Human IgM Antibody (YA3610)
(Synonyms: MU; VH; AGM1)Based on 1 Customer Validation
Human IgM Antibody (YA3610) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Human IgM.
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Host:
Mouse
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Isotype:
IgG1
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Application:
WB, IHC-P, FC, ELISA
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Reactivity :
Human
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Formulation:
Supplied in PBS with 0.05% sodium azide
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:1000 | 1:200-1:400 | 1:10000 |
Product Details
Human IgM Antibody (YA3610) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Human IgM.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 75 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 49 kDa
Purified recombinant fragment of human IGHM (AA: 310-452) expressed in E. Coli.
affinity purified.
Non-conjugated
Unmodified
IgG1
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS with 0.05% sodium azide
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Human IgM is a 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. 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; Constant 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. 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. 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. 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; Constant 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[1][2][3][4][5][6][7][8].
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Subcellular Localization
Secreted; Cell membrane; Single-pass membrane protein
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Isoforms & Post-Translational Modification
P01871 has 2 isomers: P01871-2: 51924 Da (predicted); P01871-1: 49440 Da (predicted).
N-glycosylated; important for IgM secretion and its localization at the plasma membrane. The interaction with FCMR is glycan-independent -
Subunit
The basic structural unit of both sIgM and mIgM molecules consists of two identical heavy chains and two identical light chains; disulfide-linked. N-terminal variable regions of the heavy and light chains form the antigen binding sites, whereas the C-terminal constant regions of the heavy chains interact with immune receptors to mediate effector functions
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SwissProt ID
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Synonyms
MU; VH; AGM1
Documentation
References
[1]. Schroeder HW Jr, et al. Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010 Feb;125(2 Suppl 2):S41-52. [Content Brief]
[2]. McHeyzer-Williams M, et al. Molecular programming of B cell memory. Nat Rev Immunol. 2011 Dec 9;12(1):24-34. [Content Brief]
[3]. Teng G, et al. Immunoglobulin somatic hypermutation. Annu Rev Genet. 2007;41:107-20. [Content Brief]
[4]. Li Y, et al. Structural insights into immunoglobulin M. Science. 2020 Feb 28;367(6481):1014-1017. [Content Brief]
[5]. Chen Q, et al. Structural basis for Fc receptor recognition of immunoglobulin M. Nat Struct Mol Biol. 2023 Jul;30(7):1033-1039. [Content Brief]
[6]. Kishore U, et al. Modular organization of the carboxyl-terminal, globular head region of human C1q A, B, and C chains. J Immunol. 2003 Jul 15;171(2):812-20. [Content Brief]
[7]. Gadjeva MG, et al. Interaction of human C1q with IgG and IgM: revisited. Biochemistry. 2008 Dec 9;47(49):13093-102. [Content Brief]
[8]. Lloyd KA, et al. Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor. Sci Rep. 2017 Feb 23;7:42989. [Content Brief]