Human Secretory IgA (sIgA)
Native dimeric whole molecule including the J chain and secretory component
Produktdetails
Synonyms
SIgA
Description of Human Secretory IgA (sIgA)
Human Secretory IgA (sIgA) is a 385 kDa protein. Secretory Immunoglobulin A (SIgA) is the predominant antibody found on mucosal surfaces, including the gastrointestinal, respiratory, and genitourinary tracts, as well as in secretions such as saliva, tears, and colostrum. Structurally, SIgA is a polypeptide complex composed of two IgA monomers, a joining (J) chain, and a secretory component, which protects it from enzymatic degradation and enables it to function in harsh environments like the gut. SIgA serves as the first line of immune defense by binding to pathogens and toxins, preventing their attachment and invasion of epithelial cells, a process known as immune exclusion. It also helps maintain mucosal barrier integrity and regulates the composition of the microbiota by interacting with commensal bacteria. Functionally, SIgA neutralizes viruses, bacteria, and other antigens without triggering strong inflammatory responses, thereby promoting immune tolerance and mucosal homeostasis. Clinically, altered SIgA levels are associated with increased susceptibility to infections, autoimmune diseases, and inflammatory conditions of the mucosa, making it a valuable marker for mucosal immune status and gut health.
Source
Prepared from human colostrum shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
Storage
For long term, store Human Secretory IgA (sIgA) at ≤ -20°C.
Applications
Infection, In Vitro Diagnostics, Autoimmune Diseases.
Citations/Publications
Zhang, P., et al., (2020), 'Plasmonic scattering imaging of single proteins and binding kinetics', Nature Methods. 17: pp 1010–1017. Available at: https://doi.org/10.1038/s41592-020-0947-0
Ma, G., et al., (2020), 'Optical imaging of single-protein size, charge, mobility, and binding', Nature Communications 11: pp 4768. Available at: https://doi.org/10.1038/s41467-020-18547-w
Zhang, P., et al., (2022), 'Evanescent scattering imaging of single protein binding kinetics and DNA conformation changes', NATURE COMMUNICATIONS. 13: pp 2298. Available at: https://doi.org/10.1038/s41467-022-30046-8
Ma, G., et al., (2022), 'Label-Free Single-Molecule Pulldown for the Detection of Released Cellular Protein Complexes', ACS Central Science 8(9): pp 1272-1281. Available at: https://doi.org/10.1021/acscentsci.2c00602
Wan, Z., et al., (2022), 'Single-Protein Identification by Simultaneous Size and Charge Imaging Using Evanescent Scattering Microscopy', ACS Sens. 7(9): pp 2625–2633. Available at: https://doi.org/10.1021/acssensors.2c01008
Shipped with ice packs
Gel Scan of Human Secretory IgA (sIgA)
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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Payment Methods
Paying by bank transfer
