PILRA, Recombinant, Human, aa20-196 (FDF03, PILR-alpha, Paired Immunoglobulin-like Type 2 Receptor-alpha)

PILRпїЅalpha (paired immunoglobulinпїЅlike type 2 receptorпїЅalpha; also FDF03) is one of two members that belong to a small family of immunoregulatory IgпїЅsuperfamily receptors (1пїЅ4). It is a counterpart to PILRпїЅbeta, and likely gave rise to the PILRпїЅbeta gene through duplication and rearrangement (1). The PILRs represent one of many pairs of IgпїЅlike domainпїЅcontaining receptors that participate in immune regulation. PILRпїЅalpha and пїЅbeta should not be confused with the similarly named PIRs (also paired immunoglobulinпїЅlike receptors ), or the functionallyпїЅrelated SIRP and ILT/LILR/CD85/LIR family of receptors (2). While PIRs, ILTs and SIRPs contain three to six IgпїЅlike domains in their extracellular region, PILRпїЅalpha and пїЅbeta show only one IgпїЅlike region in their extracellular domain (ECD) (1пїЅ5). Human PILRпїЅalpha is a monomeric, 55kD, 294 amino acid (aa) type I transmembrane (TM) glycoprotein (3пїЅ5). It contains a 178 aa ECD (aa 20пїЅ197), a 21 aa TM segment, and a long, 85 aa cytoplasmic region (aa 219пїЅ303). The ECD shows one VпїЅtype IgпїЅlike domain between aa 32пїЅ150, while the cytoplasmic region contains two ITIMs (immunoreceptor TyrпїЅbased inhibitory motifs) between aa 267пїЅ272 and 296пїЅ301. Given that ITIMs are known to interact with phosphatases such as PTPN6 and PTPN11, the presence of these motifs make mouse PILRпїЅalpha an inhibitory receptor. Three potential isoforms for human PILRпїЅalpha have been reported. The first contains a 24 aa substitution for aa 152пїЅ303, a second possesses a 36 aa substitution for aa 264пїЅ303, and a third shows a deletion of aa 152пїЅ224 (6). The human PILRпїЅalpha ECD shares 43% aa sequence identity with mouse PILRпїЅalpha ECD, and 82% aa sequence identity with the ECD of human PILRпїЅbeta (3, 4).\nPILRпїЅalpha is expressed by neutrophils, macrophages, monocytes, mast cells, APCs, microglia, neurons, cardiac muscle and renal proximal plus pancreatic duct eipthelium (4, 7, 8). It has multiple binding partners, including CD99 (4, 9), glycoprotein B/gB of HSVпїЅ1 (7), PANP (PILRпїЅassociated neural protein) (8) and NPDC1 plus collectinпїЅ12 (10). Although PILRпїЅalpha and пїЅbeta are related through gene duplication and highly similar in their ECD aa sequence, they do not necessarily share the same ligands (or binding partners), as PILRпїЅbeta fails to bind to gB and PANP (8, 10). Notably, PILRпїЅalpha binding appears to be dependent upon the presence of a poorlyпїЅdefined peptide sequence coupled to a sialylated, OпїЅlinked carbohydrate motif (5, 9пїЅ12). It is unclear what function(s) can be attributed to PILRпїЅalpha. One possibility suggests that in the early stage of an immune response, PILRпїЅbeta predominates over PILRпїЅalpha on the APC surface. Ligation of PILRпїЅbeta by CD99 induces ILпїЅ12 production and immune cell activation. But this ligation also upпїЅregulates PILRпїЅalpha expression, and subsequent CD99:PILRпїЅalpha engagement now promotes ILпїЅ27 production, with a concomitant increase in T cell ILпїЅ10 production, and a downпїЅregulation of the inflammatory response (10).\n\nSource:\nRecombinant protein corresponding to aa20-196 from human PILR-alpha, fused to 6-his tag at C-terminal, NS0-derived.\n\nMolecular Weight:\n~33-40kD\n\nEndotoxin:\n<0.10EU/1ug (LAL method)\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute in sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

145827

Size

50ug

Form

Supplied as a lyophilized powder in PBS, EDTA. BSA free. Reconstitute in 100ug/ml PBS.

Purity

~95% (SDS-PAGE)

References

1. Wilson, M.D. et al. (2006) Physiol. Genomics 27:201. 2. Lanier, L.L. (2001) Curr. Opin. Immunol. 13:326. 3. Fournier, N. et al. (2000) J. Immunol. 165:1197. 4. Shiratori, I. et al. (2004) J. Exp. Med. 199:525. 5. Mousseau, D.D. et al. (2000) J. Biol. Chem. 275:4467. 6. SwissProt Accession # Q9UKJ1. 7. Tato, C.M. et al. (2012) PLoS ONE 7:e31680. 8. Satoh, T. et al. (2008) Cell 132:935. 9. Tabata, S. et al. (2008) J. Biol. Chem. 283:8893. 10. Sun, Y. et al. (2012) J. Biol. Chem. 287:15837. 11. Wang, J. et al. (2008) J. Biol. Chem. 180:1686. 12. Arii, J. et al. (2010) J. Virol. 84:10733.