Immunoglobulin epsilon chains. Medical search. Web

The class of heavy chains found in IMMUNOGLOBULIN E. They have a molecular weight of approximately 72 kDa and they contain about 550 amino acid residues arranged in five domains and about three times more carbohydrate than the heavy chains of IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; and IMMUNOGLOBULIN G.

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.

Complex of at least five membrane-bound polypeptides in mature T-lymphocytes that are non-covalently associated with one another and with the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL). The CD3 complex includes the gamma, delta, epsilon, zeta, and eta chains (subunits). When antigen binds to the T-cell receptor, the CD3 complex transduces the activating signals to the cytoplasm of the T-cell. The CD3 gamma and delta chains (subunits) are separate from and not related to the gamma/delta chains of the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA).

Molecule composed of the non-covalent association of the T-cell antigen receptor (RECEPTORS, ANTIGEN, T-CELL) with the CD3 complex (ANTIGENS, CD3). This association is required for the surface expression and function of both components. The molecule consists of up to seven chains: either the alpha/beta or gamma/delta chains of the T-cell receptor, and four or five chains in the CD3 complex.

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.

The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.

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)

Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)

Heavy chains of IMMUNOGLOBULIN G having a molecular weight of approximately 51 kDa. They contain about 450 amino acid residues arranged in four domains and an oligosaccharide component covalently bound to the Fc fragment constant region. The gamma heavy chain subclasses (for example, gamma 1, gamma 2a, and gamma 2b) of the IMMUNOGLOBULIN G isotype subclasses (IgG1, IgG2A, and IgG2B) resemble each other more closely than the heavy chains of the other IMMUNOGLOBULIN ISOTYPES.

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).

A recurrent breakpoint in the most common deletion of the Ig heavy chain locus (del A1-GP-G2-G4-E). (1/68)

Human Ig heavy chain constant regions are encoded by a cluster of genes, the IGHC locus, on 14q32.3. Several forms of IGHC deletions and duplications spanning one to five genes have been described in different populations, with frequencies of 1.5-3.5% and 4.5-44%, respectively. Despite the common occurrence of these gene rearrangements, little is known about the breakpoint sites; evidence obtained from deletions in the IGHC locus and in other regions of the human genome suggests that they preferentially occur in highly homologous regions and might be favored by a variety of recombinogenic signals. We present here a detailed study of three homozygotes for the most common type of IGHC multiple gene deletion, spanning the A1-GP-G2-G4-E genes. Using a combination of Southern blotting, long-range PCR, and automated sequencing, the unequal crossover events of all of the six studied haplotypes have been mapped to a region of approximately 2 kb with almost complete homology between EP1-A1 and E-A2, flanked by two minisatellites. These results are consistent with the hypothesis that segments of complete homology may be required for efficient homologous recombination in humans. The possible role of minisatellites as recombination signals is inferred, in agreement with current knowledge. (+info)

A transcriptional defect underlies B lymphocyte dysfunction in a patient diagnosed with non-X-linked hyper-IgM syndrome. (2/68)

To establish the underlying cause of hyper-IgM syndrome in one female patient, B cell function was examined in response to CD40- and IL-4-mediated pathways. When CD40-induced functional responses were measured in unfractionated B cells, CD80 up-regulation, de novo Cmu-Cgamma recombination, and Igamma transcription were all found to be relatively unaffected. However, CD40- and IL-4-mediated CD23 up-regulation and VDJ-Cgamma transcription were clearly diminished compared to control cells. IL-4-induced CD23 expression was measurably reduced in the CD20- population as well. These results suggested that the patient's defect is positioned downstream of CD40 contact and affects both CD40- and IL-4 signal transduction pathways. Further analysis of B cell function in CD19+ B cells revealed a clear B cell defect with respect to Igamma and mature VDJ-Cgamma transcription and IgG expression. However, under the same conditions Iepsilon transcription was relatively normal. Partial restoration of B cell function occurred if PBMC or CD19+ B cells were cultured in vitro in the presence of CD154 plus IL-4. Because addition of IL-4 to cocultures containing activated T cells failed to induce B cells to undergo differentiation, the ability of the patient's B cells to acquire a responsive phenotype correlated with receiving a sustained signal through CD40. These findings support a model in which the patient expresses an intrinsic defect that is manifested in the failure of specific genes to become transcriptionally active in response to either CD154 or IL-4 and results in a functionally unresponsive B cell phenotype. (+info)

Engagement of CD153 (CD30 ligand) by CD30+ T cells inhibits class switch DNA recombination and antibody production in human IgD+ IgM+ B cells. (3/68)

CD153 (CD30 ligand) is a member of the TNF ligand/cytokine family expressed on the surface of human B cells. Upon exposure to IL-4, a critical Ig class switch-inducing cytokine, Ag-activated T cells express CD30, the CD153 receptor. The observation that dysregulated IgG, IgA, and/or IgE production is often associated with up-regulation of T cell CD30 prompted us to test the hypothesis that engagement of B cell CD153 by T cell CD30 modulates Ig class switching. In this study, we show that IgD+ IgM+ B cells up-regulate CD153 in the presence of CD154 (CD40 ligand), IL-4, and B cell Ag receptor engagement. In these cells, CD153 engagement by an agonistic anti-CD153 mAb or T cell CD30 inhibits S mu-->Sgamma, Smu-->Salpha, and S mu-->Sepsilon class switch DNA recombination (CSR). This inhibition is associated with decreased TNFR-associated factor-2 binding to CD40, decreased NF-kappaB binding to the CD40-responsive element of the Cgamma3 promoter, decreased Igamma3-Cgamma3 germline gene transcription, and decreased expression of Ku70, Ku80, DNA protein kinase, switch-associated protein-70, and Msh2 CSR-associated transcripts. In addition, CD153 engagement inhibits IgG, IgA, and IgE production, and this effect is associated with reduced levels of B lymphocyte maturation protein-1 transcripts, and increased binding of B cell-specific activation protein to the Ig 3' enhancer. These findings suggest that CD30+ T cells modulate CSR as well as IgG, IgA, and IgE production by inducing reverse signaling through B cell CD153. (+info)

