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AB97007

Goat Anti-Mouse IgM mu chain (DyLight® 488)

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(1 Publication)

Suitable for IHC-P, Flow Cyt, ICC/IF. Cited in 1 publication.

View Alternative Names

Igh-6, Ighm, Immunoglobulin heavy constant mu

1 Images
Flow Cytometry (Intracellular) - Goat Anti-Mouse IgM mu chain (DyLight® 488) (AB97007)
  • Flow Cyt (Intra)

Unknown

Flow Cytometry (Intracellular) - Goat Anti-Mouse IgM mu chain (DyLight® 488) (AB97007)

Overlay histogram showing HeLa cells stained with ab130935 (red line). The cells were fixed with 4% paraformaldehyde (10 min) and then permeabilized with 0.1% PBS-Triton X-100 for 20 min. The cells were then incubated in 1x PBS / 10% normal goat serum / 0.3M glycine to block non-specific protein-protein interactions followed by the antibody (ab130935, 1μg/1x10^6 cells) for 30 min at 22°C. The secondary antibody used was DyLight® 488 goat anti-mouse IgM (mu chain) at 1/500 dilution for 30 min at 22°C. Isotype control antibody (black line) was mouse IgM [ICIGM] (ab91545, 2μg/1x10^6 cells) used under the same conditions. Unlabelled sample (blue line) was also used as a control. Acquisition of >5,000 events were collected using a 20mW Argon ion laser (488nm) and 525/30 bandpass filter. This antibody gave a positive signal in HeLa fixed with 80% methanol (5 min)/permeabilized with 0.1% PBS-Triton X-100 for 20 min used under the same conditions.

Key facts

Host species

Goat

Target species

Mouse

Target isotype

IgM

Target specificity

Mu chain

Minimal cross-reactivity
Pre-adsorbed

No

Conjugation

DyLight® 488

Excitation/Emission

Ex: 493nm, Em: 518nm

Applications

ICC/IF, Flow Cyt, IHC-P

applications

Clonality

Polyclonal

Isotype

IgG

Specificity

By immunoelectrophoresis and ELISA this antibody reacts specifically with Mouse IgM. Cross reactivity with other immunoglobulins and light chains is less than 0.1%.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "IHC-P": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/50 - 1/500", "notes":"<p></p>" }, "Flow Cyt": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/50 - 1/500", "notes":"<p></p>" }, "ICC/IF": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/50 - 1/500", "notes":"<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Antiserum was solid phase adsorbed to ensure class specificity. This antibody was isolated by affinity chromatography using antigen coupled to agarose beads and conjugated to DyLight® 488.
Storage buffer
pH: 6.8 - 7.4 Preservative: 0.09% Sodium azide Constituents: PBS, 0.2% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Product protocols

Target data

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 (By similarity). 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 (By similarity).. Isoform 1. 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 (By similarity). 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 (PubMed : 10899913, PubMed : 28135254, PubMed : 34788614). 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 : 10899913, PubMed : 11062505, PubMed : 28135254). 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 (PubMed : 34788614).. Isoform 2. 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.
See full target information Ighm

Publications (1)

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Artificial cells, nanomedicine, and biotechnology 48:28-36 PubMed31852256

2019

Gellable silk fibroin-polyethylene sponge for hemostasis.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Wei,Jian Liu,ZhiBin Peng,Min Liang,YanSong Wang,XiaoQin Wang
View all publications

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