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M3795

Sigma-Aldrich

IgM, Kappa from murine myeloma

clone TEPC 183, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Mouse IgM-κ

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Clone

TEPC 183, monoclonal

Pureté

≥90% (HPLC)

Forme

buffered aqueous solution

Concentration

2.0-2.2 mg/mL

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

Determined by the absorbance at 280 nm (E1%/280 = 11.8). Each vial contains at least 1 mg of purified myeloma protein.
IgM antibodies are present as pentamers in the serum and are produced in response to antigens IgM, κ from murine myeloma is produced by TEPC 183 tumor line introduced subcutaneously in BALB/c mice.
IgM is a highly conserved antibody in vertebrates and is expressed early during immune response. It is secreted by peritoneal B cells.

Spécificité

The TEPC 183 tumor line is pristine-induced plasmacytoma-originated and carried subcutaneously in BALB/c mice. The hapten binding specificity of the TEPC 183 line has not been determined. It specifically recognizes mouse IgM. Identity and purity of the immunoglobulin is established by immunoelectrophoresis.

Application

IgM, Kappa from murine myeloma has been used in:
  • sandwich enzyme linked immunosorbent assay (ELISA)
  • flow cytometry
  • dot-immunobinding assay

Actions biochimiques/physiologiques

IgM plays a key role in the engulfing of apoptotic cells. A reduction in serum IgM levels leads to increased autoimmune response and higher risk for infections. IgM displays polyreactive and autoreactive functionality. It plays a key role in tissue homeostasis by mediating clearance of tissue based molecules. IgM has sites for N-linked glycosylation, with sugars namely, mannose, galactose, N-acetyl glucosamine and sialic acid. IgM linked agarose resins have been tested for efficient conjugate binding.

Forme physique

Solution in 0.05 M Tris, 0.5 M sodium chloride, pH 8.0, containing 0.02% sodium azide

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

A monoclonal antibody that specifically binds chitosan in vitro and in situ on fungal cell walls
Schubert M, et al.
Journal of microbiology and biotechnology, 20(8), 1179-1184 (2010)
Max Schubert et al.
Journal of microbiology and biotechnology, 20(8), 1179-1184 (2010-08-28)
We report the generation of the first monoclonal antibody that specifically binds to the polysaccharide chitosan. Mice were immunized with a mixture of chitosans, and hybridoma clones were screened for specific binders resulting in the isolation of a single clone
Sequential genetic modification of the hprt locus in human ESCs combining gene targeting and recombinase-mediated cassette exchange
Di Domenico AI, et al.
Cloning and Stem Cells, 10(2), 217-230 (2008)
T Sulimenko et al.
Journal of immunological methods, 289(1-2), 89-95 (2004-07-15)
Mouse monoclonal antibodies of IgG subclasses and IgM class in hybridoma culture supernatants were quantified using a dot-immunobinding assay. Immunoglobulins were bound to nitrocellulose (NC) membrane and, after blocking, the membrane was incubated with anti-mouse antibody conjugated to horseradish peroxidase
A-O Hovden et al.
Scandinavian journal of immunology, 62(1), 36-44 (2005-08-12)
The aim of this study was to compare the kinetics and the magnitude of the humoral immune response to two different influenza vaccine formulations, whole and split virus vaccines. BALB/c mice were immunized intramuscularly with one or two doses (3

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