TREM1 Human

Triggering Receptor Expressed on Myeloid Cells 1 Human Recombinant
Cat. No.
BT18346
Source
Escherichia Coli.
Synonyms
Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

TREM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (21-205 a.a.) and having a molecular mass of 23.3kDa.
TREM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
TREM1, or Triggering Receptor Expressed on Myeloid cells 1, is a cell surface receptor primarily found on neutrophils, monocytes, and macrophages. It plays a crucial role in the immune response by amplifying inflammatory signals triggered by bacterial and fungal infections. Upon activation, TREM1 initiates a cascade of events leading to the release of pro-inflammatory molecules, contributing to the body's defense mechanisms against pathogens. However, excessive TREM1 activation can lead to harmful inflammation and is implicated in conditions like sepsis. The soluble form of TREM1 serves as a potential biomarker for sepsis severity. TREM1 expression patterns show elevated levels in areas of acute inflammation, adult tissues like the liver, lung, and spleen, and peripheral blood leukocytes. Notably, its expression is lower in fetal tissues, bone marrow, and malignant cells.
Description
This product consists of the recombinant human TREM1 protein, produced in E. coli. It is engineered as a single, non-glycosylated polypeptide chain encompassing amino acids 21 to 205 of the TREM1 sequence. A 24 amino acid His-tag is attached to the N-terminus to facilitate purification. The protein has a molecular weight of 23.3 kDa and is purified using proprietary chromatographic methods to ensure high purity.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The TREM1 protein is supplied in a solution at a concentration of 0.5 mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0 and contains 0.15M NaCl, 30% glycerol, and 1mM DTT to maintain stability.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To ensure long-term stability, adding a carrier protein like HSA or BSA to a final concentration of 0.1% is advised. Repeated freezing and thawing should be avoided.
Purity
The purity of the TREM1 protein is greater than 85%, as determined by SDS-PAGE analysis.
Synonyms
Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMATKLTE EKYELKEGQT LDVKCDYTLE KFASSQKAWQ IIRDGEMPKT LACTERPSKN SHPVQVGRII LEDYHDHGLL RVRMVNLQVE DSGLYQCVIY QPPKEPHMLF DRIRLVVTKG FSGTPGSNEN STQNVYKIPP TTTKALCPLY TSPRTVTQAP PKSTADVSTP DSEINLTNVT DIIRVPVFN.

Product Science Overview

Structure and Expression

TREM-1 is a transmembrane protein that is constitutively expressed on the surface of peripheral blood monocytes and neutrophils . It is also found on other cell types such as hepatic endothelial cells and gastric epithelial cells, particularly during inflammatory processes . The receptor is upregulated upon stimulation with microbial products and works synergistically with other pattern recognition receptors like Toll-like receptors (TLRs), especially TLR4 .

Function and Mechanism

Upon activation, TREM-1 amplifies the immune response by triggering the production and release of proinflammatory cytokines and chemokines . This activation leads to a cascade of immune responses, including the respiratory burst, phagocytosis, and the release of interleukin-8 (IL-8) and myeloperoxidase . The receptor’s activation is crucial for the successful antimicrobial response and the resolution of inflammation .

Clinical Significance

TREM-1 has garnered significant attention for its role in sepsis, a condition characterized by a dysregulated immune response that can lead to organ failure and death . Elevated levels of the soluble form of TREM-1 (sTREM-1) have been observed in patients with sepsis and septic shock, making it a potential biomarker for these conditions . The receptor’s role in sepsis has led to the development of TREM-1 inhibitors, such as nangibotide, which have shown promising results in clinical trials .

Research and Therapeutic Potential

Since its discovery, TREM-1 has been the subject of numerous studies aimed at understanding its role in the immune response and its potential as a therapeutic target . Animal models have demonstrated that blocking TREM-1 can protect against lethal endotoxic shock and microbial sepsis . Clinical trials are ongoing to evaluate the efficacy of TREM-1 inhibitors in treating sepsis and other inflammatory diseases .

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Source
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