Mouse anti Pig IgM antibody, clone K52 1C3 recognizes porcine IgM heavy chain. No cross-reactivity with porcine IgA and IgG is seen in ELISA.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% Sodium Azide (NaN3)
- Carrier Free
- Porcine IgM
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells of immunised mice were fused with cells of the P3 - X63 - Ag 8.653 mouse myeloma line.
- Store at +4oC or at -20oC if preferred.
Storage in frost-free freezers is not recommended.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody.
- 18 months from date of despatch.
- For research purposes only
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Applications of IgM antibody
|Immunohistology - Frozen
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
- Flow Cytometry
- Use 10ul of the suggested working dilution to label 1x106 cells in 100ul
Copyright © 2019 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Negative Isotype Controls Available
Application Based External Images
Product Specific References
References for IgM antibody
Leitão, A. et al. (2001) The non-haemadsorbing African swine fever virus isolate ASFV/NH/P68 provides a model for defining the protective anti-virus immune response.
J Gen Virol. 82 (Pt 3): 513-23.
Baltes, N. et al. (2001) Actinobacillus pleuropneumoniae iron transport and urease activity: effects on bacterial virulence and host immune response.
Infect Immun. 69 (1): 472-8.
Hamano, M. et al. (2007) Detection of antibodies to Japanese encephalitis virus in the wild boars in Hiroshima prefecture, Japan.
Epidemiol Infect. 135: 974-7.
Andersen, J.K. et al. (1999) Systematic characterization of porcine ileal Peyer's patch, I. apoptosis-sensitive immature B cells are the predominant cell type.
Immunology. 98 (4): 612-21.
Bailey, M. (2004) Effects of infection with transmissible gastroenteritis virus on concomitant immune responses to dietary and injected antigens.
Clin Diagn Lab Immunol. 11: 337-43.
Pasternak, J.A. et al. (2015) Oral antigen exposure in newborn piglets circumvents induction of oral tolerance in response to intraperitoneal vaccination in later life.
BMC Vet Res. 11: 350.
Seele, J. et al. (2015) The immunoglobulin M-degrading enzyme of Streptococcus suis, IdeSsuis, is a highly protective antigen against serotype 2.
Vaccine. 33 (19): 2207-12.
Stepanova, H. et al. (2011) Association of attenuated mutants of Salmonella enterica serovar Enteritidis with porcine peripheral blood leukocytes.
FEMS Microbiol Lett. 321: 37-42.
Laycock, G. et al. (2012) A defined intestinal colonization microbiota for gnotobiotic pigs.
Vet Immunol Immunopathol. 149: 216-24.
Lewis MC et al. (2013) Dietary supplementation with Bifidobacterium lactis NCC2818 from weaning reduces local immunoglobulin production in lymphoid-associated tissues but increases systemic antibodies in healthy neonates.
Br J Nutr. 110: 1243-52.
Chen, F. et al. (2015) Generation of B Cell-Deficient Pigs by Highly Efficient CRISPR/Cas9-Mediated Gene Targeting.
J Genet Genomics. 42 (8): 437-44.
Rahe, M.C. & Murtaugh, M.P. (2017) Interleukin-21 Drives Proliferation and Differentiation of Porcine Memory B Cells into Antibody Secreting Cells.
PLoS One. 12 (1): e0171171.
Buermann, A. et al. (2018) Pigs expressing the human inhibitory ligand PD-L1 (CD 274) provide a new source of xenogeneic cells and tissues with low immunogenic properties.
Xenotransplantation. 25 (5): e12387.