Recombinant Human PGLYRP1/PGRP-S Protein, CF Summary
Details of Functionality
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 human PGLYRP1/PGRP-S protein Gln22-Pro196, with a C-terminal 6-His tag
>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
23-27 kDa, reducing conditions
Publications
Read Publications using 2590-PGB in the following applications:
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.
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 Human PGLYRP1/PGRP-S 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
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.
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