE GENE REARRANGEMENT) during B-LYMPHOCYTE maturation. The gene segments of the human light and heavy chain germline genes are symbolized V (variable), J (joining) and C (constant). The heavy chain germline genes have an additional segment D (diversity).
Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
One of the types of light chains of the immunoglobulins with a molecular weight of approximately 22 kDa.

Biased JH usage in plasma cell immunoglobulin gene sequences from colonic mucosa in ulcerative colitis but not in Crohn's disease. (1/605)

BACKGROUND: Ulcerative colitis is an inflammatory disease of the colonic and rectal mucosa. Autoantibodies have been observed in ulcerative colitis which may have a role in the pathogenesis of the disease. Evidence also suggests that there is an hereditary predisposition towards the disease, although no individual genes have been identified. AIMS: This is a pilot study of immunoglobulin heavy chain genes (IgH) in ulcerative colitis to determine whether they have any particular genetic characteristics which may lead to a better understanding of the disease aetiology. SUBJECTS: Colonic or rectal tissue was obtained from five children with ulcerative colitis. Tissue was also obtained from five children with Crohn's disease and five children who did not have inflammatory bowel disease as controls. METHODS: B cells and IgD+ B cells were identified by immunohistochemistry on frozen sections. Areas of lamina propria containing plasma cells, and areas of IgD+ B cells were microdissected. The immunoglobulin genes were PCR amplified, cloned, and sequenced. Sequences were analysed for content of somatic mutations and composition of heavy chain. RESULTS: An increase in the use of JH6 and DXP'1, and a decrease in the use of JH4, gene segments in immunoglobulin genes from lamina propria plasma cells, and from virgin IgD+ B cells, was found in patients with ulcerative colitis. These biases were not present in the control groups. CONCLUSIONS: There is a fundamental difference in the immunoglobulin genes from patients with ulcerative colitis. Whether this is caused by a difference in content of immunoglobulin gene segments in the germline or a difference in the recombination mechanism is not known.  (+info)

Antigen-stimulated dissociation of BCR mIg from Ig-alpha/Ig-beta: implications for receptor desensitization. (2/605)

B cell antigen receptor (BCR) ligation leads to receptor desensitization wherein BCR remain competent to bind antigen and yet fail to transduce signals. Desensitized BCR exhibit a defect at the most proximal level of signal transduction, consistent with failed transmission of signals through the receptor complex. We report that antigen stimulation leads to dissociation or destabilization of the BCR reflected by inability to coimmunoprecipitate Ig-alpha/Ig-beta with mIg. This destabilization is temporally correlated with desensitization and occurs in BCR containing mIgM and mIgD. Induction of BCR destabilization requires tyrosine kinase activation but is not induced by phosphatase inhibitors. BCR destabilization occurs at the cell surface and "dissociated" Ig-alpha/Ig-beta complexes remain responsive to anti-Ig-beta stimulation, suggesting that mIg-transducer uncoupling may mediate receptor desensitization.  (+info)

IL-5 induces IgG1 isotype switch recombination in mouse CD38-activated sIgD-positive B lymphocytes. (3/605)

Mouse B cells express CD38, whose ligation by anti-CD38 Ab induces their proliferation and protection from apoptosis. We previously showed that stimulation of mouse splenic B cells with IL-5 together with CS/2, an anti-mouse CD38 mAb, induces production of IgG1 and IgM. Here we examined the role of IL-5 and CS/2 in the expression of germline gamma1 transcripts and the generation of reciprocal products forming DNA circles as byproducts of mu-gamma1 switch recombination. By itself, CS/2 induced significant expression of germline gamma1 transcripts in splenic naive B cells, whereas IL-5 neither induced nor enhanced germline gamma1 expression. Increased cellular content of reciprocal product, which is characteristic of mu-gamma1 recombination, was not observed after culturing B cells with CS/2, but increased reciprocal product, along with high levels of lgG1 secretion, was found when B cells were cultured with CS/2 plus IL-5. Although IL-4 did not, by itself, induce mu-gamma1 recombination in B cells stimulated with CS/2, in conjunction with CS/2 plus IL-5, IL-4 dramatically enhanced sterile gamma1 transcription and IgG1 production. These results demonstrate that CD38 ligation induces only germline gamma1 transcription and that IL-5 promotes both mu-gamma1 switch recombination and lgG1 secretion in an IL-4-independent manner.  (+info)

Induction of Ig somatic hypermutation and class switching in a human monoclonal IgM+ IgD+ B cell line in vitro: definition of the requirements and modalities of hypermutation. (4/605)

Partly because of the lack of a suitable in vitro model, the trigger(s) and the mechanism(s) of somatic hypermutation in Ig genes are largely unknown. We have analyzed the hypermutation potential of human CL-01 lymphocytes, our monoclonal model of germinal center B cell differentiation. These cells are surface IgM+ IgD+ and, in the absence of T cells, switch to IgG, IgA, and IgE in response to CD40:CD40 ligand engagement and exposure to appropriate cytokines. We show here that CL-01 cells can be induced to effectively mutate the expressed VHDJH-C mu, VHDJH-C delta, VHDJH-C gamma, VHDJH-C alpha, VHDJH-C epsilon, and V lambda J lambda-C lambda transcripts before and after Ig class switching in a stepwise fashion. In these cells, induction of somatic mutations required cross-linking of the surface receptor for Ag and T cell contact through CD40:CD40 ligand and CD80: CD28 coengagement. The induced mutations showed intrinsic features of Ig V(D)J hypermutation in that they comprised 110 base substitutions (97 in the heavy chain and 13 in the lambda-chain) and only 2 deletions and targeted V(D)J, virtually sparing CH and C lambda. These mutations were more abundant in secondary VHDJH-C gamma than primary VHDJH-C mu transcripts and in V(D)J-C than V lambda J lambda-C lambda transcripts. These mutations were also associated with coding DNA strand polarity and showed an overall rate of 2.42 x 10(-4) base changes/cell division in VHDJH-CH transcripts. Transitions were favored over transversions, and G nucleotides were preferentially targeted, mainly in the context of AG dinucleotides. Thus, in CL-01 cells, Ig somatic hypermutation is readily inducible by stimuli different from those required for class switching and displays discrete base substitution modalities.  (+info)

The evolutionarily conserved sequence upstream of the human Ig heavy chain S gamma 3 region is an inducible promoter: synergistic activation by CD40 ligand and IL-4 via cooperative NF-kappa B and STAT-6 binding sites. (5/605)

Germline C gamma gene transcription is a crucial event in the process that leads to switch DNA recombination to IgG, but its regulation in the human is poorly understood. We took advantage of our monoclonal model of germinal center B cell differentiation, IgM+ IgD+ CL-01 cells, to define the role of the I gamma 3 evolutionarily conserved sequence (ECS) in the germline transcriptional activation of the human C gamma 3 gene. The I gamma 3 ECS lies upstream of the major I gamma 3 transcription initiation site and displays more than 90% identity with the corresponding human I gamma 1, I gamma 2, and I gamma 4 regions. Reporter luciferase gene vectors containing the human gamma 3 ECS were used to transfect CL-01 cells, which have been shown to undergo Smu-->S gamma 3 DNA recombination, upon engagement of CD40 by CD40 ligand (CD40L) and exposure to IL-4. In these transfected CL-01 cells, CD40:CD40L engagement and exposure to IL-4 synergistically induced gamma 3 ECS-dependent luciferase reporter gene activation. Targeted mutational analysis demonstrated that a tandem NF-kappa B/Rel binding motif is critical for the gamma 3 ECS responsiveness to both CD40L and IL-4, while a STAT-6-binding site is additionally required for IL-4 inducibility. Electrophoretic mobility shift assays showed that p50/p65/c-Rel and STAT-6 are effectively induced by CD40L and IL-4, respectively, and bind to specific DNA motifs within the ECS. These partially overlapping CD40L and IL-4 responsive elements are functionally cooperative as the disruption of one of them prevents synergistic promoter activation. Thus, the gamma 3 ECS is an inducible promoter containing cis elements that critically mediate CD40L and IL-4-triggered transcriptional activation of the human C gamma 3 gene.  (+info)

