Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Human plgR is immobilized at 2 μg/mL (100 μL/well), the concentration of human IgM that produces 50% of the optimal binding response is found to be approximately 20-100 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived human pIgR protein Lys19-Arg638, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Lys19 |
Protein/Peptide Type | Recombinant Proteins |
Gene | PIGR |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 68.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 90-95 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
The human polymeric immunoglobulin receptor (pIgR; also known as membrane secretory component) is a 100 kDa type I transmembrane glycoprotein that is synthesized as a 764 amino acid (aa) precursor. It includes a signal sequence (aa 1-18), an extracellular region (aa 19-638), a transmembrane segment (aa 639-661), and a cytoplasmic domain (aa 662-764) (1-3). The extracellular region consists of five Ig-like domains and a sixth non-Ig domain that connects to the membrane region. pIgR is expressed on secretory epithelial cells of exocrine tissues. Immunoglobulin isotypes consist of two heavy (H) and two light (L) chains. For IgA and IgM, this H2L2 monomer can form larger polymers through association with a joining chain (J chain). The Fc regions of IgA and IgM have a carboxy-terminal extension called a secretory tailpiece that binds the J chain (4). pIgR functions as a carrier that transports IgA and IgM across epithelium (5). On the basolateral surface of epithelial cells, the receptor initially binds non-covalently to IgA via a docking site on the J chain. This initiates a rearrangement in which a disulfide bond forms between pIgR and an IgA heavy chain (2). The complexes are then internalized and transcytosed to the apical surface. A soluble covalent complex called secretory IgA (SIgA) is now generated by proteolytic cleavage of the sixth extracellular domain of pIgR and released into the lumen (6). This IgA-bound and proteolytically generated pIgR fragment is referred to as secretory component (SC). Notably, human pIgR transcytoses constitutively, with or without ligand, creating both bound and free, 78 kDa SC following cleavage (3). The extracellular region of pIgR is 64%, 65% and 70% aa identical to the equivalent region in rat, mouse and porcine, respectively. The receptor component of the complex anchors the SIgA molecule to mucous (7). SIgA is a crucial component of the mucosal immune system serving to protect the large expanse of mucous membranes that form a barrier between the interior of the body and the external environment (8).
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