- SynonymPIGR,Poly-Ig receptor
- SourceHuman pIgR, His Tag (PIR-H5222) is expressed from human 293 cells (HEK293). It contains AA Lys 19 - Arg 638 (Accession # AAI10495.1).Predicted N-terminus: Lys 19Request for sequence
- Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 68.7 kDa. The protein migrates as 85-95 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>98% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human pIgR, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 98%.
- BackgroundPolymeric immunoglobulin receptor (PIGR) is also known as Poly-Ig receptor, which can becleaved into membrane secretory component (SC). PIGR is a type I transmembrane glycoprotein or a member of the immunoglobulin superfamily, and is synthesized by secretory epithelial cells and delivered to the basolateral plasma membrane where it can bind larger polymers of IgA (pIgA ) and pentameric IgM. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.
- References
- (1)Krajci P., et al., 1991, Hum. Genet. 87:642-648.
- (2)Eiffert H., et al., 1984, Hoppe-Seyler"s Z. Physiol. Chem. 365:1489-1495.
- (3)Hughes G.J., et al., 1997, FEBS Lett. 410:443-446.
- (4)Hamburger A.E., et al., 2004, Structure 12:1925-1935.
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