Differential regulation of transcription termination occurring at two different sites on the micro-delta gene complex. (6/605)

The progression of polymerases across the micro-delta Ig heavy chain gene complex is characterized by two termination events occurring at different sites on the transcription unit and at different times during B cell differentiation. We have utilized two mouse strains to analyze the regulatory determinants for these events in primary B cells. In the transgenic pmicro.microdeltaRatt strain a 1160 bp intervening DNA segment (the att site) has been inverted. This mutation results in the abrogation of transcription termination that occurs in early B cells. Using a novel method that takes advantage of an internal ribosome entry site we have further restricted the size of the segment that is needed for inducing transcription termination in transfectants. This 200 bp termination-inducing sequence operates in tumor equivalents of early but not mature B cells and the activity is correlated with differential binding of nuclear proteins. To explore the regulatory basis for the change in site of transcription termination upon B cell activation we have examined the microS-/- deletion mutant strain in which the microS poly(A) site has been eliminated. The results suggest that polyadenylation at the microS site plays a dominant but not exclusive role in regulating transcription termination in activated B cells.  (+info)

Serum hyaluronan in patients with multiple myeloma: correlation with survival and Ig concentration. (7/605)

Serum from 386 myeloma patients were analyzed for serum hyaluronan (HYA) at diagnosis. Median age was 68 years (range, 32 to 87 years). The distribution of Ig classes was typical (58% IgG, 21% IgA, 1% IgD, and 20% light chain disease). The patients comprised 58% in stage III, 33% in stage II, and 9% in stage I. The majority (82%) had HYA values within an intermediate range (10 to 120 micrograms/L), 13% had high values (>120 micrograms/L), and 5% had abnormally low values (0 to 9 micrograms/L). For the first time, a patient group with abnormally low HYA serum values is reported. An inverse correlation between survival and HYA serum level was found (P =.015). When tested separately, patients with abnormally low or high HYA values had significantly shorter median survival (21.1 and 19.7 months, respectively) than those with an intermediate HYA concentration (32. 6 months; P =.005). Patients with abnormally low or high HYA levels had more advanced disease as judged by staging and biochemical markers. Interestingly, there was an inverse correlation between the HYA value and the M-component concentration in serum. Fifty percent of patients with abnormally low HYA values had IgA myelomas. In conclusion, the serum concentration of HYA may be of prognostic value in selected cases of multiple myeloma. Further studies will be performed to elucidate possible explanations for our findings, especially those related to the HYA cell surface binding proteins.  (+info)

Composite low grade B-cell lymphomas with two immunophenotypically distinct cell populations are true biclonal lymphomas. A molecular analysis using laser capture microdissection. (8/605)

Low grade B-cell lymphomas comprise several well defined, clinically and immunophenotypically distinct disease entities. Composite lymphomas showing phenotypic characteristics of more than one of these tumor subtypes in the same site are rare, and both common and separate clonal origins of the two tumor parts have been reported for cases studied by molecular methods. We describe the detailed immunohistochemical and molecular findings in three cases with features of composite low grade B-cell non-Hodgkin's lymphoma (B-NHL). All three neoplasms contained morphologically distinct but interwoven compartments of different cell types, which exhibited discordant expression of several markers, including CD5, CD10, CD43, and cyclin D1. According to their morphology and phenotypes, they were classified as mantle cell lymphoma and follicular lymphoma (Case 1), follicular lymphoma and small lymphocytic lymphoma (Case 2), and mantle cell lymphoma and chronic lymphocytic leukemia/small lymphocytic lymphoma (Case 3). PCR analysis of DNA obtained from whole tissue sections failed to reveal evidence for biclonality in any of the cases. We therefore isolated cell populations with different antigen expression patterns by laser capture microdissection and analyzed them by polymerase chain reaction amplification and sequencing of clonal immunoglobulin heavy chain gene rearrangements and oncogene rearrangements. Sequence analysis revealed unrelated clonal rearrangements in each of the two tumor parts in all three cases, suggesting distinct clonal origins. In addition, Case 1 showed a bcl-2 rearrangement present only in the follicular lymphoma part. Our findings suggest that low grade B-NHL with two distinct morphological and immunophenotypic patterns in the same anatomical site are frequently biclonal. This is in keeping with current classification schemes, which recognize subtypes of low grade B-NHL as separate disease entities. Furthermore, our analysis demonstrates the power of laser capture microdissection in revealing molecular microheterogeneity in complex neoplasms.  (+info)

Immunoglobulin D (IgD) is a type of antibody that is present in the blood and other bodily fluids. It is one of the five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) found in humans and plays a role in the immune response.

IgD is produced by B cells, a type of white blood cell that is responsible for producing antibodies. It is primarily found on the surface of mature B cells, where it functions as a receptor for antigens (foreign substances that trigger an immune response). When an antigen binds to IgD on the surface of a B cell, it activates the B cell and stimulates it to produce and secrete antibodies specific to that antigen.

IgD is found in relatively low concentrations in the blood compared to other immunoglobulins, and its precise functions are not fully understood. However, it is thought to play a role in the regulation of B cell activation and the immune response. Additionally, some research suggests that IgD may have a direct role in protecting against certain types of infections.

It's worth noting that genetic deficiencies in IgD are not typically associated with any significant immunological abnormalities or increased susceptibility to infection.

Immunoglobulin delta-chains (IgD) are a type of heavy chain found in immunoglobulins, which are also known as antibodies. Antibodies are proteins that play a crucial role in the immune system's response to foreign substances, such as bacteria and viruses.

The heavy chains of an antibody consist of four polypeptide regions: the variable region, which varies between different antibodies and is responsible for recognizing and binding to specific antigens; and three constant regions, known as Cμ, Cγ, Cα, or Cδ, which determine the class of the antibody and its effector functions.

IgD heavy chains contain a single Cδ region and are found only in a small subset of antibodies, primarily located on the surface of mature B cells. IgD is co-expressed with IgM on the surface of naive B cells and plays a role in activating the immune response by binding to antigens and initiating signal transduction pathways that lead to B cell activation and differentiation into antibody-secreting plasma cells.

While the function of IgD is not fully understood, it is thought to play a role in regulating the immune response, including modulating allergic reactions and protecting against autoimmunity. Additionally, IgD has been found to have a role in the development and survival of B cells, as well as in the regulation of calcium signaling in B cells.

Mevalonate kinase deficiency (MKD) is a rare autosomal recessive genetic disorder that affects the metabolism of cholesterol and other essential isoprenoids. It is caused by mutations in the MVK gene, which provides instructions for making the enzyme mevalonate kinase.

This enzyme plays a critical role in the production of isoprenoids, including cholesterol, coenzyme Q10, and dolichols, which are essential for various cellular functions such as membrane stability, protein prenylation, and glycosylation. In MKD, the deficiency of mevalonate kinase leads to an accumulation of its substrate, mevalonic acid, and a decrease in isoprenoid production.

MKD has two clinical manifestations: hyperimmunoglobulin D syndrome (HIDS) and mevalonic aciduria (MA). HIDS is the milder form of the disorder, characterized by recurrent fever episodes, gastrointestinal symptoms, rash, lymphadenopathy, and joint pain. MA is the severe form of MKD, which presents with developmental delay, neurological impairment, cataracts, failure to thrive, and recurrent infections. Both forms of MKD are associated with increased levels of mevalonic acid in body fluids, including urine and blood.

The diagnosis of MKD is based on clinical features, biochemical markers, and genetic testing. Treatment options for MKD include anti-inflammatory medications such as nonsteroidal anti-inflammatory drugs (NSAIDs), corticosteroids, and biologic agents such as anakinra and canakinumab, which target the interleukin-1 (IL-1) pathway. In some cases, dietary modifications and supplementation with coenzyme Q10 may also be beneficial.

Immunoglobulin constant regions are the invariant portions of antibody molecules (immunoglobulins) that are identical in all antibodies of the same isotype. These regions are responsible for effector functions such as complement activation, binding to Fc receptors, and initiating immune responses. They are composed of amino acid sequences that remain unchanged during antigen-driven somatic hypermutation, allowing them to interact with various components of the immune system. The constant regions are found in the heavy chains (CH) and light chains (CL) of an immunoglobulin molecule. In contrast, the variable regions are responsible for recognizing and binding to specific antigens.

