• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie? Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When peptidoglycan is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Human PGLYRP1/PGRP-S that produces 50% optimal binding response is 0.75-4.5 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived Gln22-Pro196, with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  No results obtained. Gln22 predicted

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  20 kDa

• SDS-PAGE

  23-27 kDa, reducing conditions

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).

• References:

1. Girardin, S.E. and D.J. Philpott (2004) Eur. J. Immunol. 34:1777.

2. Steiner, H. (2004) Immunol. Rev. 198:83.

3. Liu, C. et al. (2001) J. Biol. Chem. 276:34686.

4. Kang, D. et al. (1998) Proc. Natl. Acad. Sci. USA 95:10078.

5. Dziarski, R. et al. (2003) Blood 102:689.

• Long Name:

  Peptidoglycan Recognition Protein Short/Peptidoglycan Recognition Protein 1

• Entrez Gene IDs:

  8993 (Human); 21946 (Mouse)

• Alternate Names:

  peptidoglycan recognition protein 1; Peptidoglycan recognition protein short; PGLYRP; PGLYRP1; PGRPpeptidoglycan recognition protein; PGRPS; PGRP-S; PGRP-SMGC126894; PGRPSMGC126896; TAG7; TNF superfamily, member 3 (LTB)-like (peptidoglycan recognition protein); TNFSF3L