PGLYRP1 Protein

PGLYRP1 Protein Overview

PGLYRP1 reagents

Innate nonself immune recognition relies on structures common among invading microbes, a process termed pattern recognition. Peptidoglycan is a fundamental component of the bacterial cell wall and is thus a candidate for a pattern recognized by the immune system. Using differential display to identify bacteria-induced genes in the moth Trichoplusia ni, Kang et al. (1998) cloned a cDNA encoding the T. ni peptidoglycan recognition protein (PGRP, or PGLYRP). Recombinant T. ni PGLYRP bound to peptidoglycan and to gram-positive bacteria. By PCR of human and mouse spleen cDNAs, they isolated human and mouse PGLYRP cDNAs, respectively. The deduced human PGLYRP protein has 196 amino acids. Both the human and mouse PGLYRP proteins share 43% sequence identity with the T. ni PGLYRP protein. Recombinant mouse Pglyrp protein expressed in insect cells possessed an affinity for peptidoglycan. Dot blot analysis of a number of human tissue mRNAs detected strong expression in bone marrow and weak expression in lung, kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, and fetal spleen. Liu et al. (2001) cloned PGLYRP, which they called PGRPS, by PCR of a bone marrow cDNA library. The deduced 196-amino acid protein contains an N-terminal signal peptide, followed by the extracellular PGRP domains III, II, and I, which are highly conserved in mammalian and insect PGRPs. PGRPS shares 40%, 43%, and 42% amino acid identity with PGRPL (608199), PGRPI-alpha (PGLYRP3; 608197), and PGRPI-beta (PGLYRP4; 608198). RNA dot blot analysis detected strong PGRPS expression in bone marrow and expression that was 50 to 100 times lower in polymorphonuclear leukocytes and fetal liver. Northern blot analysis detected 1.4-, 0.9-, and 0.5-kb transcripts in bone marrow, a 0.9-kb transcript in fetal liver, and 1.4- and 0.9-kb transcripts in peripheral blood leukocytes. PCR detected low expression of PGRPS in spleen, jejunum, and thymus, possibly due to the presence of polymorphonuclear leukocytes in these tissues. Transiently transfected COS-7 and human embryonic kidney cells expressed PGRPS as a protein with an apparent molecular mass of 24 kD. About half of the expressed PGRPS was detected in the culture medium, and the remainder was a Triton X-100-soluble membrane protein.

PGLYRP1 protein family

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

PGLYRP1 protein name

Recommended name
Peptidoglycan recognition protein 1
Aliases
PGRP, PGRPS, PGRP-S, TAG7
Alternative name
Peptidoglycan recognition protein short

PGLYRP1 Gene family protein

Peptidoglycan recognition proteins
Approved symbol Common name
PGLYRP4 PGLYRP4 protein, recombinant

PGLYRP1 Protein Sequence

Species Human PGLYRP1 protein
Length 196
Mass (Da) 21731
Sequence Human PGLYRP1 protein sequence
Species Mouse PGLYRP1 protein
Length 182
Mass (Da) 20489
Sequence Mouse PGLYRP1 protein sequence
Species Rat PGLYRP1 protein
Length 183
Mass (Da) 20591
Sequence Rat PGLYRP1 protein sequence

PGLYRP1 Protein Molecular Weight & PI

Peptidoglycan recognition protein 1 precursor (Peptidoglycan recognition protein short) (PGRP-S) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 22-196 Peptidoglycan recognition protein 1.

Molecular weight (Da)

19434.95

Theoretical pI

8.23

PGLYRP1 Protein Structure

Crystal structure of human peptidoglycan recognition protein (PGRP-S)
Deposited
2004-12-22   Released:  2005-03-22
Deposition Author(s)
Guan, R., Wang, Q., Sundberg, E.J., Mariuzza, R.A.
Organism(s)
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
1.7000 Å
R-Value Free
0.210
R-Value Work
0.183
1YCK From PDB

Human PGLYRP1 protein Secondary structure

PGLYRP1 Protein Interaction

Recombinant PGLYRP1 Protein Feature

PGLYRP1 Protein, Mouse, Recombinant (His Tag)

High Purity
> 95 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

Bulk Order of Recombinant PGLYRP1 Protein

Please Leave Us a Message if you have any questions regarding bulk price quote of our products on the website, our customer specialist will get back to you in 24 hours by email.

Custom Recombinant Protein Production Service Features

  • Over 10 years' experience for 6000+ recombinant proteins production.
  • One-stop service from gene synthesis and vector construction to protein expression and purification.
  • Multiple protein expression systems: bacterial, yeast, baculovirus-insect and mammalian expression system.
  • Multiple purification systems (30+) to choose.
  • High R & D ability with over 1000 new proteins per year and quick problem-solving ability.
  • Close to 100 bioreactors with various volume between 2-1000 L to guarantee high-throughput and large-scale production.

Custom Recombinant Protein Production Service Advantages

  • High-efficiency expression vectors
  • High cell density culturing
  • Proprietary medium formulation
  • >6000 proteins expression and purification experience
  • High-efficiency expression vectors
  • High cell density culturing

Recombinant Protein Production Service Description

We offer one-stop services for recombinant protein production using our advanced protein expression platform technologies. Our full services include protein gene synthesis, protein codon optimization, protein expression vector design, large scale cell culture and fermentation, protein purification, and protein quality control testing. We offer significant cost saving advantages and record speed in protein expression and bulk production. We also have extensive experiences and expertise in handling various types of recombinant protein purification projects, with or without purification tags.