Immunoglobulin M (IgM) is a type of antibody that is primarily found in the blood and lymph fluid. It is the first antibody to be produced in response to an initial exposure to an antigen, making it an important part of the body's primary immune response. IgM antibodies are large molecules that are composed of five basic units, giving them a pentameric structure. They are primarily found on the surface of B cells as membrane-bound immunoglobulins (mlgM), where they function as receptors for antigens. Once an mlgM receptor binds to an antigen, it triggers the activation and differentiation of the B cell into a plasma cell that produces and secretes large amounts of soluble IgM antibodies.

IgM antibodies are particularly effective at agglutination (clumping) and complement activation, which makes them important in the early stages of an immune response to help clear pathogens from the bloodstream. However, they are not as stable or long-lived as other types of antibodies, such as IgG, and their levels tend to decline after the initial immune response has occurred.

In summary, Immunoglobulin M (IgM) is a type of antibody that plays a crucial role in the primary immune response to antigens by agglutination and complement activation. It is primarily found in the blood and lymph fluid, and it is produced by B cells after they are activated by an antigen.

Immunoglobulin heavy chains are proteins that make up the framework of antibodies, which are Y-shaped immune proteins. These heavy chains, along with light chains, form the antigen-binding sites of an antibody, which recognize and bind to specific foreign substances (antigens) in order to neutralize or remove them from the body.

The heavy chain is composed of a variable region, which contains the antigen-binding site, and constant regions that determine the class and function of the antibody. There are five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) that differ in their heavy chain constant regions and therefore have different functions in the immune response.

Immunoglobulin heavy chains are synthesized by B cells, a type of white blood cell involved in the adaptive immune response. The genetic rearrangement of immunoglobulin heavy chain genes during B cell development results in the production of a vast array of different antibodies with unique antigen-binding sites, allowing for the recognition and elimination of a wide variety of pathogens.

Immunoglobulins (Igs), also known as antibodies, are glycoprotein molecules produced by the immune system's B cells in response to the presence of foreign substances, such as bacteria, viruses, and toxins. These Y-shaped proteins play a crucial role in identifying and neutralizing pathogens and other antigens, thereby protecting the body against infection and disease.

Immunoglobulins are composed of four polypeptide chains: two identical heavy chains and two identical light chains, held together by disulfide bonds. The variable regions of these chains form the antigen-binding sites, which recognize and bind to specific epitopes on antigens. Based on their heavy chain type, immunoglobulins are classified into five main isotypes or classes: IgA, IgD, IgE, IgG, and IgM. Each class has distinct functions in the immune response, such as providing protection in different body fluids and tissues, mediating hypersensitivity reactions, and aiding in the development of immunological memory.

In medical settings, immunoglobulins can be administered therapeutically to provide passive immunity against certain diseases or to treat immune deficiencies, autoimmune disorders, and other conditions that may benefit from immunomodulation.

B-lymphocytes, also known as B-cells, are a type of white blood cell that plays a key role in the immune system's response to infection. They are responsible for producing antibodies, which are proteins that help to neutralize or destroy pathogens such as bacteria and viruses.

When a B-lymphocyte encounters a pathogen, it becomes activated and begins to divide and differentiate into plasma cells, which produce and secrete large amounts of antibodies specific to the antigens on the surface of the pathogen. These antibodies bind to the pathogen, marking it for destruction by other immune cells such as neutrophils and macrophages.

B-lymphocytes also have a role in presenting antigens to T-lymphocytes, another type of white blood cell involved in the immune response. This helps to stimulate the activation and proliferation of T-lymphocytes, which can then go on to destroy infected cells or help to coordinate the overall immune response.

Overall, B-lymphocytes are an essential part of the adaptive immune system, providing long-lasting immunity to previously encountered pathogens and helping to protect against future infections.

Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.

IgG has several important functions:

1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.

IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.

Immunoglobulin A (IgA) is a type of antibody that plays a crucial role in the immune function of the human body. It is primarily found in external secretions, such as saliva, tears, breast milk, and sweat, as well as in mucous membranes lining the respiratory and gastrointestinal tracts. IgA exists in two forms: a monomeric form found in serum and a polymeric form found in secretions.

The primary function of IgA is to provide immune protection at mucosal surfaces, which are exposed to various environmental antigens, such as bacteria, viruses, parasites, and allergens. By doing so, it helps prevent the entry and colonization of pathogens into the body, reducing the risk of infections and inflammation.

IgA functions by binding to antigens present on the surface of pathogens or allergens, forming immune complexes that can neutralize their activity. These complexes are then transported across the epithelial cells lining mucosal surfaces and released into the lumen, where they prevent the adherence and invasion of pathogens.

In summary, Immunoglobulin A (IgA) is a vital antibody that provides immune defense at mucosal surfaces by neutralizing and preventing the entry of harmful antigens into the body.

Intravenous Immunoglobulins (IVIG) are a preparation of antibodies, specifically immunoglobulins, that are derived from the plasma of healthy donors. They are administered intravenously to provide passive immunity and help boost the immune system's response in individuals with weakened or compromised immune systems. IVIG can be used for various medical conditions such as primary immunodeficiency disorders, secondary immunodeficiencies, autoimmune diseases, and some infectious diseases. The administration of IVIG can help prevent infections, reduce the severity and frequency of infections, and manage the symptoms of certain autoimmune disorders. It is important to note that while IVIG provides temporary immunity, it does not replace a person's own immune system.

Immunoglobulins (Igs), also known as antibodies, are proteins produced by the immune system to recognize and neutralize foreign substances such as pathogens or toxins. They are composed of four polypeptide chains: two heavy chains and two light chains, which are held together by disulfide bonds. The variable regions of the heavy and light chains contain loops that form the antigen-binding site, allowing each Ig molecule to recognize a specific epitope (antigenic determinant) on an antigen.

Genes encoding immunoglobulins are located on chromosome 14 (light chain genes) and chromosomes 22 and 2 (heavy chain genes). The diversity of the immune system is generated through a process called V(D)J recombination, where variable (V), diversity (D), and joining (J) gene segments are randomly selected and assembled to form the variable regions of the heavy and light chains. This results in an enormous number of possible combinations, allowing the immune system to recognize and respond to a vast array of potential threats.

There are five classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, each with distinct functions and structures. For example, IgG is the most abundant class in serum and provides long-term protection against pathogens, while IgA is found on mucosal surfaces and helps prevent the entry of pathogens into the body.

Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.

Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.

Immunoglobulin kappa-chains are one of the two types of light chains (the other being lambda-chains) that make up an immunoglobulin molecule, also known as an antibody. These light chains combine with heavy chains to form the antigen-binding site of an antibody, which is responsible for recognizing and binding to specific antigens or foreign substances in the body.

Kappa-chains contain a variable region that differs between different antibodies and contributes to the diversity of the immune system's response to various antigens. They also have a constant region, which is consistent across all kappa-chains. Approximately 60% of all human antibodies contain kappa-chains, while the remaining 40% contain lambda-chains. The relative proportions of kappa and lambda chains can be used in diagnostic tests to identify clonal expansions of B cells, which may indicate a malignancy such as multiple myeloma or lymphoma.

