Recombinant Human PGLYRP1/PGRP-S Protein, CF Summary
Gln22-Pro196, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in MOPS and NaCl.|
|Reconstitution||Reconstitute at 200 μg/mL in 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.
When peptidoglycan is coated at 1 µg/mL, 100 µL/well, Recombinant Human PGLYRP1/PGRP-S binds with an ED50 of 0.75-4.5 ng/mL.
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.
Citation for Recombinant Human PGLYRP1/PGRP-S Protein, CF
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.
1 Citation: Showing 1 - 1
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;194(4):1417-21.
Applications: Surface Plasmon Resonance
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