Recombinant Mouse PGLYRP1/PGRP-S His-tag Protein, CF

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When Peptidoglycan is immobilized at 5 μg/mL (100 µL/well), Recombinant Mouse PGLYRP1/PGRP-S His-tag Protein (Catalog # 2696-PGB) binds with an ED50 of 0.400‑4.80 ng/mL.
2 μg/lane of Recombinant Mouse PGLYRP1/PGRP-S His-tag Protein (Catalog # 2696-PGB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse PGLYRP1/PGRP-S His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Peptidoglycan is immobilized at 5 μg/mL (100 µL/well), Recombinant Mouse PGLYRP1/PGRP-S His-tag (Catalog # 2696-PGB) binds with an ED50 of 0.400-4.80 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse PGLYRP1/PGRP-S protein
Cys17-Glu182, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Cys17
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
20 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
18-21 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS and NaCl with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse PGLYRP1/PGRP-S His-tag Protein, CF

  • 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

Background

The mouse PGRP family comprises 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 530 amino acids (aa) in length, while PGRP-I alpha and I beta are intermediate (I) in length at 347 aa and 374 aa, respectively, and PGRP-S is shortest at 182 aa in length (3, 4). All mouse 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). Mouse PGRP-S, the first described member of the family, is an 18 kDa secreted protein associated with neutrophils (4, 5). The mature molecule is 166 aa in length and presumably contains three variably-sized peptide-carbohydrate recognition sequences. Mouse PGRP-S is 86%, 69% and 72% aa identical to rat, bovine and human mature PGRP‑S, respectively. Studies with PGRP-S deficient mice indicate that knock-out mice have increased susceptibility to infections with low (but not high) pathogenicity bacteria. Neutrophils from knock-out mice exhibit normal phagocytosis of bacteria but are defective in intracellular killing and digestion of nonpathogenic bacteria (5). The three longer 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).

  1. Girardin, S.E. and D.J. Philpott (2004) Eur. J. Immunol. 34:1777.
  2. Steiner, H. (2004) Immunol. Rev. 198:83.
  3. Kiselev, S.L. et al. (1998) J. Biol. Chem. 273:18633.
  4. Kang, D. et al. (1998) Proc. Natl. Acad. Sci. USA 95:10078.
  5. Dziarski, R. et al. (2003) Blood 102:689.

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