... (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most ... This repertoire of immunoglobulins is crucial for the newborns who are very sensitive to infections, especially within the ... Stadlmann J, Pabst M, Kolarich D, Kunert R, Altmann F (2008). "Analysis of immunoglobulin glycosylation by LC-ESI-MS of ... de Haan, Noortje; Falck, David; Wuhrer, Manfred (2019-07-08). "Monitoring of Immunoglobulin N- and O-glycosylation in Health ...
Immunodeficiency with hyper-immunoglobulin M Immunoglobulin M deficiency Immune system "Immunoglobulin M". The American ... Immunoglobulin M (IgM) is one of several isotypes of antibody (also known as immunoglobulin) that are produced by vertebrates. ... Immunoglobulin+M at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Immunoglobulin M Deficiency Reference ... Mestecky, J.; Zikin, J.; Butler, W. T. (1971). "Immunoglobulin M an secretory immunoglobulin A: presence of common polypeptide ...
... human normal immunoglobulin), and Flebogamma DIF (human normal immunoglobulin). In the EU human normal immunoglobulin (SCIg) ( ... Some believe that immunoglobulin therapy may work via a multi-step model where the injected immunoglobulin first forms a type ... Immunoglobulin therapy is the use of a mixture of antibodies (normal human immunoglobulin or NHIG) to treat several health ... Human normal immunoglobulin (human immunoglobulin G) (Cutaquig) was approved for medical use in Australia in May 2021. Brands ...
... antibodies may bind to either the variable or constant region of the immunoglobulin. Anti-immunoglobulin ... anti-immunoglobulin antibodies are created by B-cells as antibodies to bind to other immunoglobulins. Immunoglobulins have two ... Kappa light chains are the second of the two classes of light chains present on mammalian immunoglobulins. One immunoglobulin ... The most practical use for anti-immunoglobulin antibodies is in diagnostic tests. Assays use anti-immunoglobulin antibodies to ...
... (Ig A, also referred to as sIgA in its secretory form) is an antibody that plays a role in the immune function ... Immunoglobulin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Herich, R. (2017). "Is the role of ... The IgA dimeric form is the most prevalent and is also called secretory IgA (sIgA). sIgA is the main immunoglobulin found in ... This represents up to 15% of total immunoglobulins produced throughout the body. IgA has two subclasses (IgA1 and IgA2) and can ...
... (IgD) is an antibody isotype that makes up about 1% of proteins in the plasma membranes of immature B- ... Immunoglobulin+D at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short description, ... Rogentine GN, Rowe DS, Bradley J, Waldmann TA, Fahey JL (1966). "Metabolism of human immunoglobulin D (IgD)". J. Clin. Invest. ... Nitschke L, Kosco MH, Köhler G, Lamers MC (1993). "Immunoglobulin D-deficient mice can mount normal immune responses to thymus- ...
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer ... SCOP listing of immunoglobulin domains of known structure This article incorporates text from the public domain Pfam and ... Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions. Human genes encoding proteins ... Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies ...
... is expensive and hard to come by in the developing world. In the United States it is estimated to be more ... Rabies immunoglobulin (RIG) is a medication made up of antibodies against the rabies virus. It is used to prevent rabies ... The use of rabies immunoglobulin in the form of blood serum dates from 1891. Use became common within medicine in the 1950s. It ... Rabies immunoglobulin (RIG) is indicated for the passive, transient post-exposure prophylaxis of rabies infection, when given ...
... (IgE) is a type of antibody (or immunoglobulin (Ig) "isotype") that has been found only in mammals. IgE is ... Presence of a unique immunoglobulin as a carrier of reaginic activity". Journal of Immunology. 97 (1): 75-85. doi:10.4049/ ... November 2013). "A beneficial role for immunoglobulin E in host defense against honeybee venom". Immunity. 39 (5): 963-75. doi: ... Winter WE, Hardt NS, Fuhrman S (September 2000). "Immunoglobulin E: importance in parasitic infections and hypersensitivity ...
The immunoglobulin superfamily (IgSF) is a large protein superfamily of cell surface and soluble proteins that are involved in ... Proteins of the IgSF possess a structural domain known as an immunoglobulin (Ig) domain. Ig domains are named after the ... Otherwise, the sperm-specific protein IZUMO1, a member of the immunoglobulin superfamily, has also been identified as the only ... Harpaz Y, Chothia C (May 1994). "Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface ...
In chickens, immunoglobulin Y is the functional equivalent to Immunoglobulin G (IgG). Like IgG, it is composed of two light and ... Immunoglobulin Y (abbreviated as IgY) is a type of immunoglobulin which is the major antibody in bird, reptile, and lungfish ... Thus, in preparations from chicken eggs, there is no contamination with Immunoglobulin A (IgA) or Immunoglobulin M (IgM). The ... after they were able to show differences between the immunoglobulins found in chicken eggs, and immunoglobulin G. Other ...
... (BiPS) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 ( ... GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 ... Corrigall VM, Vittecoq O, Panayi GS (October 2009). "Binding immunoglobulin protein-treated peripheral blood monocyte-derived ...
Immunoglobulin+class+switching at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short ... Naïve mature B cells produce both IgM and IgD, which are the first two heavy chain segments in the immunoglobulin locus. After ... Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a ... Laffleur B, Bardet SM, Garot A, Brousse M, Baylet A, Cogné M (2014). "Immunoglobulin genes undergo legitimate repair in human B ...
The immunoglobulin is categorized as immunoglobulin G (IgG). Since the tetanus toxin permanently binds to human tissues, only ... Anti-tetanus immunoglobulin, also known as tetanus immune globulin (TIG) and tetanus antitoxin, is a medication made up of ... unbounded molecules can be neutralized by the immunoglobulin. Use of the horse version became common in the 1910s, while the ...
The immunoglobulin light chain is the small polypeptide subunit of an antibody (immunoglobulin). A typical antibody is composed ... The immunoglobulin light chain genes in tetrapods can be classified into three distinct groups: kappa (κ), lambda (λ), and ... Free immunoglobulin light chains secreted by neoplastic plasma cells, such as in multiple myeloma, can be called Bence Jones ... Immunoglobulin+Light+Chains at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Educational Resource for ...
pIgR has a strong specificity to polymeric immunoglobulins and is not responsive to monomeric immunoglobulin. The ligand's J- ... "Entrez Gene: PIGR polymeric immunoglobulin receptor". Kaetzel CS (August 2005). "The polymeric immunoglobulin receptor: ... Polymeric immunoglobulin receptor (pIgR) is a transmembrane protein that in humans is encoded by the PIGR gene. It is an Fc ... Polymeric+Immunoglobulin+Receptor at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology This ...
The immunoglobulin heavy chain (IgH) is the large polypeptide subunit of an antibody (immunoglobulin). In human genome, the IgH ... There are five types of mammalian immunoglobulin heavy chain: γ, δ, α, μ and ε. They define classes of immunoglobulins: IgG, ... Immunoglobulin+Heavy+Chains at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Educational Resource for ... Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs ...
... , or sometimes Immunoglobulin binding protein is a generic name for any protein that binds ... Immunoglobulin-binding protein 1 (IGBP1), a protein that binds B-cells in the blood. Protein A, a 42 kDa protein originally ... It, therefore, can mean: Binding immunoglobulin protein (BiP, or heat shock 70 kDa protein 5, with an official symbol HSPA5), a ...
V-set domains are found in diverse protein families, including immunoglobulin light and heavy chains; in several T-cell ... "Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A". J. Mol. Biol. 190 (4): 593-604. doi: ... Immunoglobulin V-set, subgroup InterPro: IPR003596 T-cell surface antigen CD2 InterPro: IPR013285 ACAM; ACAN; ADAMTSL1; AGC1; ...
The underlying cause of MIDD is the production of monoclonal immunoglobulins. Monoclonal immunoglobulins are produced in ... The immunoglobulin heavy chain in HCDD is frequently a truncated heavy chain. HCDD is the rarest subtype of MIDD. Serum protein ... Monoclonal immunoglobulins are produced by monoclonal plasma cells, which are found in a variety of plasma cell dyscrasias. The ... Monoclonal Immunoglobulin Deposition Disorder, or MIDD, is a disease characterised by the deposition of monoclonal ...
