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Human IGJ / Immunoglobulin J chain Protein (His Tag)

IGCJ,JCH

Catalog Number P13015-H08E
Organism Species Human
Host E. coli
Synonyms IGCJ,JCH
Molecular Weight The recombinant human IGJ comprises 147 amino acids and has a predicted molecular mass of 17 kDa. It migrates as an approximately 26 kDa band in SDS-PAGE under reducing conditions.
predicted N Gln 23
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human IGJ (NP_653247.1) (Gln 23-Asp 159) was fused with a polyhistidine tag at the C-terminus and a pelB singnal peptide at the N-terminus.
Bio-activity
Research Area
Formulation Lyophilized from sterile PBS, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Immunoglobulin J chain, also known as IGJ and IGCJ, is a secreted polypeptide which is the first immunoglobulin-related polypeptide expressed during the embryogenesis and differentiation of B cells in the fetal liver. The joining Immunoglobulin J chain is a small polypeptide, expressed by mucosal and glandular plasma cells, which regulates polymer formation of immunoglobulin (Ig)A and IgM. Immunoglobulin J chain / IGJ serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. Immunoglobulin J chain / IGJ also help to bind these immunoglobulins to secretory component. J-chain incorporation into polymeric IgA (pIgA, mainly dimers) and pentameric IgM endows these antibodies with several salient features. Immunoglobulin J chain / IGJ is involved in creating the binding site for pIgR / SC in the Ig polymers, not only by determining the polymeric quaternary structure but apparently also by interacting directly with the receptor protein. Both the immunoglobulin J chain / IGJ and the pIgR/SC are key proteins in secretory immunity.
Reference
  • Zikan, J. et al., 1985, Proc Natl Acad Sci USA. 82 (17): 5905-9.
  • Koshland, M.E. et al., 1985, Annu Rev Immunol. 3: 425-53.
  • Iwase,T. et al., 1993, Cell Struct Funct. 18 (5): 297-302.
  • Johansen, F.E. et al., 2000, Scand J Immunol. 52 (3): 240-8.
  • Lim, J.H. et al., 2006, J Immunol. 177 (8): 5420-9.