Native Human IgM protein is a Human Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Native
Tag free
SDS-PAGE
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. 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. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).Isoform 1Constant region of secreted IgM (sIgM), also known as the Fc region of IgM antibody. Able to multimerize, forms high order polymers, mainly pentamers and occasionally hexamers, providing for multivalency and high avidity recognition of antigens (PubMed:32029689, PubMed:37095205). Natural sIgM are polyreactive and recognize conserved self- and pathogen-derived structures, whereas immune sIgM are secreted only upon exposure to pathogens and are antigen-specific. Both natural and immune sIgM are required for an efficient humoral immune response to infection (By similarity). Mediates sIgM effector functions mostly via Fc receptors and the complement system. On lymphoid cells binds high-affinity Fc receptor FCMR and promotes induction of an efficient neutralizing IgG response while maintaining tolerance to self-antigens. Recruits C1q complement component to initiate the classical complement pathway, facilitating the recognition and neutralization of pathogens by the host. Together with C1q and mannose-binding lectin promotes the phagocytosis of apoptotic cells by macrophages, ensuring the clearance of potential autoimmune epitopes from tissues (By similarity) (PubMed:12847249, PubMed:19006321, PubMed:28230186, PubMed:32029689). Involved in mucosal immunity. It is transported by transcytosis across mucosal epithelium by PIGR and secreted on the apical side in complex with PIGR secretory component to scan mucosal lining for pathogens. IgM-antigen complexes undergo FCMR-mediated retrotranscytosis across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (By similarity) (PubMed:32029689).Isoform 2Constant region of membrane-bound IgM, part of the B cell receptor complex (BCR). IgM BCR provides constitutive tonic signaling for B cell survival. Mediates pre-BCR signaling that regulates B cell selection and rearrangement of Ig genes via allelic exclusion.
Immunoglobulin heavy constant mu, Ig mu chain C region, Ig mu chain C region BOT, Ig mu chain C region GAL, Ig mu chain C region OU, IGHM
Native Human IgM protein is a Human Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Native
Tag free
SDS-PAGE
No
No
Human
pH: 8
Preservative: 0.05% Sodium azide
Constituents: 1.16% Sodium chloride, 0.79% Tris HCl
Full Length
950 kDa
Native
Liquid
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. 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. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
N-glycosylated; important for IgM secretion and its localization at the plasma membrane. The interaction with FCMR is glycan-independent.
Dry Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Human myeloma plasma protein.
Protein Determination: Extinction Coefficient (E) 0.1% at 280nm = 1.18.
Prepared from myeloma plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
This supplementary information is collated from multiple sources and compiled automatically.
IgM also known as immunoglobulin M is a type of antibody with a molecular mass of approximately 970 kDa. It is the largest antibody present in the human circulatory system mostly found in plasma and lymphatic tissue. IgM is secreted primarily by B cells as a pentamer with a J chain providing a high avidity for antigens. When bound to an antigen IgM can activate the complement system a part of the immune system that helps clear pathogens from an organism.
IgM acts as the first line of defense during the initial stages of an immune response. It plays an important part in agglutination and neutralization of pathogens forming a complex that alerts other components of the immune system to take action. IgM exists before class-switching to IgG providing immediate protection. It also plays a role in antibody-dependent cellular cytotoxicity. Although not typically a long-term solution its presence is critical for providing initial protection until more specific antibodies like IgG and IgA are produced.
The immune response that involves IgM begins with the activation of the classical complement pathway. This pathway bridges the innate and adaptive immunity ensuring the communication and coordination of immune responses. The pathway involves C1q protein binding to IgM-antigen complexes. IgM also interacts with antigen-presenting cells facilitating the processing of antigens and interaction with T cells. These interactions connect IgM with other proteins like IgG and IgA influencing various immune response pathways.
IgM is associated with conditions such as Waldenström's macroglobulinemia and rheumatoid arthritis. Waldenström's macroglobulinemia involves the overproduction of IgM by clonal B cells leading to symptoms like anemia bleeding and neuropathy. Rheumatoid arthritis shows increased IgM levels as part of the autoimmune response affecting joints. In these diseases the IgM antibody interacts with rheumatoid factor and other immune proteins involved in inflammation demonstrating its significant role in autoimmunity and abnormal immune responses.
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SDS-PAGE (reduced/heated) analysis of ab90348. Lane 1 - 5μg, Lane 2 - 10μg, Lane 3 - 20μg, Lane 4 - 10μg.
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