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Human PIGR Protein (365 Ser/Gly, His Tag)

FLJ22667,MGC125361,MGC125362,PIGR

Catalog Number P10131-H08H
Organism Species Human
Host Human Cells
Synonyms FLJ22667,MGC125361,MGC125362,PIGR
Molecular Weight The soluble form of recombinant human PIGR consists of 630 amino acids after removal of the signal peptide and has a predicted molecular mass of 69 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 80-90 kDa due to glycosylation.
predicted N Lys 19
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the extracellular domain (Met 1-Arg 638, 365 Ser/Gly) of human PIGR (NP_002635.2) was expressed with a C-terminal polyhistidine tag.
Bio-activity Measured by its binding ability in a functional ELISA .
1. Immobilized rhhuman IgM at 2 μg/ml (100 μl/well) can bind biotinylated PIGR with a linear range of 0.94-15 ng/ml.
2. When human human IgM is immobilized at 2 μg/ml (100 μl/well), PIGR inhibits 50% binding of biotinylated PIGR (0.062 μg/ml) at the concentration range of 0.03-20 μg/ml.
Research Area
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Polymeric immunoglobulin receptor, also known as PIGR, is a member of the immunoglobulin superfamily and a Fc receptor. The ectodomain of this receptor consists of five units with homology to the variable units of immunoglobulins and a transmembrane region, which also has some homology to certain immunoglobulin variable regions. PIGR is expressed on several glandular epithelia including those of liver and breast. The deduced amino-acid sequence has a length of 764 residues and shows an overall similarity of 56% and 64% with the rabbit and rat counterpart. PIGR mediates transcellular transport of polymeric immunoglobulin molecules, and thus facilitates the secretion of IgA and IgM. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment of PIGR.
Reference
  • Coyne, R. S. et al., 1995, J. Biol. Chem. 269 (50) :31620-31625. 
  • Kaetzel,C.S., 2001,  Curr Biol. 11(1): R35-38.