Molecular basis for nonanaphylactogenicity of a monoclonal anti-IgE antibody. (4/68)

IgE Abs mediate allergic responses by binding to specific high affinity receptors (FcepsilonRI) on mast cells and basophils. Therefore, the IgE/FcepsilonRI interaction is a target for clinical intervention in allergic disease. An anti-IgE mAb, termed BSW17, is nonanaphylactogenic, although recognizing IgE bound to FcepsilonRI, and interferes with binding of IgE to FcepsilonRI. Thus, BSW17 represents a candidate Ab for treatment of IgE-mediated disorders. By panning BSW17 against random peptide libraries displayed on phages, we defined mimotopes that mimic the conformational epitope recognized on human IgE. Two types of mimotopes, one within the Cepsilon3 and one within the Cepsilon4 domain, were identified, indicating that this mAb may recognize either a large conformational epitope or eventually two distinct epitopes on IgE. On the basis of alignments of the two mimotopes with the human IgE sequence, we postulate that binding of BSW17 to the Cepsilon3 region predominantly blocks binding of IgE to FcepsilonRI, leading to neutralization of IgE. Moreover, binding of BSW17 to the Cepsilon4 region may explain how BSW17 recognizes FcepsilonRI-bound IgE, and binding to this region may also interfere with degranulation of IgE sensitized cells (basophils and mast cells). As a practical application of these findings, mimotope peptides coupled to a carrier protein may be used for the development of a peptide-based anti-allergy vaccine by induction of anti-IgE Abs similar to the current approach of using humanized nonanaphylactogenic anti-IgE Abs as a passive vaccine. (+info)

Inhibition of IgG1 and IgE production by stimulation of the B cell CTLA-4 receptor. (5/68)

Although a large amount of information is available on the activity of CTLA-4 in T cells, the role of this receptor in B cells has not been previously characterized. Our results show that CD40 or LPS stimulation in the presence of IL-4 induces CTLA-4 expression in purified B cells; the maximum level is reached in both membrane and intracellular compartments after 48-72 h. Engagement of the B cell CTLA-4 by immobilized mAb inhibits IgG1 and IgE production and reduces the frequency of IgG1- and IgE-expressing B cells. Cepsilon and Cgamma(1) germline mRNA expression as well as NF-kappaB and STAT6 activation, events required for isotype switching, are also inhibited by CTLA-4 engagement. Together these findings show the critical role of CTLA-4 in the control of IL-4-driven isotype switching and suggest new approaches for modulating immediate-type hypersensitivity responses. (+info)

Activation of the mouse Ig germline epsilon promoter by IL-4 is dependent on AP-1 transcription factors. (6/68)

Induction of germline (GL) epsilon transcripts, an essential step preceding Ig isotype switching to IgE, requires activation of transcription factors by IL-4 and a B cell activator, e.g., CD40 ligand or LPS. We demonstrate that AP-1 (Fos and Jun), induced transiently by CD40 ligand or LPS, binds a DNA element in the mouse GL epsilon promoter. AP-1 synergizes with Stat6 to activate both the intact GL epsilon promoter and a minimal heterologous promoter driven by the AP-1 and Stat6 sites of the mouse GL epsilon promoter. By contrast, C/EBP beta, which trans-activates the human GL epsilon promoter, inhibits IL-4 induction of the mouse promoter, probably by attenuating the synergistic interaction between AP-1 and Stat6. Furthermore, AP-1 does not trans-activate the human GL epsilon promoter. Thus, induction of GL epsilon transcripts in mice and humans may be regulated differently. In addition, although mouse GL epsilon transcripts have a half-life of approximately 100 min, the RNA level continues to increase for up to 24 h, and the promoter appears to be active for at least 2 days after B cell activation. Altogether, these data suggest that induction of AP-1 activity, although transient, is required for activation of the mouse GL epsilon promoter by IL-4-induced Stat6. (+info)

IgE isotype determination: epsilon-germline gene transcription, DNA recombination and B-cell differentiation. (7/68)

Immunoglobulin class switching is the process which determines whether a B-cell secretes antibodies of the IgM, IgG, IgA or IgE class (or isotype). IgE is the antibody that mediates the allergic response by sensitising mast cells to allergens at the mucosal barrier. Class switching proceeds by three successive steps, culminating in the synthesis and secretion of antibody: these are germline gene transcription, DNA recombination and B-cell differentiation. We review here the present state of knowledge concerning the mechanisms involved in each of these steps, with particular reference to IgE. Intervention in the mechanisms that specify the selection of IgE may offer a means to combat allergy. (+info)

Differential regulation of mouse germline Ig gamma 1 and epsilon promoters by IL-4 and CD40. (8/68)

