PGLYRP1 Human
Description
Product Specs
Product Science Overview
PGLYRP1 was independently discovered by two laboratories in 1998. Håkan Steiner and his team identified and cloned Peptidoglycan Recognition Protein (PGRP) in a moth and subsequently discovered mouse and human orthologs. Sergei Kiselev and his team also discovered and cloned a protein from a mouse adenocarcinoma with the same sequence as mouse PGRP, which they named Tag7 .
The human recombinant form of PGLYRP1 is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 185 amino acids, including a 10 amino acid N-terminal His tag. The total molecular mass is approximately 20.68 kDa .
PGLYRP1 is an innate immunity protein that performs several important functions in antimicrobial and antitumor defense systems. It acts as a pattern recognition receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria, providing bactericidal activity . Additionally, PGLYRP1 forms an equimolar complex with heat shock protein HSPA1A, inducing programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane .
Moreover, PGLYRP1, in complex with the Ca²⁺-binding protein S100A4, acts as a chemoattractant that induces lymphocyte movement. This complex serves as a ligand for the chemotactic receptors CCR5 and CXCR3, which are present on immune system cells .
PGLYRP1 is involved in various biological processes, including:
- Peptidoglycan catabolic process
- Negative regulation of natural killer cell differentiation
- Negative regulation of interferon-gamma production
- Innate immune response
- Defense response to bacterium
- Detection of bacterium
- Pattern recognition receptor signaling pathway
- Antimicrobial humoral response
- Neutrophil degranulation
- Positive regulation of cytolysis in other organisms
