Treml1 Antibodies

Trem-like transcript 1 protein (Treml1)

Cell surface receptor that may play a role in the innate and adaptive immune response. .

Gene Information

Mouse
Gene Name:	Treml1
Uniprot:	Q8K558
Entrez:	71326

Family

Belongs to:
No superfamily

Alternative Names

dJ238O23.3; GLTL1825; PRO3438; TLT1; TLT-1; TLT1MGC119173; TREML1; trem-like transcript 1 protein; triggering receptor expressed on myeloid cells-like 1; Triggering receptor expressed on myeloid cells-like protein 1

Molecular Weight

Mass (kDA):
33.522 kDA

Genomic Context

Mouse
Location:	17|17 C
Sequence:	17;

Tissue Specificity

Highly expressed in bone marrow leukocytes, splenic megakaryocytes and platelets. Detected in brain, liver and in peritoneal monocytes.

Diseases

• Inflammation
• Systemic Infection
• Inflammatory Response
• Hemorrhage
• Gout
• Gout Acute
• Maple Syrup Urine Disease
• Coinfection
• Septic Shock
• Vascular System Injuries
• Bacteroides Fragilis Infection In Conditions Classified Elsewhere And Of Unspecified Site

• Gray Platelet Syndrome
• Innate Immune Response
• Thrombosis
• Disseminated Intravascular Coagulation
• Salmonella Infections
• Platelet Storage Pool Deficiency

Pathways

• Coagulation
• Hemostasis
• Platelet Aggregation
• Inflammatory Response
• Platelet Activation
• Leukocyte Activation
• Osteoclast Differentiation
• Cell Activation

• Cytokine Production
• Immune Response
• Cell Maturation

PTMs

• Phosphorylation

• Cleavage

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/Treml1

Best Uses of the TREML1 Marker

The TREML1 marker is a decoy receptor type 1 splice variant single Ig domain orphan receptor. It is in contact with SHP-1, SHP-2. In addition to these biological functions it also functions as a TREML1 gene is a vital biomarker that can be used to identify human cancer. This article explores how TREML1 Marker could be utilized by scientists.

TREML1 Marker acts as a decoy receptor

Researchers from Columbia University, the National Institutes of Health, and the California Institute of Technology have identified a putative ligand for the TREML1 marker. These ligands can be identified in GRAM positive and GRAM-negative bacteria's surface anionic residues. These ligands have diverse expression patterns and co-regulatory mechanisms. They are believed to play a role in the pathophysiology and progression of Alzheimer's disease.

It is a splice variation

TLT-1, the splice variant of TREMl1, encodes 199 amino acid. The full-length variant is 20 kD shorter than the short variant. In human studies it was found that higher TREML1 levels are associated with a lower risk of AD. In turn, higher levels TREML1 may be protective against AD.

Splicing can take place in one direction, or both. In the first scenario, the splicing process produces multiple mature mRNAs that are derived from one gene. The spliceosome detects a consensus sequence of RNA that mediates the first. The second is caused by a protein known as U1snRNP that binds the 5' splice site and U2AF65, which binds the poly-pyrimidine tract.

It is a type 1 Ig domain receptor that is an orphan receptor

Sandwich ELISA technology is used to create the Mouse TREML1 ELISA kit. The ELISA kit comes with a monoclonal antibody from rat specific to TREML1 as well as a biotinylated detect protein antibody and an HRP substrate. The TREML1 combination protein contains amino acids from human TREML1.

Researchers employed a PCR-based approach to create an overlapping BAC/PAC clone on chromosome 6, in order to determine TREML1 proteins in human cells. These clones contained TLT1 and three other full Ig superfamily genes. The TLT1 gene was identified through an PCR-based analysis of monocyte cell line mRNA. TLT1 was identified using an estimated molecular mass of 33 kD. TLT1 is characterized by a lack of charged residues in the cytoplasmic region and contains two tyrosine residues (Tyr-prolyl-resulfonine) in ITIM. Allcock et al. Also, they have cloned an alternative of TLT1 that did not contain exon 5 through splice.

Low ADP and collagen concentrations were proven to increase platelet aggregation when using the rsTLT-1 antibody. The peptide from residues 94-110 of TLT-1 was found to be specific, since it increased the aggregation rate only when bound to platelet membranes. A 17-mer peptide did not affect rsTLT-1-enhanced aggregateion.

The Fusion of the extracellular domain with the Fc domain of human IgG has been proven to increase platelet aggregation in vitro. When stimulated by TLT-1 that is soluble, it was found to correlate with the presence disseminated intravascularcoagulation. TLT-1 also binds to fibrinogen and increases platelet aggregation. The cytoplasmic domain (TLT-1) is capable of binding to ezrin/radixin/moesin protein family proteins. This suggests that the TLT-1 binding to fibrinogen is linked to the cytoskeleton of platelets. Moreover, mice lacking Treml1 were unable to effectively aggregate, extending tail bleeding times.

It interacts with SHP-1 and SHP-2

The phosphatase activity of SHP-1 is controlled by an interaction between the SH2 domain of the protein and the phosphotyrosine residues of the SIRPa peptide. SHP1 R136Q replaced the critical amino acid arginine in the binding of phosphotyrosine while SHP1 R30Q and have the same basal activities and continue to exhibit catalytic activity.

A study has demonstrated that the absence of Shp1 hinders the growth of two immunogenic tumor cell lines in vitro and in vivo while the same mutations are not detrimental to anti-tumor activity of the non-immunogenic B16F10 cell line. The results of immunophenotyping suggest that anti-tumor activity observed is likely to result from multiple immune cells, including macrophages as well as T.

Both TLT1 as well as ITGA2 were found to be involved in platelet function and are likely to play a role in platelet biology. Platelets have receptors that are not present in other plates, these two phosphatases appear to be the main targets of RUNX1.

These studies reveal that TREML1 directly bonds to fibrinogen and aids in the inflammation response. It also blocks calcium signaling pathways. Additionally, TREML1 recruits SHP-1 and SHP-2 for intragenic RUNX1 binding. They also demonstrated that ITGA2 and TREML1 are essential for adhesion of platelets to endothelial cells during homostasis.

Immunotherapy can be achieved through targeting the protein tyrosinephosphatase Shp1. It is widely expressed in the hematopoetic hematopoetic chamber and is an antagonist of immune cells' signaling. Changes in Shp1 alter the immune response to tumors. Shp1 is specifically a receptor for immunoreceptor tyrosine inhibitory motes and dephosphorylates its substrates.

In GFP-high CD41+ cell lines the interaction between TREML1- and SHP-1 was evident. The results presented here demonstrate that phosphorylated TREML1- and SHP-2 increase the phosphorylated SHP-1 calcium signaling in rat basophilic Leukemia cells. These results suggest that TREML1 and SHP-2 play a role in both adaptive and innate immune responses.

We also discovered that RUNX1 and ITGA2 are positively regulated by RUNX1. These results show that TREML1 & ITGA2 are targets of RUNX1. Further research will be required to confirm the role played by these transcription factors. If you have any questions, contact us. We're more than happy to address any questions. The scientific community must continue its work!