Before Ig class switching, RNA transcription through the specific S regions undergoing recombination is induced by cytokines and other activators that induce and direct switching. The resulting germline (GL) transcripts are essential for switch recombination. To understand the differential regulation of mouse IgG1 and IgE, we compared the promoters for GL gamma1 and epsilon transcripts. We addressed the question of why the promoter that regulates GL epsilon transcription is more responsive to IL-4 than the gamma1 promoter and also why GL epsilon transcription is more dependent on IL-4 than is gamma1 transcription. We found that the IL-4-responsive region of the GL epsilon promoter is more inducible than that of the gamma1 promoter, although each promoter contains a binding site for the IL-4-inducible transcription factor Stat6, located immediately adjacent to a binding site for a basic region leucine zipper (bZip) family protein. However, the arrangement and sequences of the sites differ between the epsilon and gamma1 promoters. The GL epsilon promoter binds Stat6 with a 10-fold higher affinity than does the gamma1 promoter. Furthermore, the bZip elements of the two promoters bind different transcription factors, as the GL epsilon promoter binds and is activated by AP-1, whereas the gamma1 promoter binds and is activated by activating transcription factor 2. C/EBPbeta and C/EBPgamma also bind the gamma1 bZip element, although they inhibit rather than activate transcription. However, inhibition of promoter activity by C/EBPbeta does not require the bZip element and may instead occur via inhibiting the activity of NF-kappaB. (+info)

Immunoglobulin E (IgE) chains are a type of heavy chain component of an immunoglobulin molecule, specifically belonging to the IgE class of antibodies. IgE is one of the five classes of antibodies (along with IgA, IgD, IgG, and IgM) that play a crucial role in the immune system's response to foreign substances, such as allergens, parasites, and toxins.

IgE molecules are composed of two heavy chains (ε-chains) and two light chains (either kappa or lambda). The ε-chains have a molecular weight of approximately 72 kDa and contain four constant regions (Cε1-Cε4) and one variable region (Vε). The variable region is responsible for antigen recognition, while the constant region interacts with effector cells like mast cells and basophils.

IgE molecules are primarily involved in type I hypersensitivity reactions, such as allergies, where they bind to Fc receptors on the surface of effector cells and trigger degranulation upon secondary exposure to an allergen. This process leads to the release of mediators like histamine, leukotrienes, and prostaglandins, which cause symptoms associated with allergic reactions, such as itching, swelling, and redness.

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.

CD3 antigens are a group of proteins found on the surface of T-cells, which are a type of white blood cell that plays a central role in the immune response. The CD3 antigens are composed of several different subunits (ε, δ, γ, and α) that associate to form the CD3 complex, which is involved in T-cell activation and signal transduction.

The CD3 complex is associated with the T-cell receptor (TCR), which recognizes and binds to specific antigens presented by antigen-presenting cells. When the TCR binds to an antigen, it triggers a series of intracellular signaling events that lead to T-cell activation and the initiation of an immune response.

CD3 antigens are important targets for immunotherapy in some diseases, such as certain types of cancer. For example, monoclonal antibodies that target CD3 have been developed to activate T-cells and enhance their ability to recognize and destroy tumor cells. However, CD3-targeted therapies can also cause side effects, such as cytokine release syndrome, which can be serious or life-threatening in some cases.

The Receptor-CD3 Complex is a multimeric protein complex found on the surface of T-cells, a type of white blood cell crucial to the adaptive immune system. The complex plays a critical role in the activation and regulation of T-cells. It is composed of the T-cell receptor (TCR) and the CD3 proteins (CD3δ, ε, γ, and ζ).

The T-cell receptor is responsible for recognizing specific antigens presented in the context of major histocompatibility complex (MHC) molecules on the surface of antigen-presenting cells. The CD3 proteins are involved in signal transduction upon TCR engagement with an antigen, leading to T-cell activation and downstream effects such as cytokine production and cytotoxicity.

An antigen is any substance (usually a protein) that can be recognized by the immune system and stimulate an immune response. Antigens are typically foreign substances, but they can also include self-proteins in certain circumstances, such as during autoimmune diseases. In the context of T-cells, antigens are presented in the form of peptides bound to MHC molecules on the surface of antigen-presenting cells.

T-cells are a type of lymphocyte that plays a central role in cell-mediated immunity. They recognize and respond to specific antigens, contributing to the elimination of infected or damaged cells and providing long-lasting immune protection against pathogens. T-cells can be further classified into various subsets based on their surface receptors and functions, including CD4+ helper T-cells, CD8+ cytotoxic T-cells, regulatory T-cells, and memory T-cells.

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.

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 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.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Immunoglobulin G (IgG) gamma chains are the heavy, constant region proteins found in IgG immunoglobulins, which are a type of antibody. These gamma chains are composed of four subunits - two heavy chains and two light chains - and play a crucial role in the immune response by recognizing and binding to specific antigens, such as pathogens or foreign substances.

IgG is the most abundant type of antibody in human serum and provides long-term immunity against bacterial and viral infections. The gamma chains contain a region that binds to Fc receptors found on various immune cells, which facilitates the destruction of pathogens or foreign substances. Additionally, IgG can cross the placenta, providing passive immunity to the fetus.

Abnormalities in the production or function of IgG gamma chains can lead to various immunodeficiency disorders, such as X-linked agammaglobulinemia, which is characterized by a lack of functional B cells and low levels of IgG antibodies.

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.

