Human Immunoglobulin D (IgD)
Native whole molecule protein, purified from multiple donor pool
Produktdetails
Synonyms
IgD
Description of Human Immunoglobulin D (IgD)
Human Immunoglobulin D (IgD) is a 185 kDa protein. Serum IgD is a unique immunoglobulin with a low plasma concentration (~30 µg/mL) and a half-life of 2.8 days. Structurally, IgD features a long hinge region rich in O-linked glycans, conferring flexibility for antigen binding and interaction with immune cells. While predominantly expressed as a membrane-bound receptor on mature B cells alongside IgM, secreted IgD is produced by plasma cells in mucosal tissues and circulates at trace levels. IgD enhances humoral immunity by binding basophils and mast cells via galectin-9 and CD44, triggering antimicrobial peptide release (e.g., cathelicidin) and cytokines like IL-4, IL-5, and IL-13, which promote Th2-mediated responses5. Additionally, IgD induces IgD-receptor expression on T lymphocytes, amplifying B-T cell cooperation and antibody production. Dysregulated IgD is linked to hyperimmunoglobulinemia D syndrome (HIDS), an autoinflammatory disorder characterized by recurrent fever, elevated serum IgD (>100 U/mL), and mutations in the mevalonate kinase gene. IgD also plays a role in IgD multiple myeloma, a rare plasma cell malignancy associated with lambda light chains, renal impairment, and poor prognosis. Clinically, serum IgD quantification aids in diagnosing HIDS and monitoring disease flares. Emerging therapeutic strategies target IgD-basophil interactions to modulate Th2 responses in allergies and autoimmune conditions. Despite its enigmatic role, IgD’s evolutionary conservation underscores its importance in bridging innate and adaptive immunity.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Immunoglobulin D (IgD) at ≤ -80°C.
Applications
Glycoproteomics, ELISA Standards, In Vitro Diagnostic, Hyperimmunoglobulinemia D Syndrome.
Citations/Publications
Hinneburg, H., et al., (2016), 'The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics', J. Am. Soc. Mass Spectrom., 201 (27): pp 507-519. Available at: DOI: 10.1007/s13361-015-1308-6
Whitley, C. S., et al., (2022), 'Monobiotinylated Proteins Tethered to Microspheresfor Detection of Antigen-Specific Serum Antibodies', Journal of Biological Methods, 8(4): pp 1. Available at: https://doi.org/10.14440/jbm.2022.390
Shan, M., et al., (2018), 'Secreted IgD Amplifies Humoral T Helper 2 Cell Responses by Binding Basophils via Galectin-9 and CD44', Immunity 49: pp 709–724. Available at: https://doi.org/10.1016/j.immuni.2018.08.013
Scarrone, M., et al., (2021), 'Development of anti-human IgM nanobodies as universal reagents for general immunodiagnostics', New BIOTECHNOLOGY 64: pp 9–16. Available at: https://doi.org/10.1016/j.nbt.2021.05.002
Shipped with dry ice
Gel Scan of Human Immunoglobulin D (IgD)
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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