MAdCAM-1 belongs to a subclass of the immunoglobulin superfamily (IgSF), the members of which are ligands for integrins. The ... In molecular biology, the adhesin molecule (immunoglobulin-like) is a protein domain. This domain is found in mucosal vascular ... "The structure of immunoglobulin superfamily domains 1 and 2 of MAdCAM-1 reveals novel features important for integrin ... crystal structure of this domain has been reported; it adopts an immunoglobulin-like beta-sandwich structure, with seven ...
Selective immunoglobulin A (IgA) deficiency (SIgAD) is a kind of immunodeficiency, a type of hypogammaglobulinemia. People with ... They rarely present with severe reactions, including anaphylaxis, to blood transfusions or intravenous immunoglobulin due to ... There is an inherited inability to produce immunoglobulin A (IgA), a part of the body's defenses against infection at the ... There is a historical popularity in using intravenous immunoglobulin (IVIG) to treat SIgAD, but the consensus is that there is ...
I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signalling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis. ADAMTSL1, ADAMTSL3, ALPK3, AXL, BOC, C9orf94, CADM2, CADM4, CCDC141, CDON, CEACAM7, CHL1, CILP2, CNTN1, CNTN2, CNTN3, CNTN4, CNTN5, CNTN6, CXADR, DCC, DSCAM, DSCAML1, ESAM, FGFR1, FGFR3, FGFR4, FGFRL1, FLT1, FLT4, FSTL4, FSTL5, HMCN1, HNT, HSPG2, ICAM5, IGFBP7, IGFBPL1, IGSF10, IGSF22, IGSF9, ISLR, KALRN, KAZALD1, KDR, KIAA0626, KIRREL, KIRREL2, KIRREL3, L1CAM, LINGO1, LINGO2, LRFN2, LRFN3, LRFN4, LRFN5, LRIG1, LRIG2, ...
The leukocyte immunoglobulin-like receptors (LILR) are a family of receptors possessing extracellular immunoglobulin domains. ... LAIR1 Killer-cell immunoglobulin-like receptor David E. Sloane; Nicodemus Tedla; Muyiwa Awoniyi; Donald W. MacGlashan Jr.; Luis ... v t e v t e v t e (Protein pages needing a picture, Immunoglobulin superfamily, All stub articles, Biochemistry stubs, Receptor ... Borges; K. Frank Austen; Jonathan P. Arm (November 2004). "Leukocyte immunoglobulin-like receptors: novel innate receptors for ...
... is a protein that in humans is encoded by the IGSF3 gene. The protein encoded by this gene ... "Entrez Gene: Immunoglobulin superfamily member 3". Retrieved 2018-10-06. v t e This article incorporates text from the United ... is an immunoglobulin-like membrane protein containing several V-type Ig-like domains. A mutation in this gene has been ...
C1-set domains are found almost exclusively in molecules involved in the immune system, such as in immunoglobulin light and ...
CD2 CD4 VCAM1 Smith DK, Xue H (1997). "Sequence profiles of immunoglobulin and immunoglobulin-like domains". J. Mol. Biol. 274 ... Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. ... CD4 is the primary receptor for HIV-1. CD4 has four immunoglobulin-like domains in its extracellular region that share the same ... The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by ...
... (TIM) proteins are a family of cell surface immunomodulatory proteins. TIM1 Kane ...
Members of the IgSF family include the human killer cell immunoglobulin-like receptor (KIR) and the Immunoglobulin-like ... includes immunoglobulin-like transcripts (ILT, also known as leukocyte immunoglobulin-like receptors (LIRs)), leukocyte- ... Human killer cell immunoglobulin-like receptors recognize the α1 and α2 domains of class I human leukocyte antigens (HLA-A, -B ... Killer-cell immunoglobulin-like receptors (KIRs), are a family of type I transmembrane glycoproteins expressed on the plasma ...
... is a immunoglobulin gene with symbol IGHA1. It encodes a constant (C) segment of ... Immunoglobulin A is an antibody that plays a critical role in immune function in the mucous membranes. IgA shows the same ... "Entrez Gene: IGHA1 immunoglobulin heavy constant alpha 1". Kratzin, H.; Altevogt, P.; Ruban, E.; Kortt, A.; Staroscik, K.; ... "IGHA1 immunoglobulin heavy constant alpha 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-10-16 ...
Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most ... This repertoire of immunoglobulins is crucial for the newborns who are very sensitive to infections, especially within the ... Stadlmann J, Pabst M, Kolarich D, Kunert R, Altmann F (2008). "Analysis of immunoglobulin glycosylation by LC-ESI-MS of ... de Haan, Noortje; Falck, David; Wuhrer, Manfred (2019-07-08). "Monitoring of Immunoglobulin N- and O-glycosylation in Health ...
Posts about immunoglobulin written by What Doctors Dont Tell You ...
... is a class of antibody (a type of protein) found in the blood and tissue fluids. ... There are five classes of immunoglobulin; of these, immunoglobulin G (IgG) is the major immunoglobulin in human blood. The IgG ... Immunoglobulin is a class of antibody (a type of protein) found in the blood and tissue fluids. Immunoglobulins are produced by ... Immunoglobulins also play a central role in allergies and hypersensitivity reactions. In this case they bind to antigens that ...
... immunoglobulin G (IgG), immunoglobulin A (IgA), immunoglobulin M (IgM), immunoglobulin D (IgD), and immunoglobulin E (IgE). The ... Serum immunoglobulin and immunoglobulin G subclasses in children with allergic colitis. West Afr J Med. 1998 Jul-Sep. 17(3):206 ... Immunoglobulin G deficiency. Changes in serum immunoglobulin G concentrations during infancy and childhood. View Media Gallery ... encoded search term (Immunoglobulin G Deficiency) and Immunoglobulin G Deficiency What to Read Next on Medscape ...
Intravenous Immunoglobulin Therapy (IVIg) Medically Reviewed by Jennifer Robinson, MD on August 15, 2022 ... Liquid immunoglobulin is taken from the blood plasma of donors who are screened to make sure they are healthy. The plasma is ... Immunoglobulin is part of your bloods plasma. It has antibodies in it to fight germs or disease. When people donate blood, ... Youd get shots with small amounts of immunoglobulin under your skin either once a week or every few days. Talk to your doctor ...
An immunoglobulins test measures the levels of certain antibodies in your blood. Abnormal levels can indicate a serious health ... What is an immunoglobulins blood test?. This test measures the amount of immunoglobulins in your blood. Immunoglobulins are ... Why do I need an immunoglobulins blood test?. You may need this test if you have symptoms that could mean your immunoglobulin ... An immunoglobulins test usually measures three main types of immunoglobulin (Ig) antibodies that do different jobs to protect ...
Immunoglobulin G: A class of immunoglobulins found in all body fluids. They are the smallest but most common antibodies (75 ...
Immunoglobulin (IG) is a life-sustaining, blood plasma-derived product that has become standard immune replacement therapy for ... established treatment guidelines to support doctors and nurses in correctly dosing and administering intravenous immunoglobulin ... Standards needed for immunoglobulin therapy. August 12, 2005. ScienceBlog.com A review article published in the July/August ... Immunoglobulin (IG) is a life-sustaining, blood plasma-derived product that has become standard immune replacement therapy for ...
What Is an Allergen-Specific Immunoglobulin E Test?. An allergen-specific immunoglobulin E (IgE) test measures the levels of ... Antibodies (also called immunoglobulins) are proteins the immune system makes to protect the body from bacteria, viruses, and ...
Intravenous immunoglobulin (IVIG) has been used primarily for immune deficiency patients, and its greatest expansion is seen ... Intravenous immunoglobulin (IVIG) is a polymeric highly purified immunoglobulin fraction derived from large pools of up to ... With immunoglobulin treatment, 48% to 92% (mean, 87%) of the patients were reported to improve at least 1 grade on the global ... High-dose immunoglobulin therapy in sporadic inclusion body myositis: a double-blind, placebo-controlled study. J Neurol. 2000; ...
Hazard - P - B - T - Risk Exempt. According to the European Medicines Agency guideline on environmental risk assessments for pharmaceuticals (EMA/CHMP/SWP/4447/00),vitamins, electrolytes, amino acids, peptides, proteins, carbohydrates, lipids proteins, vaccines and herbal medicinal products are exempted because they are unlikely to result in significant risk to the environment. ...
The UK EQUATOR Centre is hosted by the Centre for Statistics in Medicine (CSM), NDORMS, University of Oxford. The EQUATOR Network website and database is provided by the UK EQUATOR Centre.. ...
