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Contributor Information

  • Name Tomasz Klaus ; Monika Bzowska ; Joanna Bereta
  • Institute Jagiellonian University

Tool Details

  • Tool name: Recombinant, super stable IgM, anti-blood group B antibody
  • Tool type: Antibodies
  • Class: Recombinant
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Application: ELISA ; Fn ; WB
  • Description: Adapted from Klaus et al Sci Rep. 2018 Jan 11;8(1):519. IgM is a multivalent antibody which evolved as a first line defense of adaptive immunity. It consists of heavy and light chains assembled into a complex oligomer. In mouse serum there are two forms of IgM, a full-length and a truncated one. The latter contains Î?' chain, which lacks a variable region. Although Î?' chain was discovered many years ago, its origin has not yet been elucidated. The inventing PI's results indicate that Î?' chain is generated from a full-length heavy chain by non-enzymatic cleavage of the protein backbone. The cleavage occurred specifically after Asn209 and is prevented by mutating this residue into any other amino acid. The process requires the presence of other proteins, preferentially with an acidic isoelectric point, and is facilitated by neutral or alkaline pH. This unique characteristic of the investigated phenomenon distinguishes it from other, already described, Asn-dependent protein reactions. A single IgM molecule is able to bind up to 12 epitopes via its antigen binding fragments (Fabs). The cleavage at Asn209 generates truncated IgM molecules and free Fabs, resulting in a reduced IgM valence and probably affecting IgM functionality in vivo.
  • Immunogen: various
  • Immunogen UniProt ID: various
  • Isotype: IgM
  • Research area: Other

  • For Research Use Only

Target Details

  • Target: Human blood group B antigen
  • Target background: Adapted from Klaus et al Sci Rep. 2018 Jan 11;8(1):519. IgM is a multivalent antibody which evolved as a first line defense of adaptive immunity. It consists of heavy and light chains assembled into a complex oligomer. In mouse serum there are two forms of IgM, a full-length and a truncated one. The latter contains Î?' chain, which lacks a variable region. Although Î?' chain was discovered many years ago, its origin has not yet been elucidated. The inventing PI's results indicate that Î?' chain is generated from a full-length heavy chain by non-enzymatic cleavage of the protein backbone. The cleavage occurred specifically after Asn209 and is prevented by mutating this residue into any other amino acid. The process requires the presence of other proteins, preferentially with an acidic isoelectric point, and is facilitated by neutral or alkaline pH. This unique characteristic of the investigated phenomenon distinguishes it from other, already described, Asn-dependent protein reactions. A single IgM molecule is able to bind up to 12 epitopes via its antigen binding fragments (Fabs). The cleavage at Asn209 generates truncated IgM molecules and free Fabs, resulting in a reduced IgM valence and probably affecting IgM functionality in vivo.

Application Details

  • Application: ELISA ; Fn ; WB

Handling

  • Format: Liquid
  • Shipping conditions: Shipping at 4°C

Documentation

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References

  • •  Klaus et al. 2018. Sci Rep. 8(1):519. PMID: 29323348.
  • •  IgM with improved stability and method for obtaining it and applications