Flanagan JG, Rabbitts TH (1984). "The sequence of a human immunoglobulin epsilon heavy chain constant region gene, and evidence ... "Cloning and sequence determination of the gene for the human immunoglobulin epsilon chain expressed in a myeloma cell line". ... "Molecular cloning and nucleotide sequencing of human immunoglobulin epsilon chain cDNA". Nucleic Acids Research. 11 (3): 719-26 ... Ig epsilon chain C region is a protein that in humans is encoded by the IGHE gene. GRCh38: Ensembl release 89: ENSG00000211891 ...

https://en.wikipedia.org/wiki/IGHE

147180 Immunoglobulin: heavy epsilon chain; IGHE. Cross references. Phenotypically related immunodeficiencies. Incidence. ... Immunoglobulins of the IgE isotype are responsible for the immediate hypersensitivity reactions in diseases like hay fever, ...

http://structure.bmc.lu.se/idbase/IDRefSeq/xml/idr/ff/FF343155.html?style=GI

It does not crossreact with other immunoglobulin heavy chain isotypes. IgE exists in a transmembrane form that is expressed by ... It does not crossreact with other immunoglobulin heavy chain isotypes. IgE exists in a transmembrane form that is expressed by ... The G7-26 monoclonal antibody specifically recognizes the constant region of human Immunoglobulin E (IgE). ... The G7-26 monoclonal antibody specifically recognizes the constant region of human Immunoglobulin E (IgE). ...

https://www.bdbiosciences.com/ja-jp/products/reagents/immunoassay-reagents/elisa/purified-mouse-anti-human-ige.555857

Immunoglobulin E can also be called IGHE, Immunoglobulin Heavy Constant Epsilon, Ig epsilon chain C region, IgE. ... E04I0037 Rabbit Immunoglobulin E ELISA kit. Rabbit Immunoglobulin E ELISA kit is suitable for detecting samples from rabbit ... Citations of Rabbit Immunoglobulin E ELISA kit. E04I0037 has been referenced in the below publications: ... BlueGene Biotech Rabbit Immunoglobulin E ELISA kit * Immunology ... Specifications of Rabbit Immunoglobulin E ELISA kit. Product ...

https://www.elisakit.cc/products/rabbit-immunoglobulin-e-elisa-kit/

... immunoglobulin heavy chain #LOC90925 #epsilon IgE #AK128652 #AK128346 #BC144457 #PKI55 #AX746885 #LOC92249 #AK130294 #SNORD18C ... immunoglobulin epsilon chain constant... #ELK2AP #IGHCgamma1 #FLJ00385 #FLJ00382 #ADAM6 #BC042994 #Z49973 #BC011773 # ...

https://hivlatency.erc.monash.edu/unMappedGenes.txt

Recombinant Human High affinity immunoglobulin epsilon receptor subunit gamma(FCER1G),partial ... Alternative Name(s): Fc receptor gamma-chain ;FcRgammaFc-epsilon RI-gammaIgE Fc receptor subunit gamma ;FceRI gamma ... Recombinant Human High affinity immunoglobulin epsilon receptor subunit gamma(FCER1G),partial. CSB-EP008533HU1 Regular price $ ... Relevance: Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of ...

https://www.genebiosystems.com/en-us/products/recombinant-human-high-affinity-immunoglobulin-epsilon-receptor-subunit-gammafcer1g-partial

HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL CRYSTAL FORM 2 ... HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT: A. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. A ... Chain. Unique Chain. Rainbow. 2° Structure. Bfactor. Bfactor Range. SOA. Entropy. Clustal. Hydrophobic. Size. Charged. Polar. ... HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL CRYSTAL FORM 2 Coordinates. PDB Format Method. X-RAY ...

https://swissmodel.expasy.org/templates/1j89.1

Light chain types[edit]. Further information: Immunoglobulin light chain. In mammals there are two types of immunoglobulin ... the heavy chain types α (alpha), γ (gamma), δ (delta), ε (epsilon), μ (mu) give rise to IgA, IgG, IgD, IgE, IgM, respectively. ... Simplified overview of V(D)J recombination of immunoglobulin heavy chains. Somatic recombination of immunoglobulins, also known ... two identical heavy chains and two identical light chains connected by disulfide bonds.[8] Each chain is a series of domains: ...

https://en.wikipedia.org/wiki/Antibody

... identified as gamma heavy chain of human immunoglobulins. It reacts with all sub-classes of gamma chain of human ... immunoglobulins. It does not cross-react with alpha (IgA), mu (IgM), epsilon (IgE), or delta (IgD), heavy chains, T-cells, ... identified as gamma heavy chain of human immunoglobulins. It reacts with all sub-classes of gamma chain of human ... identified as gamma heavy chain of human immunoglobulins. It reacts with all sub-classes of gamma chain of human ...

https://fgf-erk.com/luciferase-chain-reaction-to-id2020/

The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by ... CD3 EPSILON AND DELTA ECTODOMAIN FRAGMENT COMPLEX IN SINGLE-CHAIN CONSTRUCT. 1ya5. Crystal structure of the titin domains z1z2 ... CD3 Epsilon and gamma Ectodomain Fragment Complex in Single-Chain Construct. 1koa. TWITCHIN KINASE FRAGMENT (C.ELEGANS), ... There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three ( ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=IGc2&START=786&END=858&E_VALUE=4.28e-12&TYPE=SMART&BLAST=LLGDTVLLQCKACGRPKPSITWKGPDQNILDTDNSSATYTISSCDSGESTLKICNLMPQDSGIYTCIAANDHG

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=IGc2&START=277&END=338&E_VALUE=3.91e-6&TYPE=SMART&BLAST=REGQKLLLHCEGRGNPVPQQYVWVKEGSEPPLKMTQESALIFPFLNKSDSGTYGCTATSNMG