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IGLVIVOR22-1 immunoglobulin lambda variable (IV)/OR22-1 (pseudogene) [Homo sapie... IGLVIVOR22-1 immunoglobulin lambda variable ... immunoglobulin lambda variable (IV)/OR22-1 (pseudogene)provided by HGNC. Primary source. HGNC:HGNC:15694 See related. IMGT/GENE ... IGLVIVOR22-1 immunoglobulin lambda variable (IV)/OR22-1 (pseudogene) [ Homo sapiens (human) ] Gene ID: 84088, updated on 25-Jan ...
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Antibodies (also called immunoglobulins) are proteins the immune system makes to recognize and get rid of germs. ... An IgA test measures the blood level of immunoglobulin A, one of the most common types of antibodies in the body. ...
... Scand J Immunol. 1976;5(1-2):9-14. doi: 10.1111/j.1365-3083.1976. ... The three immunoglobulins showed reactions of antigenic identity with the corresponding Ig classes of serum when examined with ...
... they include autoantibodies against liver-specific and non-liver-specific antigens and increased immunoglobulin G (IgG) levels. ... Serum Proteins and Immunoglobulins. An immunoglobulin G (IgG)-predominant polyclonal hypergammaglobulinemia is a common finding ... If immunoglobulin G (IgG) is over the upper limit of normal (ULN), assign 1 point; if it is over 1.10 times the ULN, assign 2 ...
"Immunoglobulin Subunits" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... The PROTEIN SUBUNITS of the multimeric IMMUNOGLOBULIN proteins, such as IGA; IGD; IGE; IGG; and IGM. Included are the heavy and ... This graph shows the total number of publications written about "Immunoglobulin Subunits" by people in Harvard Catalyst ... Below are the most recent publications written about "Immunoglobulin Subunits" by people in Profiles. ...
The global intravenous immunoglobulin market is expected to witness robust growth in the near future due to rise in prevalence ... Intravenous Immunoglobulin (IVIG) Market: Improved Technology for Production and Purification Methods. February 25th, 2021 ... The global intravenous immunoglobulin market is characterized by the presence of major companies competing against each other ... In terms of revenue, North America dominated the global intravenous immunoglobulin market in 2017. The U.S. FDA approval for ...
Global Immunoglobulins Market: OverviewThis report analyzes the current and future scenario of the global immunoglobulins ... Immunoglobulins Market Global Industry Analysis, Size, Share, Growth, Trends, and Forecast 2018 - 2026. ... Global Immunoglobulins Market: Regional Outlook. In terms of region, the global immunoglobulins market has been segmented into ... Global Immunoglobulins Market: Overview. This report analyzes the current and future scenario of the global immunoglobulins ...
Immunoglobulins (antibodies) are the glycoproteins involved in the immune response. Immunoglobulins recognize and bind antigens ... the most common human immunoglobulins, represent 75% of all plasma immunoglobulins and have several functions including ... In addition, immunoglobulins differ in their structure and shape, especially in the non-variable portion of the antibody [3]. ... Immunoglobulins are separated into 5 subclasses, IgG, IgA, IgM, IgD and IgE. The classes are distinguished by their ...
J:164272 Giudicelli V, et al., IMGT/GENE-DB: a comprehensive database for human and mouse immunoglobulin and T cell receptor ...
Anti-HLA-A antibody produced in mouse is polyclonal, unconjugated and is suitable for flow cytometry, western blot
Immunoglobulin E (IgE) secondary antibodies * » Immunoglobulin G (IgG) secondary antibodies * » Immunoglobulin M (IgM) ... Anti-Immunoglobulin E (IgE). Reactivity. Host. Unconj.. AP. Biotin. FITC. HRP. TRITC. PE. ... anti-Immunoglobulin E (IgE) secondary antibodies. Written/Edited by Julian Pampel, BSc ...
The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on ... Immunoglobulin Fc Heterodimer Platform Technology: From Design to Applications in Therapeutic Antibodies and Proteins Front ... Immunoglobulin Fc heterodimers have been engineered through modifications to the CH3 domain interface, with different mutations ... The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on ...
By-products of immunoglobulin somatic hypermutation. *Mark. Bemark, Mats LU and Neuberger, Michael S. (2003) In Genes ... we analyzed aberrant rearrangements involving the immunoglobulin loci in a human B-cell line (Ramos) that performs Ig V gene ... we analyzed aberrant rearrangements involving the immunoglobulin loci in a human B-cell line (Ramos) that performs Ig V gene ... we analyzed aberrant rearrangements involving the immunoglobulin loci in a human B-cell line (Ramos) that performs Ig V gene ...
IGCJ, JCH, Immunoglobulin J chain, IGJ. Introduction. Immunoglobulin J chain (IGJ) helps to link 2 monomer units of either IgM ... or IgA and also also helps to bind these immunoglobulins to secretory component. When it comes to IgM, the J chain-joined dimer ...
All genes belonging to the secretome have been classified according to function based on Uniprot molecular function and biological processes keywords. The functional annotations are prioritized according to the following hierarchy: Blood coagulation, Complement pathway, Acute phase, Cytokine, Hormone, Neuropeptide, Growth factor, Receptor, Transport, Developmental protein, Defence, Enzyme, Enzyme inhibitor, Transcription, Immunity, Cell adhesion, Other and each gene is assigned a single function.. ...
  • Immunoglobulins are also called antibodies. (medlineplus.gov)
  • IgM antibodies are the first immunoglobulins your body makes after you're exposed to germs. (medlineplus.gov)
  • An IgA test measures the blood level of immunoglobulin A, one of the most common types of antibodies in the body. (kidshealth.org)
  • Antibodies (also called immunoglobulins) are proteins the immune system makes to recognize and get rid of germs . (kidshealth.org)
  • Immunoglobulins (antibodies) are the glycoproteins involved in the immune response. (visualscience.ru)
  • The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on homodimerization of the fragment crystallizable (Fc) regions of two identical heavy chains (HCs) and the subsequent assembly of two identical light chains (LCs) via disulfide linkages between each HC and LC. (nih.gov)
  • You are being given this leaflet if you receive immunoglobulin therapy, either to support an immune system that is under-producing antibodies (primary or secondary antibody deficiency) or to help treat a condition resulting from an overactive immune system. (esht.nhs.uk)
  • The existence of immunoglobulin G antibodies specifically indicates recent or prior infection and can help identify individuals with an adaptive immune response to SARS-CoV-2. (pharmacytimes.com)
  • Officials with the FDA have issued an emergency use authorization for the Anti-SARS-CoV-2 S1 Curve ELISA (IgG), an assay for the qualitative and semi-quantitative detection of immunoglobulin G antibodies formed against the SARS-CoV-2 antigen in human serum and plasma. (pharmacytimes.com)
  • According to a press release, clinical laboratories can immediately begin using the assay for the detection of immunoglobulin G antibodies. (pharmacytimes.com)
  • Assays that enable the detection of [immunoglobulin G] antibodies are an important tool in the arsenals of scientists and researchers working to understand the nature of SARS-CoV-2 and prevent the spread of other highly infectious viruses like it in the future," said Wolfgang Schlumberger, MD, CEO of EUROIMMUN, in the press release. (pharmacytimes.com)
  • Antibodies in the dam's colostrum, specifically immunoglobulins G and A, are the reason why newborn calves are able to immediately combat bacterial and viral pathogens in the environment. (cornell.edu)
  • The underlying pathology is the autoimmune production of immunoglobulin G (IgG) antibodies directed toward receptors on the postsynaptic membrane at neuromuscular junctions (NMJs). (medscape.com)
  • The infusion therapy nursing specialists who authored the Journal of Infusion Nursing article, titled, "Developing Practice Guidelines for the Administration of Intravenous Immunoglobulin," offer an in-depth examination of all aspects of IVIG treatment, including the benefits and risks, and the roles of physicians, nurses and patients in achieving best results from therapy, as well as a comprehensive look at the expanding use of IVIG therapy and the associated clinical challenges. (scienceblog.com)
  • Intravenous immunoglobulin (IVIG) has been used primarily for immune deficiency patients, and its greatest expansion is seen more and more in the treatment of autoimmune disorders, especially in neurology. (nursingcenter.com)
  • Intravenous immunoglobulin (IVIG) is a polymeric highly purified immunoglobulin fraction derived from large pools of up to 60,000 plasma donors. (nursingcenter.com)
