Name :
Recombinant Human TREM-1 Protein (His & hFc Tag)
Biological Activity :
Background :
TREM1 (trIgGering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain, and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors, TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS, a ligand for TLR4, as well as lipoteichoic acid. Although its natural ligand has not been identified, engagement of TREM1 with agonist mAbs trIgGers secretion of the proinflammatory cytokines TNF-α and IL-1β, as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly, TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1), ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock, blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus, it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges, and is suggested to be a potential therapeutic target for septic shock.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_061113.1
NCBI Gene ID :
Synonyms :
Synonyms :
trIgGering receptor expressed on myeloid cells 1
Amino Acid Sequence :
Molecular Weight :
The recombinant human TREM1/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer consists of 428 amino acids and has a predicted molecular mass of 48.3 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhTREM1/Fc monomer is approximately 60-65 kDa due to glycosylation.
Purity :
> 95 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the extracellular domain (Met 1-Arg 200) of human TREM1 (NP_061113.1) precursor was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
CD354 Protein, Human; TREM-1 Protein, Human TREM-1 背景信息 TREM1 (trIgGering receptor expressed on myeloid cells) is a type I transmembrane protein with a single Ig-like domain, and is selectively expressed on blood neutrophils and a subset of monocytes. As a member of the growing family of receptors related to NK cell receptors, TREM1 activates downstream signaling events with the help of an adapter protein called DAP12. Expression of TREM1 is up-regulated by bacterial LPS, a ligand for TLR4, as well as lipoteichoic acid. Although its natural ligand has not been identified, engagement of TREM1 with agonist mAbs trIgGers secretion of the proinflammatory cytokines TNF-α and IL-1β, as well as chemokines such as IL-8 and monocyte chemoattractant protein (MCP)-1. Intracellularly, TREM1 induces Ca2+ mobilization and tyrosine phosphorylation of extracellular signal-related kinase 1 (ERK1), ERK2 and phospholipase C-γ. In an animal model of LPS-induced septic shock, blockade of TREM1 signaling inhibited hyperresponsiveness and death. Thus, it has been demonstrated that TREM1 performs a critical function in immune responses involved in host defense against microbial challenges, and is suggested to be a potential therapeutic target for septic shock.
References & Citations :
Bouchon, A. et al., 2000, J. Immunol. 164: 4991-4995. Bouchon, A. et al., 2001, Nature. 410: 1103-1107. Bleharski, J.R. et al., 2003, J. Immunol. 170: 3812-3818.
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