Heavy Chain Diseases - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD Manuals - Medical ... without light chains. Epsilon (ε) heavy chain disease has not been described. Most heavy chain proteins are fragments of their ... Heavy chain diseases are neoplastic plasma cell disorders characterized by overproduction of monoclonal immunoglobulin heavy ... IgA Heavy Chain Disease (alpha chain disease) IgA heavy chain disease is the most common heavy chain disease and is sometimes ...

https://www.msdmanuals.com/en-in/professional/hematology-and-oncology/plasma-cell-disorders/heavy-chain-diseases

From NCBI Gene: The immunoglobulin epsilon receptor (IgE receptor) is the initiator of the allergic response. When two or more ... Fc epsilon RI alpha-chain. *Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide ... immunoglobulin E receptor, high-affinity, of mast cells, alpha polypeptide. Description. ... high affinity immunoglobulin epsilon receptor alpha-subunit. *high affinity immunoglobulin epsilon receptor subunit alpha ...

https://edrn.nci.nih.gov/data-and-resources/biomarkers/fcer1a/

Immunoglobulin delta-Chains. Immunoglobulins, epsilon-Chain. Immunoglobulin epsilon-Chains. Immunoglobulins, gamma-Chain. ... Immunoglobulins, alpha-Chain. Immunoglobulin alpha-Chains. Immunoglobulins, delta-Chain. ... Immunoglobulin Heavy Chains. Immunoglobulins, J-Chain. Immunoglobulin J-Chains. Immunoglobulins, Light-Chain. Immunoglobulin ... Immunoglobulins, Fc. Immunoglobulin Fc Fragments. Immunoglobulins, Heavy-Chain. ...

https://decs2012.bvsalud.org/I/rep_i2006.htm

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https://decs2015.bvsalud.org/I/rep_i2006.htm

https://decs2020.bvsalud.org/I/rep_i2006.htm

We also annotated two functional and distinct immunoglobulin epsilon genes and four distinctive functional immunoglobulin gamma ... we constructed and annotated the immunoglobulin heavy chain locus, finding an expansion on immunoglobulin variable genes ... Epsilon, Zeta, Eta, Theta, Iota, Kappa, Lambda, Mu, and Omicron) to escape from mRNA vaccine-induced antibodies. The variants ...

https://phgkb.cdc.gov/PHGKB/cdcSCFinder.action?Mysubmit=init&action=search&query=Larson++T+

CD3 epsilon and CD3 zeta (CD247). These CD3 subunits are structurally related members of the immunoglobulins super family ... Kosugi A, Saitoh S, Noda S, Yasuda K, Hayashi F, Ogata M, Hamaoka T: Translocation of tyrosine-phosphorylated TCRzeta chain to ... The Armenian hamster antibody H146-968 reacts with an intracellular epitope (amino acids 151-164) of CD3 zeta chain (CD247), ... Rozdzial MM, Kubo RT, Turner SL, Finkel TH: Developmental regulation of the TCR zeta-chain. Differential expression and ...

https://www.exbio.cz/research-product/antibodies/cd-and-related-antigens/anti-cd3-zeta-pe-cy-7

It is an immunoglobulin light chain either kappa or lambda, excreted in urine and found in various pathological conditions. ... Heavy chains are gamma, alpha, mu, epsilon, and delta. *Light chains are kappa and lambda ... Normally Ig molecule consists of 4 polypeptide chains 2 heavy chains and 2 light chains. ... Free monoclonal kappa or lambda light chain of immunoglobulin appears in the urine as Bence Jones Protein.. ...

https://emedicodiary.com/que/486/multiple-myeloma

Immunoglobulin heavy constant epsilon. * Relevance. IgE is the class of antibodies produced in the lungs, skin, and mucous ... ab152001 is purified Human IgE with kappa light chains produced in vitro from a monoclonal hybridoma. Original material is ...

https://www.abcam.com/products/proteins-peptides/native-human-ige-protein-ab152001.html

The basic structure of immunoglobulin (Ig) [1] molecules is a tetramer of two light chains and two heavy chains linked by ... There are five types of heavy chains: α, delta, epsilon, γ and mu, all consisting of a variable domain (VH) and three (in α, ... The β chain (β-2-microglobulin) is composed of a single extracellular domain. In class II [3], both the α and the β chains are ... The heavy chain of human histocompatibility antigen HLA-B7 contains an immunoglobulin-like region. ...

https://prosite.expasy.org/PDOC00262

Ig epsilon chain C region is a protein that in humans is encoded by the IGHE gene. (wikipedia.org)
Immunoglobulin E can also be called IGHE, Immunoglobulin Heavy Constant Epsilon, Ig epsilon chain C region, IgE. (elisakit.cc)

In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. (fgf-erk.com)
T cell activation through the antigen receptor (TCR) involves the cytoplasmic tails of the CD3 subunits CD3 gamma, CD3 delta, CD3 epsilon and CD3 zeta (CD247). (exbio.cz)
The heavy chain of human histocompatibility antigen HLA-B7 contains an immunoglobulin-like region. (expasy.org)
The portion of the heavy and light chains that contact the antigen is called the variable region. (bioexplorer.net)
The heavy chains of the IgG antibody are of the subclass Gamma, with two antigen binding sites. (bioexplorer.net)
The bispecific antigen-binding molecules of the invention are useful for the treatment of diseases and disorders in which an upregulated or induced Fc epsilon-R1 alpha-targeted immune response is desired and/or therapeutically beneficial. (justia.com)
CD3, also known as T3, is a member of the immunoglobulin superfamily that plays a role in antigen recognition, signal transduction, and T cell activation. (biolegend.com)