  • According to the report, the global intravenous immunoglobulin market was valued at US$ 8,983.5 Mn in 2017 and is projected to expand at a CAGR of 8.1% from 2018 to 2026. (medgadget.com)
  • The global intravenous immunoglobulin market is expected to witness robust growth in the near future due to rise in prevalence of autoimmune disorders, increase in the global geriatric population, surge in IVIG usage in off-label indications, high demand for more reliable and adequate treatment measures, and increase in incidence of various hematological and neurological disorders. (medgadget.com)
  • The report offers detailed segmentation of the global intravenous immunoglobulin market. (medgadget.com)
  • This is anticipated to drive demand for better immunological treatments, which in turn would provide opportunities for the companies operating in the global intravenous immunoglobulin market. (medgadget.com)
  • Hospitals, clinics, and home care are the major end-users of intravenous immunoglobulin (IVIG). (medgadget.com)
  • Hence, home care is anticipated to be the most lucrative end-user segment of the global intravenous immunoglobulin market during the forecast period. (medgadget.com)
  • In terms of revenue, North America dominated the global intravenous immunoglobulin market in 2017. (medgadget.com)
  • Large patient pool, developing economies, and presence of large underserved patient population are the key factors augmenting the intravenous immunoglobulin market in the region. (medgadget.com)
  • Intravenous immunoglobulin is a therapeutic consideration for patients with SIgM deficiency who have demonstrated findings of defective antigen-specific IgG responses, particularly if they lack IgG against encapsulated bacteria and have chronic or recurrent sinopulmonary infection. (medscape.com)
  • Immunoglobulin G (IgG) is a type of antibody. (wikipedia.org)
  • Immunoglobulin is a class of antibody (a type of protein ) found in the blood and tissue fluids. (daviddarling.info)
  • Immunoglobulins, which are protein molecules that contain antibody activity, are produced by the terminal cells of B-cell differentiation known as plasma cells. (medscape.com)
  • Immune Deficiency Foundation: "Immunoglobulin Therapy & Other Medical Therapies for Antibody Deficiencies. (webmd.com)
  • Immunoglobulin E (IgE) is a type of protein in the body called an antibody. (kidshealth.org)
  • IgG antibody subtype is the most abundant serum immunoglobulins of the immune system. (sigmaaldrich.com)
  • In addition, immunoglobulins differ in their structure and shape, especially in the non-variable portion of the antibody [3]. (visualscience.ru)
  • The immunoglobulins derive their name as they migrate with globular proteins when antibody-containing serum is placed in an electrical field. (medscape.com)
  • If you have severe side effects from IVIg, you might be able to switch to another type of treatment called subcutaneous immunoglobulin therapy, or SCIG. (webmd.com)
  • The action of IVIG is mediated through both the variable and the constant regions of the Fab 2 as well as the Fc portion of the immunoglobulin molecule. (nursingcenter.com)
  • The three immunoglobulins showed reactions of antigenic identity with the corresponding Ig classes of serum when examined with rabbit antisera against human IgG, IgA, and IgM. (nih.gov)
  • A positive correlation was observed between serum IgM levels and the density of corresponding immunoglobulin-containing cells. (bmj.com)
  • The major immunoglobulin isotype class in normal human serum. (umassmed.edu)
  • Indications for serum immunoglobulin testing include diagnosis and monitoring of monoclonal gammopathies and immune deficiencies. (medscape.com)
  • To analyze the presence of selective immunoglobulin M immunodeficiency (SIgMD) among long-term clozapine-treated outpatients in a nested case-control study. (psychiatrist.com)
  • Selective immunoglobulin M immunodeficiency (SIgMD) is a rare form of dysgammaglobulinemia, which is characterized by a selective low level of IgM in conjunction with normal T cell numbers and function and no other identifiable immunodeficiency. (psychiatrist.com)
  • Hong R, Gupta S. Selective immunoglobulin M deficiency in an adult with Streptococcus pneumoniae sepsis and invasive aspergillosis. (medscape.com)
  • Belgemen T, Suskan E, Dogu F, Ikinciogullari A. Selective Immunoglobulin M Deficiency Presenting with Recurrent Impetigo: A Case Report and Review of the Literature. (medscape.com)
  • Antar M, Lamarche J, Peguero A, Reiss A, Cole S. A case of selective immunoglobulin M deficiency and autoimmune glomerulonephritis. (medscape.com)
  • Chronic recurrent multifocal osteomyelitis in a patient with selective immunoglobulin M deficiency. (medscape.com)
  • Immunoglobulins are produced by cells of the immune system known as B-lymphocytes . (daviddarling.info)
  • An immunoglobulins blood test measures the amounts of IgM, IgG, and IgA in your blood to help diagnose different types of health conditions that may affect your immune system. (medlineplus.gov)
  • With these disorders your immune system attacks your own healthy cells by mistake, including cells that make immunoglobulins. (medlineplus.gov)
  • You may also need this test if your provider thinks you may have high levels of immunoglobulins from an autoimmune disease or a cancer that affects your blood, bone marrow, and/or immune system. (medlineplus.gov)
  • Rise in neurology, immunology, hematology, and other disease prevalence, high unmet medical needs, and rich pipeline are likely to be major drivers of the global immunoglobulins market during the forecast period. (bccresearch.com)
  • In a recent study published in Science Immunology , researchers evaluated immunoglobulin G (IgG) responses to coronavirus disease 2019 (COVID-19) messenger ribonucleic acid (mRNA) vaccinations. (news-medical.net)
  • In terms of route of administration, the global immunoglobulins market has been classified into intravenous, subcutaneous, and intramuscular. (bccresearch.com)
  • Among anti-S memory B lymphocytes, the frequency of immunoglobulin G4 subclass-switched B lymphocytes (from IgG1 and IgG3 to IgG4) was 14.0% (median) compared to the repertoire of memory B lymphocytes (median of 1.0%) post-booster doses. (news-medical.net)
  • These studies provide evidence that immunoglobulins belonging to the same IgG1 subtype can have notable differences in their conformational stability, dynamics, aggregation propensity, hydration properties and their response to co-solutes. (ku.edu)
  • Members of the IgG class of immunoglobulins can be subdivided according to their biochemical features, which include their affinity for complement system proteins and their concentration in the plasma [4]. (visualscience.ru)
  • Proteins, such as immunoglobulins, are inherently dynamic molecules with unique biological functions. (ku.edu)
  • If you have too few immunoglobulins, you have an immunodeficiency. (medlineplus.gov)
  • You may need an immunoglobulins test if immunodeficiency runs in your family, or your health care provider thinks you may have a problem making normal levels of immunoglobulins. (medlineplus.gov)
  • Efficacy, safety and pharmacokinetics of a new 10% normal human immunoglobulin for intravenous infusion, BT595, in children and adults with primary immunodeficiency disease. (iasp-pain.org)
  • Autoimmune neuropathies encompass acute forms such as Guillain-Barre syndrome (GBS) and its variants, as well as chronic forms including chronic inflammatory demyelinating polyradiculoneuropathy (CIDP), multifocal motor neuropathy, and polyneuropathies associated with immunoglobulin M (IgM) monoclonal gammopathy and paraneoplastic neuropathies. (nursingcenter.com)
  • An immunoglobulin G (IgG)-predominant polyclonal hypergammaglobulinemia is a common finding in patients with untreated autoimmune hepatitis. (medscape.com)
  • Schematic representation of an immunoglobulin G molecule. (medscape.com)
  • Immunoglobulins have important roles in humoral immunity, and they consist of 5 major classes or isotypes: immunoglobulin G (IgG), immunoglobulin A (IgA), immunoglobulin M (IgM), immunoglobulin D (IgD), and immunoglobulin E (IgE). (medscape.com)
  • The combination of methylprednisolone and intravenous immunoglobulins works better than intravenous immunoglobulins alone for multisystem inflammatory syndrome in children (MIS-C), researchers say. (the-hospitalist.org)
  • To characterize the types of by-products of somatic hypermutation, we analyzed aberrant rearrangements involving the immunoglobulin loci in a human B-cell line (Ramos) that performs Ig V gene hypermutation constitutively during culture. (lu.se)
