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Merck

A9935

Anti-Human IgM (μ-chain specific)−Agarose antibody produced in goat

affinity isolated antibody, PBS suspension

동의어(들):

Anti Human IgM Antibody - Anti-Human IgM (μ-chain specific)-Agarose antibody produced in goat, Anti Human Igm Antibody

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
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제품 이름

Anti-Human IgM (μ-chain specific)−Agarose antibody produced in goat, affinity isolated antibody, PBS suspension

biological source

goat

conjugate

agarose conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

PBS suspension

technique(s)

Ouchterlony double diffusion: suitable
immunoelectrophoresis: suitable

capacity

2-3 mg/mL, resin binding capacity (human IgM)

storage temp.

2-8°C

target post-translational modification

unmodified

Quality Level

Application

Anti-Human IgM (μ-chain specific)−Agarose antibody produced in goat has been used in affinity chromatography purification of human IgM.
Goat polyclonal anti-Human IgM (μ-chain specific)−Agarose antibody conjugate is used as an immuno-adsorbent to affinity purify antibodies, to remove species specific cross-reacting antibodies or to remove contaminating antibodies from an antiserum preparation. It has been used for IgM depletion from normal human serum from fasted patients.

Biochem/physiol Actions

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.

Disclaimer

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.

General description

Goat polyclonal anti-Human IgM (μ-chain specific)−Agarose antibody specific for human IgM when tested against purified human IgA, IgG, IgM, and kappa and lambda light chains. No reactivity with mouse or rat IgG is observed by Ouchterlony Double Diffusion (ODD), prior to agarose bead coupling.
IgM is a highly conserved antibody in vertebrates and is expressed early during immune response. It exists as a pentamer and is secreted by peritoneal B cells.
Immunoglobulin M (IgM) antibodies appear early in the course of infections. IgM antibodies are responsible for agglutination of red blood cells in mis-matched blood transfusions. The level of IgM may vary with the status of disease or infection.
Cyanogen bromide activated cross-linked beaded agarose is frequently conjugated to proteins such as immunoglobulins to facilitate their use in physicochemical processes such as precipitation, absorption and clarification.

Other Notes

Antibody adsorbed with mouse and rat IgG

Physical form

Suspension in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

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저장 등급

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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문서 라이브러리 방문

Rationally designed mimotope library for profiling of the human IgM repertoire
Pashov AD, et al.
bioRxiv, 308973-308973 (2018)
Anastas Pashov et al.
Frontiers in immunology, 10, 2796-2796 (2019-12-19)
Specific antibody reactivities are routinely used as biomarkers, but the antibody repertoire reactivity (igome) profiles are still neglected. Here, we propose rationally designed peptide arrays as efficient probes for these system level biomarkers. Most IgM antibodies are characterized by few
Whitney Bullard et al.
Virulence, 3(1), 72-76 (2012-01-31)
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Solid?phase preparation of protein complexes.
Pengo P, et al.
Journal of Molecular Recognition, 23(6), 551-558 (2010)
Jan Koopmans et al.
Cell transplantation, 13(6), 631-637 (2005-01-15)
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