The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. (embl.de)

An antibody ( Ab ), also known as an immunoglobulin ( Ig ), [1] is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses . (wikipedia.org)
Description: Recognizes a protein of 75kDa, identified as gamma heavy chain of human immunoglobulins. (fgf-erk.com)
Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. (embl.de)
This entry represents a subtype of the immunoglobulin domain, and is found in a diverse range of protein families that includes glycoproteins, fibroblast growth factor receptors, vascular endothelial growth factor receptors, interleukin-6 receptor, and neural cell adhesion molecules. (embl.de)
In most plasma cell disorders, M-proteins (monoclonal immunoglobulin protein) are structurally similar to normal antibody molecules. (msdmanuals.com)
Disorders characterized by abnormal proliferation of immunoglobulin-producing cells and abnormal proliferation of immunoglobulin monoclonal (M protein)represent part of the spectrum of disease due to the neoplastic behavior of the B lymphocyte series. (emedicodiary.com)
We report on the cloning and expression of a recombinant F. gigantica 14-3-3 epsilon protein (rFg14-3-3e), and testing its effects on specific functions of goat peripheral blood mononuclear cells (PBMCs). (biomedcentral.com)
The protein encoded by this gene is the CD3-epsilon polypeptide, which together with CD3-gamma, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T-cell receptor-CD3 complex. (bioss.com.cn)

Each Ig molecules have either 2 kappa or 2 lambda light chains. (emedicodiary.com)
The major histocompatibility complex (MHC) molecules are made of two chains. (expasy.org)
Immunoglobulin A (IgA) molecules are important components of mucosal fluids. (biomedcentral.com)
Immunoglobulins are glycoprotein molecules that are produced by plasma cells in response to an immunogen. (medscape.com)

Primary humoral deficiencies vary from complete absence of B cells, serum immunoglobulin (Ig), or both to lacunar deficits that involve specific antibody responses to polysaccharides. (medscape.com)
Indications for serum immunoglobulin testing include diagnosis and monitoring of monoclonal gammopathies and immune deficiencies. (medscape.com)

Antibodies are glycoproteins belonging to the immunoglobulin superfamily . (wikipedia.org)
Description: Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. (fgf-erk.com)
Antibodies, also known as Immunoglobulins , are glycoproteins produced by the B lymphocytes upon encountering a pathogenic substance. (bioexplorer.net)
The present invention provides novel full-length human antibodies that bind to human Fc epsilon-R1 alpha (monospecific antibodies). (justia.com)
The present invention also provides novel bispecific antibodies (bsAbs) that bind to both Fc epsilon-R1 alpha and CD3 and activate T cells via the CD3 complex in the presence of Fc epsilon-R1 alpha-expressing cells. (justia.com)

A model of the Fc of immunoglobulin E". Molecular Immunology. (wikipedia.org)

The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms. (expasy.org)

Plasma cells are derived from B lymphocytes and produce immunoglobulin (Ig) which contains heavy and light chains. (emedicodiary.com)
The TCR/CD3 complex of T-lymphocytes consists of either a TCR alpha/beta or TCR gamma/delta heterodimer coexpressed at the cell surface with the invariant subunits of CD3 labeled gamma, delta, epsilon, zeta, and eta. (bioss.com.cn)

The G7-26 monoclonal antibody specifically recognizes the constant region of human Immunoglobulin E (IgE). (bdbiosciences.com)
The terms antibody and immunoglobulin are often used interchangeably, [1] though the term 'antibody' is sometimes reserved for the secreted, soluble form, i.e. excluding B-cell receptors. (wikipedia.org)
Schematic structure of an antibody: two heavy chains (blue, yellow) and the two light chains (green, pink). (wikipedia.org)
Human IgG antibody Laboratories manufactures the luciferase chain reaction to id2020 reagents distributed by Genprice. (fgf-erk.com)
Description: This recombinant Human IgG antibody reacts to the Fc region of all gamma heavy chains of human immunoglobulins, including G1, G2, G3, and G4. (fgf-erk.com)
The Armenian hamster antibody H146-968 reacts with an intracellular epitope (amino acids 151-164) of CD3 zeta chain (CD247), which is a component of TCR/CD3 complex expressed on T cells. (exbio.cz)
Rabbit anti-human IgE epsilon-chain antibody purified by ion exchange and human IgG absorbed. (arxsciences.com)
The immunoglobulins derive their name as they migrate with globular proteins when antibody-containing serum is placed in an electrical field. (medscape.com)
The antibody molecule comprises four polypeptide chains - two heavy chains and two light chains. (bioexplorer.net)
The heavy and light chains are held together by disulfide bonds, giving the structure of the antibody molecule a Y shape. (bioexplorer.net)
The other portion of the heavy and light chains that define their subtypes is known as the constant region, and the amino acid content of this region remains constant for each subtype of the antibody molecule. (bioexplorer.net)
Five antibody or immunoglobulins classes are categorized by their constant region differences. (bioexplorer.net)
The IgA1 antibody, also called secretory immunoglobulin or sIgA, is most commonly found in secretions in high quantities. (bioexplorer.net)
The OKT3 monoclonal antibody reacts with an epitope on the epsilon-subunit within the human CD3 complex. (biolegend.com)

Paraproteinaemia is a disorder characterized by abnormal proliferation of immunoglobulin-producing cells due to the neoplastic behavior of B-Lymphocytic series with an increase in serum level of homogenous immunoglobulin (monoclonal IG) or its fragments. (emedicodiary.com)

