Recombinant Human PGLYRP1/PGRP-S Protein Summary
Product Specifications
Gln22-Pro196, with a C-terminal 6-His tag
Analysis
Product Datasheets
2590-PG/CF (carrier free)
Discontinued Product
2590-PG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: PGLYRP1/PGRP-S
The human PGRP family is comprised of four peptidoglycan recognition proteins that may function as innate immunity pattern recognition molecules (1, 2). Termed PGRP-L, PGRP-I alpha, PGRP-I beta and PGRP-S, they are all products of separate genes, and all are named for the relative length of their translated product (3). PGRP-L (for long) is 576 amino acids (aa) in length, while PGRP-I alpha and I beta are (I) intermediate in length at 341 aa and 373 aa, respectively, and PGRP-S is the shortest at 196 aa in length (3, 4). All human PGRPs bind peptidoglycan and Gram-positive bacteria, and all have at least three C-terminal PGRP domains at variable sites that are highly conserved from insects to mammals (3). Human PGRP-S, the first described member of the family, is a 28 kDa secreted glycoprotein associated with neutrophils (4). The mature molecule is 175 aa in length and contains three variably-sized peptide-carbohydrate recognition sequences of 15 aa, 29 aa and 49 aa, respectively. Human PGRP-S is 72%, 71% and 70% aa identical to mouse, bovine and rat mature PGRP-S, respectively. Studies with PGRP-S deficient mice indicate that knock-out mice have increased susceptibility to infections with non-pathogenic bacteria. Neutrophils from knock-out mice exhibit normal phagocytosis of bacteria but are defective in intracellular killing and digestion of nonpathogenic bacteria (5). The longer three PGRP members are all membrane-bound molecules that contain two membrane-spanning segments. Both the N- and C-termini are depicted as being extracellular with a joining cytoplasmic domain. All three transmembrane forms show at least one PGRP domain on the C-terminal extracellular region; other PGRP domains are variably distributed over their two extracellular and one cytoplasmic region (3).
- Girardin, S.E. and D.J. Philpott (2004) Eur. J. Immunol. 34:1777.
- Steiner, H. (2004) Immunol. Rev. 198:83.
- Liu, C. et al. (2001) J. Biol. Chem. 276:34686.
- Kang, D. et al. (1998) Proc. Natl. Acad. Sci. USA 95:10078.
- Dziarski, R. et al. (2003) Blood 102:689.
Citations for Recombinant Human PGLYRP1/PGRP-S Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 2
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A human secretome library screen reveals a role for Peptidoglycan Recognition Protein 1 in Lyme borreliosis
Authors: A Gupta, G Arora, CE Rosen, Z Kloos, Y Cao, J Cerny, A Sajid, D Hoornstra, M Golovchenk, N Rudenko, U Munderloh, JW Hovius, CJ Booth, C Jacobs-Wag, NW Palm, AM Ring, E Fikrig
PLoS Pathog, 2020-11-11;16(11):e1009030.
Species: Borrelia burgdorferi (Lyme Disease)
Sample Types: Cell Lysates
Applications: ICC -
Cutting Edge: identification of neutrophil PGLYRP1 as a ligand for TREM-1.
Authors: Read C, Kuijper J, Hjorth S, Heipel M, Tang X, Fleetwood A, Dantzler J, Grell S, Kastrup J, Wang C, Brandt C, Hansen A, Wagtmann N, Xu W, Stennicke V
J Immunol, 2015-01-16;194(4):1417-21.
Species: Human
Sample Types:
Applications: Surface Plasmon Resonance
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