Secretory Iga
16-13-090701
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameSecretory Iga
- Delivery Days Customer9
- Applications SupplierInfection, In Vitro Diagnostics, Autoimmune Diseases
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE. No reaction by IEP with antiserum to human Albumin, IgD, IgE, IgG, IgM and Lactoferrin
- Scientific DescriptionSecretory 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.
- Shelf life instructionmore then 1 year
- SourcePrepared 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 Instruction≤ -20°C
- UNSPSC12352202
References
- Zhang, P., et al., (2020), 'Plasmonic scattering imaging of single proteins and binding kinetics', Nature Methods. 17: pp 1010–1017Read this paper
- Ma, G., et al., (2020), 'Optical imaging of single-protein size, charge, mobility, and binding', Nature Communications 11: pp 4768Read this paper
- Zhang, P., et al., (2022), 'Evanescent scattering imaging of single protein binding kinetics and DNA conformation changes', NATURE COMMUNICATIONS. 13: pp 2298.Read this paper
- 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.Read this paper
- 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.Read this paper