Multiple Myeloma Multiple myeloma is a cancer of plasma cells that produce monoclonal immunoglobulin and invade and destroy adjacent bone tissue. (msdmanuals.com)
In myeloma, plasma cells produce monoclonal (M) Ig of a single heavy and light chain commonly referred to as a paraprotein. (emedicodiary.com)

Like many cell surface receptors/markers, CD4 is a member of the immunoglobulin superfamily . (wikidoc.org)

Heavy chain diseases are neoplastic plasma cell disorders characterized by overproduction of monoclonal immunoglobulin heavy chains. (msdmanuals.com)
Atopy is a predisposition to an immune response against diverse antigens and allergens leading to CD4+ Th2 differentiation and overproduction of immunoglobulin E (IgE). (clairegood.com)

CD3 subunits gamma, delta and epsilon are required for proper assembly, trafficking and surface expression of the TCR complex. (thermofisher.com)
Along with the other CD3 subunits gamma and delta, the epsilon chain is required for proper assembly, trafficking and surface expression of the TCR complex. (thermofisher.com)

It reacts with all sub-classes of gamma chain of human immunoglobulins. (fgf-erk.com)
ab52959 reacts with CD3 epsilon. (abcam.cn)

An immunoglobulin associated with MAST CELLS . (nih.gov)

Normally Ig molecule consists of 4 polypeptide chains 2 heavy chains and 2 light chains. (emedicodiary.com)

Kubota T, Mukai K, Minegishi Y, Karasuyama H. Different stabilities of the structurally related receptors for IgE and IgG on the cell surface are determined by length of the stalk region in their alpha-chains. (bdbiosciences.com)
These CD3 subunits are structurally related members of the immunoglobulins super family encoded by closely linked genes on human chromosome 11. (exbio.cz)

There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). (embl.de)
Immunoglobulin D (IgD) is composed of two delta (δ) heavy chains and two light chains. (bankowe-promocje.pl)
The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. (bioss.com.cn)

No cross reactivity with other human heavy chains or mouse/rat/goat IgG. (fgf-erk.com)

From NCBI Gene: The immunoglobulin epsilon receptor (IgE receptor) is the initiator of the allergic response. (nih.gov)
In intrinsic B-cell defect, the alpha1 gene may be deleted along with other heavy-chain genes. (medscape.com)

Linkage and sequence homology of two human immunoglobulin gamma heavy chain constant region genes" (PDF). (wikipedia.org)

It is defined as a group of disorders arising from the abnormal proliferation of a single clone of immunoglobulin-secreting cells giving rise to paraproteinaemia. (emedicodiary.com)

There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). (embl.de)
There are two types of light chains - Lambda and Kappa. (bioexplorer.net)

[ 1 ] In 1993, Plebani et al described 2 siblings who appeared to be healthy and who did not have increased infections despite extensive deletion of immunoglobulin heavy chain locus. (medscape.com)

two identical heavy chains and two identical light chains connected by disulfide bonds . (wikipedia.org)
The most common abnormality is the production of excess of light chains over heavy chains. (emedicodiary.com)
The excess light chains are secreted into the extracellular fluid and readily pass through the glomerulus. (emedicodiary.com)
ab152001 is purified Human IgE with kappa light chains produced in vitro from a monoclonal hybridoma. (abcam.com)
Monomeric IgA consists of two heavy chains and two light chains, which are stabilized by non-covalent interactions. (biomedcentral.com)
Each heavy chain is composed of four subdomains: the variable region of the heavy chain (VH), and the constant regions α1 (Cα1), Cα2 and Cα3, whereas the light chains have two subdomains, the variable region of the light chain (VL) and the constant region (CL) (Figure 1 ). (biomedcentral.com)
Each light chain is made up of polypeptides of around 20,000 Da. (bioexplorer.net)
light chain variable domain. (justia.com)

Rabbit Immunoglobulin E ELISA kit is suitable for detecting samples from rabbit species. (elisakit.cc)

In class I [ 2 ] the α chain is composed of three extracellular domains, a transmembrane region and a cytoplasmic tail. (expasy.org)
In class II [ 3 ], both the α and the β chains are composed of two extracellular domains, a transmembrane region and a cytoplasmic tail. (expasy.org)
D 1 and D 3 resemble immunoglobulin variable (IgV) domains. (wikidoc.org)
D 2 and D 4 resemble immunoglobulin constant (IgC) domains. (wikidoc.org)

Immunoglobulins of the IgE isotype are responsible for the immediate hypersensitivity reactions in diseases like hay fever, allergic asthma, and anaphalaxis. (lu.se)

however both chains are required for signal transduction . (lookformedical.com)

He stayed at Sheffield and undertook research into the molecular basis of Immunoglobulin E (IgE) receptor interactions with a focus on therapeutic intervention in allergy graduating with a PhD in 1997. (nottingham.ac.uk)

The immunoglobulins are divided into 5 different classes, based on differences in the amino acid sequences in the constant region of the heavy chains. (medscape.com)
All immunoglobulins within a given class have very similar heavy chain constant regions. (medscape.com)

Associates with a variety of FcR alpha chains to form a functional signaling complex. (genebiosystems.com)
CD3ε is a 20 kD chain of the CD3/T cell receptor (TCR) complex, which is composed of two CD3ε, one CD3γ, one CD3δ, one CD3ζ (CD247), and a T cell receptor (α/β or γ/δ) heterodimer. (biolegend.com)

Heavy chain diseases are plasma cell disorders that are typically malignant. (msdmanuals.com)
Heavy chain diseases are considered in patients with clinical manifestations suggesting lymphoproliferative disorders. (msdmanuals.com)