  • Immunoglobulins recognize and bind antigens and can be found in the plasma linked to lymphocyte cellular membranes. (visualscience.ru)
  • This report analyzes the current and future scenario of the global immunoglobulins market for the period 2018 to 2026. (bccresearch.com)
  • A network of Sub Regional Advisory Panels (SRIAPs) was created by NHS England in 2018 to manage immunoglobulin usage by ensuring it is only used in accordance with national guidelines, as developed by an expert consensus group drawn from across the UK. (plymouthhospitals.nhs.uk)
  • B-cell immunity is mediated by the immunoglobulins and is commonly referred to as humoral immunity. (medscape.com)
  • Adaptive immune responses require rearrangement of the genes responsible for the specific recognition structures, ie, immunoglobulins for humoral immunity and T-cell receptors for cellular immunity. (medscape.com)
  • IMGT/GENE-DB: a comprehensive database for human and mouse immunoglobulin and T cell receptor genes. (jax.org)
  • The most abundant class of immunoglobulins in the blood is IgG (73%), which has a molecular weight of 150 kd. (medscape.com)
  • of these, immunoglobulin G (IgG) is the major immunoglobulin in human blood. (daviddarling.info)
  • IgGs, the most common human immunoglobulins, represent 75% of all plasma immunoglobulins and have several functions including triggering the complement system (the proteolytic plasma enzyme cascade involved in antigen degradation in the blood). (visualscience.ru)
  • A class of immunoglobulins found in all body fluids. (rxlist.com)
  • NC16A, a non-collagenous stretch of the BP180 ectodomain, is the primary target of pathogenic immunoglobulin (Ig)G autoantibodies and IgE class autoantibodies. (unboundmedicine.com)
  • After 5.0 months to 7.0 months of the second mRNA vaccination, anti-SARS-CoV-2 IgG responses primarily comprised the non-inflammatory immunoglobulin G4 subclass and were enhanced by the booster dose or breakthrough infection. (news-medical.net)
  • N- glycosylation of immunoglobulin G ( IgG ) plays a key role in the development of SLE by affecting the balance of anti-inflammatory and proinflammatory responses. (bvsalud.org)
  • How was your experience with hepatitis B immunoglobulin? (rxwiki.com)
  • What tips would you provide a friend before taking hepatitis B immunoglobulin? (rxwiki.com)
  • What are you taking hepatitis B immunoglobulin for? (rxwiki.com)
  • How well did hepatitis B immunoglobulin work for you? (rxwiki.com)
  • How likely would you be to recommend hepatitis B immunoglobulin to a friend? (rxwiki.com)
  • Hepatitis B Immunoglobulin should be used during pregnancy only if the possible benefit outweighs the possible risk to the unborn baby. (rxwiki.com)
  • Hepatitis B Immunoglobulin should be given to a pregnant woman only if clearly needed. (rxwiki.com)
  • Take hepatitis b immunoglobulin exactly as prescribed by your doctor. (rxwiki.com)
  • Assessment of immunoglobulin use for hepatitis A control in New Mexico. (cdc.gov)
  • The intra- and intermolecular interactions that govern the dynamic nature and function of immunoglobulins may also influence their stability. (ku.edu)
  • Furthermore, molecular interactions in immunoglobulins can be unique at low and high concentrations, which necessitate newer complementary approaches to investigate such complex systems. (ku.edu)
  • In addition, an ultraviolet spectroscopy based approach was developed to understand interactions modulating solution viscosity in high concentration immunoglobulin solutions. (ku.edu)
  • You don't need any special preparations for an immunoglobulins blood test. (medlineplus.gov)
  • Biomeda's immunoglobulin (IgG) preparations are used for affinity columns, blocking agents, and normal controls in a variety of immuno assays. (biomeda.com)
  • IgG deficiencies may occur as isolated deficiencies (eg, selective IgG deficiency) or in association with deficiencies of other immunoglobulin types. (medscape.com)
  • For information on deficiencies of other immunoglobulin types, see the Medscape Reference articles IgA Deficiency , IgD Deficiency , and IgM Deficiency . (medscape.com)
  • During the therapy, prepared immunoglobulin is infused into your veins. (webmd.com)
  • Immunoglobulin (IG) is a life-sustaining, blood plasma-derived product that has become standard immune replacement therapy for most people living with PI. (scienceblog.com)
  • Among the 181 cases they scrutinized, 111 fulfilled the World Health Organization criteria for MIS-C. Of these, the researchers were able to match 64 patients who had received immunoglobulins alone with 32 who had received the combined therapy and could be matched using propensity scores. (the-hospitalist.org)
  • Those receiving the combination therapy spent a mean of 4 days in the pediatric intensive care unit compared with 6 days for those receiving immunoglobulins alone. (the-hospitalist.org)
  • You'd get shots with small amounts of immunoglobulin under your skin either once a week or every few days. (webmd.com)
  • Immunoglobulins can be extracted from the blood of recovering patients and used for passive immunization against certain infectious diseases. (daviddarling.info)
  • This repertoire of immunoglobulins is crucial for the newborns who are very sensitive to infections, especially within the respiratory and digestive systems. (wikipedia.org)
  • Your blood may break down about half of the immunoglobulin over that period, so you'll need another dose to keep fighting infections. (webmd.com)
  • So, even though your levels are high, you may have frequent infections and other symptoms of low immunoglobulin levels. (medlineplus.gov)
  • You may need this test if you have symptoms that could mean your immunoglobulin levels are too low. (medlineplus.gov)
  • Therefore, due to speculated immunosuppressive effects of clozapine as a part of its antipsychotic effect, which can alter levels of immunoglobulins and eventually may lead to SIgMD, we investigated the presence of SIgMD among clozapine-treated patients with the purpose of clinical management. (psychiatrist.com)
  • Immunoglobulin is part of your blood's plasma. (webmd.com)
  • Liquid immunoglobulin is taken from the blood plasma of donors who are screened to make sure they are healthy. (webmd.com)
  • Immunoglobulins are glycoprotein molecules that are produced by plasma cells in response to an immunogen. (medscape.com)
  • The use of cell lines does, however, introduce a risk the immunoglobulin (Ig)-secreting plasma cell in the spleen, of obtaining cell line-specific features as a result of the trans- gut, or BM [1, 2]. (lu.se)
  • Immunoglobulin J chain (IGJ) helps to link 2 monomer units of either IgM or IgA and also also helps to bind these immunoglobulins to secretory component. (prospecbio.com)
  • Association between immunoglobulin G N-glycosylation and lupus nephritis in female patients with systemic lupus erythematosus: a case-control study. (bvsalud.org)
  • Reference ranges of immunoglobulins may vary based on sex and factors such as alcohol use, smoking status, and chronic conditions (eg, diabetes/metabolic syndrome) (see Considerations). (medscape.com)
  • Since steroids and immunoglobulin create a partial splenic dysfunction, through different mechanisms, we investigated whether combined treatment with both drugs could produce a rapid platelet count increase comparable to that of splenectomy. (karger.com)
  • In the group whose jejunal biopsies were normal using routine histological examination, the predominant type of immunoglobulin-containing cell was IgA followed by IgM, then IgG, with the approximate ratio of 3:2:1 respectively. (bmj.com)
  • In childhood idiopathic thrombocytopenic purpura (ITP), both intravenous high-dose steroids and immunoglobulin treatments have been demonstrated to raise platelet counts reliably and in most cases within 72 h, when used as separate therapeutic modalities. (karger.com)
  • This graph shows the total number of publications written about "Immunoglobulin Subunits" by people in Harvard Catalyst Profiles by year, and whether "Immunoglobulin Subunits" was a major or minor topic of these publication. (harvard.edu)
  • The report also profiles major players operating in the global Immunoglobulins market based on various attributes, such as company overview, financial overview, product portfolio, business strategies, and recent developments. (bccresearch.com)
  • Immunoglobulin Subunits" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • The section also provides market attractiveness analysis based on region and market share analysis in terms of key players, thereby presenting a thorough analysis of the overall competitive scenario in the global immunoglobulins market. (bccresearch.com)