Diagnosis requires the detection of a monoclonal alpha chain on immunofixation electrophoresis. (msdmanuals.com)
If this monoclonal alpha chain cannot be found in serum or urine, intestinal biopsy is required. (msdmanuals.com)
The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits. (lookformedical.com)

Each heavy chain comprises large polypeptides of around 50,000 Da. (bioexplorer.net)

The β chain (β-2-microglobulin) is composed of a single extracellular domain. (expasy.org)
Contains 1 Ig-like (immunoglobulin-like) domain. (abcam.cn)
The immunoglobulin variable (IgV) domain of D 1 adopts an immunoglobulin-like β-sandwich fold with seven β-strands in 2 β-sheets, in a Greek key topology . (wikidoc.org)

Epsilon ( ε ) heavy chain disease has not been described. (msdmanuals.com)
IgA heavy chain disease is the most common heavy chain disease and is sometimes called Mediterranean lymphoma (immunoproliferative small intestinal disease). (msdmanuals.com)
IgA heavy chain disease usually appears between ages 10 and 30 years and is geographically concentrated in the Middle East. (msdmanuals.com)

Therefore, homozygous deletions of large portions of the Ig heavy-chain locus result in individuals with complete absence of 3 or more Ig classes (IgG2, IgG4, IgA1, occasionally IgE). (medscape.com)
Monomeric IgA is also one of the major immunoglobulin classes present in serum, second only to IgG. (biomedcentral.com)
In humans, the production of IgA per day is greater than that of the other classes of immunoglobulins combined [ 1 ]. (biomedcentral.com)

Chemicals and Drugs8

Phenomena and Processes1

Information Science1

A recurrent breakpoint in the most common deletion of the Ig heavy chain locus (del A1-GP-G2-G4-E). (1/68)

A transcriptional defect underlies B lymphocyte dysfunction in a patient diagnosed with non-X-linked hyper-IgM syndrome. (2/68)

Engagement of CD153 (CD30 ligand) by CD30+ T cells inhibits class switch DNA recombination and antibody production in human IgD+ IgM+ B cells. (3/68)

Molecular basis for nonanaphylactogenicity of a monoclonal anti-IgE antibody. (4/68)

Inhibition of IgG1 and IgE production by stimulation of the B cell CTLA-4 receptor. (5/68)

Activation of the mouse Ig germline epsilon promoter by IL-4 is dependent on AP-1 transcription factors. (6/68)

IgE isotype determination: epsilon-germline gene transcription, DNA recombination and B-cell differentiation. (7/68)

Differential regulation of mouse germline Ig gamma 1 and epsilon promoters by IL-4 and CD40. (8/68)

Immunoglobulin epsilon-Chains

Immunoglobulin Heavy Chains

Antigens, CD3

Receptor-CD3 Complex, Antigen, T-Cell

Immunoglobulins

Immunoglobulin G

Immunoglobulin Constant Regions

Encyclopedias as Topic

Immunoglobulin gamma-Chains

Genes, Immunoglobulin

A recurrent breakpoint in the most common deletion of the Ig heavy chain locus (del A1-GP-G2-G4-E). (1/68)

A transcriptional defect underlies B lymphocyte dysfunction in a patient diagnosed with non-X-linked hyper-IgM syndrome. (2/68)

Engagement of CD153 (CD30 ligand) by CD30+ T cells inhibits class switch DNA recombination and antibody production in human IgD+ IgM+ B cells. (3/68)

Molecular basis for nonanaphylactogenicity of a monoclonal anti-IgE antibody. (4/68)

Inhibition of IgG1 and IgE production by stimulation of the B cell CTLA-4 receptor. (5/68)

Activation of the mouse Ig germline epsilon promoter by IL-4 is dependent on AP-1 transcription factors. (6/68)

IgE isotype determination: epsilon-germline gene transcription, DNA recombination and B-cell differentiation. (7/68)

Differential regulation of mouse germline Ig gamma 1 and epsilon promoters by IL-4 and CD40. (8/68)

IGHE - Wikipedia

Fact file for ε isotype deficiency

Purified Mouse Anti-Human IgE

Rabbit Immunoglobulin E ELISA kit - Shanghai BlueGene Biotech CO., LTD.

LOC728392

Recombinant Human High affinity immunoglobulin epsilon receptor subuni - GeneBio Systems

1j89.1 | SWISS-MODEL Template Library

Antibody - Wikipedia

Luciferase Chain Reaction To Id2020 - Fibroblast growth factor

SMART: IGc2 domain annotation

SMART: IGc2 domain annotation

Heavy Chain Diseases - Hematology and Oncology - MSD Manual Professional Edition

FCER1A - Early...

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

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DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

DeCS 2006 - Changed terms

CDC Science Clips

Anti-CD3 zeta PE-Cy™7 - EXBIO Antibodies

Multiple Myeloma - Emedicodiary

Native Human IgE protein (ab152001) | Abcam

PROSITE

IGHE2

Antigen7

Basic structure of immunoglobulin1

Protein8

Molecules4

Serum immunoglobulin2

Antibodies5

Immunology1

Affinity1

Lymphocytes2

Antibody14

Increase in serum1

Produce monoclonal2

Superfamily1

Overproduction2

Subunits gamma2

Reacts2

Mast cells1

Molecule1

Structurally2

Delta3

Reactivity1

Gene2

Sequence1

Abnormal1

Lambda2

Deletion1

Light8

Rabbit1

Domains4

Isotype1

Signal transduction1

Interactions1